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pymol-open-source/testing/data/1rx1.pdb
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HEADER OXIDOREDUCTASE 19-SEP-96 1RX1
TITLE DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH
TITLE 2 NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE (REDUCED FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHFR;
COMPND 5 EC: 1.5.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: RT500;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PRWA-1
KEYWDS OXIDOREDUCTASE, NADP, TRIMETHOPRIM RESISTANCE, METHOTREXATE
KEYWDS 2 RESISTANCE, ONE-CARBON METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.SAWAYA
REVDAT 2 24-FEB-09 1RX1 1 VERSN
REVDAT 1 11-JAN-97 1RX1 0
JRNL AUTH M.R.SAWAYA,J.KRAUT
JRNL TITL LOOP AND SUBDOMAIN MOVEMENTS IN THE MECHANISM OF
JRNL TITL 2 ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE:
JRNL TITL 3 CRYSTALLOGRAPHIC EVIDENCE.
JRNL REF BIOCHEMISTRY V. 36 586 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9012674
JRNL DOI 10.1021/BI962337C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH V.M.REYES,M.R.SAWAYA,K.A.BROWN,J.KRAUT
REMARK 1 TITL ISOMORPHOUS CRYSTAL STRUCTURES OF ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE COMPLEXED WITH FOLATE,
REMARK 1 TITL 3 5-DEAZAFOLATE, AND 5,10-DIDEAZATETRAHYDROFOLATE:
REMARK 1 TITL 4 MECHANISTIC IMPLICATIONS
REMARK 1 REF BIOCHEMISTRY V. 34 2710 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.BYSTROFF,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED
REMARK 1 TITL 3 CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING
REMARK 1 REF BIOCHEMISTRY V. 30 2227 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.BYSTROFF,S.J.OATLEY,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE: THE NADP+ HOLOENZYME AND
REMARK 1 TITL 3 THE FOLATE.NADP+ TERNARY COMPLEX. SUBSTRATE
REMARK 1 TITL 4 BINDING AND A MODEL FOR THE TRANSITION STATE
REMARK 1 REF BIOCHEMISTRY V. 29 3263 1990
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT V. 5-D
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 11692
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1800
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 118
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.019 ; 0.020 ; 1354
REMARK 3 BOND ANGLES (DEGREES) : 3.000 ; 3.000 ; 1841
REMARK 3 TORSION ANGLES (DEGREES) : 24.200; NULL ; 769
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.019 ; 0.020 ; 37
REMARK 3 GENERAL PLANES (A) : 0.007 ; 0.020 ; 189
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 5.700 ; NULL ; 1354
REMARK 3 NON-BONDED CONTACTS (A) : 0.022 ; 0.100 ; 36
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : MOEWS AND KRETSINGER
REMARK 3 KSOL : 0.94
REMARK 3 BSOL : 295.90
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : TNT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RX1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-96
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : XUONG-HAMLIN MULTIWIRE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : UCSD
REMARK 200 DATA SCALING SOFTWARE : UCSD
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11692
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18700
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: DHFR-FOLATE-NADP COMPLEX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 17.22750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.35050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.68500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.35050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.22750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.68500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 17 CD GLU A 17 OE2 0.068
REMARK 500 GLU A 48 CD GLU A 48 OE2 0.071
REMARK 500 GLU A 118 CD GLU A 118 OE1 0.080
REMARK 500 GLU A 129 CD GLU A 129 OE2 0.085
REMARK 500 GLU A 154 CD GLU A 154 OE1 0.070
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 LEU A 24 CB - CG - CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 ASP A 27 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 27 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 37 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 71 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 79 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 87 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 87 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 VAL A 88 CA - CB - CG1 ANGL. DEV. = -10.7 DEGREES
REMARK 500 LYS A 109 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASP A 122 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 132 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 132 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 142 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 144 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 24 78.18 -117.38
REMARK 500 ASP A 87 40.52 -95.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 300 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 391 O
REMARK 620 2 ARG A 159 OXT 98.7
REMARK 620 3 HOH A 390 O 71.7 89.1
REMARK 620 4 HOH A 310 O 73.7 80.9 142.0
REMARK 620 5 HOH A 370 O 83.7 176.5 94.2 97.4
REMARK 620 6 HIS A 149 ND1 137.2 82.9 65.5 147.2 97.1
REMARK 620 7 ASP A 116 O 148.0 87.4 140.1 76.4 89.2 74.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 300
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 164
DBREF 1RX1 A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
SEQADV 1RX1 ASP A 37 UNP P0ABQ4 ASN 37 CONFLICT
SEQRES 1 A 159 MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL
SEQRES 2 A 159 ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA
SEQRES 3 A 159 ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO
SEQRES 4 A 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG
SEQRES 5 A 159 PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN
SEQRES 6 A 159 PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL
SEQRES 7 A 159 ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE
SEQRES 8 A 159 MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU
SEQRES 9 A 159 PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA
SEQRES 10 A 159 GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO
SEQRES 11 A 159 ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA
SEQRES 12 A 159 ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU
SEQRES 13 A 159 GLU ARG ARG
HET CA A 300 1
HET NAP A 164 48
HETNAM CA CALCIUM ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 CA CA 2+
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 HOH *118(H2 O)
HELIX 1 2 PRO A 25 THR A 35 1 11
HELIX 2 3 ARG A 44 ILE A 50 1 7
HELIX 3 4 VAL A 78 CYS A 85 1 8
HELIX 4 5 GLY A 97 LYS A 106 1 10
SHEET 1 8 8 TRP A 133 SER A 135 0
SHEET 2 8 8 TYR A 151 ARG A 158 -1 N GLU A 157 O GLU A 134
SHEET 3 8 8 ALA A 107 ILE A 115 -1 N HIS A 114 O CYS A 152
SHEET 4 8 8 ILE A 2 ILE A 5 1 N ILE A 2 O GLN A 108
SHEET 5 8 8 ILE A 91 GLY A 95 1 N ILE A 91 O SER A 3
SHEET 6 8 8 PRO A 39 GLY A 43 1 N PRO A 39 O MET A 92
SHEET 7 8 8 LYS A 58 LEU A 62 1 N LYS A 58 O VAL A 40
SHEET 8 8 8 THR A 73 VAL A 75 1 N THR A 73 O ILE A 61
LINK CA CA A 300 O HOH A 391 1555 1555 2.36
LINK CA CA A 300 OXT ARG A 159 1555 1555 2.49
LINK CA CA A 300 O HOH A 390 1555 1555 2.22
LINK CA CA A 300 O HOH A 310 1555 3645 2.59
LINK CA CA A 300 O HOH A 370 1555 1455 2.42
LINK CA CA A 300 ND1 HIS A 149 1555 1455 2.61
LINK CA CA A 300 O ASP A 116 1555 1455 2.30
CISPEP 1 GLY A 95 GLY A 96 0 0.50
SITE 1 AC1 7 ASP A 116 HIS A 149 ARG A 159 HOH A 310
SITE 2 AC1 7 HOH A 370 HOH A 390 HOH A 391
SITE 1 AC2 28 ALA A 6 ALA A 7 ILE A 14 GLY A 15
SITE 2 AC2 28 MET A 16 ASN A 18 ALA A 19 MET A 20
SITE 3 AC2 28 GLY A 43 ARG A 44 HIS A 45 THR A 46
SITE 4 AC2 28 LEU A 62 SER A 63 SER A 64 LYS A 76
SITE 5 AC2 28 ILE A 94 GLY A 95 GLY A 96 GLY A 97
SITE 6 AC2 28 ARG A 98 VAL A 99 TYR A 100 GLN A 102
SITE 7 AC2 28 ASP A 131 HOH A 362 HOH A 415 HOH A 439
CRYST1 34.455 45.370 98.701 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.029023 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022041 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010132 0.00000
ATOM 1 N MET A 1 12.284 42.763 10.037 1.00 15.67 N
ATOM 2 CA MET A 1 13.039 42.249 11.169 1.00 22.34 C
ATOM 3 C MET A 1 14.463 42.676 11.106 1.00 13.33 C
ATOM 4 O MET A 1 15.086 42.541 10.088 1.00 20.18 O
ATOM 5 CB MET A 1 12.961 40.710 11.174 1.00 30.79 C
ATOM 6 CG MET A 1 13.589 39.989 12.350 1.00 41.28 C
ATOM 7 SD MET A 1 14.460 38.553 11.659 1.00 53.22 S
ATOM 8 CE MET A 1 15.212 39.482 10.276 1.00 55.67 C
ATOM 9 N ILE A 2 14.934 43.154 12.235 1.00 7.74 N
ATOM 10 CA ILE A 2 16.279 43.629 12.431 1.00 3.94 C
ATOM 11 C ILE A 2 17.215 42.663 13.112 1.00 5.88 C
ATOM 12 O ILE A 2 16.919 42.055 14.135 1.00 13.77 O
ATOM 13 CB ILE A 2 16.045 44.814 13.291 1.00 10.15 C
ATOM 14 CG1 ILE A 2 15.063 45.663 12.445 1.00 11.60 C
ATOM 15 CG2 ILE A 2 17.386 45.409 13.669 1.00 11.43 C
ATOM 16 CD1 ILE A 2 14.818 47.031 12.981 1.00 7.91 C
ATOM 17 N SER A 3 18.365 42.511 12.557 1.00 3.33 N
ATOM 18 CA SER A 3 19.321 41.611 13.121 1.00 3.18 C
ATOM 19 C SER A 3 20.601 42.344 13.326 1.00 10.13 C
ATOM 20 O SER A 3 20.868 43.266 12.577 1.00 12.19 O
ATOM 21 CB SER A 3 19.593 40.527 12.100 1.00 9.07 C
ATOM 22 OG SER A 3 18.371 39.800 11.817 1.00 10.34 O
ATOM 23 N LEU A 4 21.384 41.927 14.310 1.00 1.00 N
ATOM 24 CA LEU A 4 22.620 42.562 14.547 1.00 2.30 C
ATOM 25 C LEU A 4 23.659 41.568 14.268 1.00 4.79 C
ATOM 26 O LEU A 4 23.440 40.439 14.667 1.00 8.76 O
ATOM 27 CB LEU A 4 22.780 42.878 16.073 1.00 12.49 C
ATOM 28 CG LEU A 4 22.325 44.320 16.444 1.00 17.75 C
ATOM 29 CD1 LEU A 4 20.873 44.585 16.065 1.00 9.38 C
ATOM 30 CD2 LEU A 4 22.473 44.550 17.928 1.00 14.85 C
ATOM 31 N ILE A 5 24.784 41.969 13.625 1.00 4.33 N
ATOM 32 CA ILE A 5 25.853 41.009 13.393 1.00 4.93 C
ATOM 33 C ILE A 5 27.126 41.640 13.937 1.00 8.97 C
ATOM 34 O ILE A 5 27.444 42.774 13.583 1.00 9.74 O
ATOM 35 CB ILE A 5 25.979 40.599 11.897 1.00 7.63 C
ATOM 36 CG1 ILE A 5 27.110 39.590 11.657 1.00 12.19 C
ATOM 37 CG2 ILE A 5 26.174 41.845 11.032 1.00 8.98 C
ATOM 38 CD1 ILE A 5 26.878 38.690 10.419 1.00 7.23 C
ATOM 39 N ALA A 6 27.886 40.915 14.792 1.00 3.37 N
ATOM 40 CA ALA A 6 29.117 41.458 15.324 1.00 4.27 C
ATOM 41 C ALA A 6 30.070 40.376 15.726 1.00 1.88 C
ATOM 42 O ALA A 6 29.623 39.265 15.961 1.00 8.48 O
ATOM 43 CB ALA A 6 28.803 42.307 16.576 1.00 3.35 C
ATOM 44 N ALA A 7 31.364 40.684 15.833 1.00 3.64 N
ATOM 45 CA ALA A 7 32.383 39.712 16.259 1.00 7.31 C
ATOM 46 C ALA A 7 32.862 40.250 17.623 1.00 15.49 C
ATOM 47 O ALA A 7 33.201 41.440 17.726 1.00 10.20 O
ATOM 48 CB ALA A 7 33.562 39.617 15.319 1.00 5.57 C
ATOM 49 N LEU A 8 32.887 39.410 18.647 1.00 8.92 N
ATOM 50 CA LEU A 8 33.301 39.821 19.965 1.00 6.06 C
ATOM 51 C LEU A 8 34.442 39.026 20.538 1.00 6.67 C
ATOM 52 O LEU A 8 34.433 37.839 20.477 1.00 13.09 O
ATOM 53 CB LEU A 8 32.146 39.481 20.975 1.00 7.60 C
ATOM 54 CG LEU A 8 31.013 40.485 21.227 1.00 12.74 C
ATOM 55 CD1 LEU A 8 30.316 40.869 19.947 1.00 21.39 C
ATOM 56 CD2 LEU A 8 29.999 39.811 22.138 1.00 7.33 C
ATOM 57 N ALA A 9 35.392 39.702 21.152 1.00 9.04 N
ATOM 58 CA ALA A 9 36.479 39.075 21.790 1.00 6.26 C
ATOM 59 C ALA A 9 36.122 39.003 23.280 1.00 15.47 C
ATOM 60 O ALA A 9 35.006 39.255 23.726 1.00 9.66 O
ATOM 61 CB ALA A 9 37.749 39.839 21.618 1.00 8.62 C
ATOM 62 N VAL A 10 37.097 38.640 24.034 1.00 15.94 N
ATOM 63 CA VAL A 10 36.944 38.525 25.440 1.00 15.09 C
ATOM 64 C VAL A 10 36.468 39.877 26.004 1.00 23.75 C
ATOM 65 O VAL A 10 36.970 40.996 25.673 1.00 18.06 O
ATOM 66 CB VAL A 10 38.306 38.102 25.977 1.00 19.30 C
ATOM 67 CG1 VAL A 10 38.341 38.257 27.466 1.00 25.38 C
ATOM 68 CG2 VAL A 10 38.626 36.645 25.612 1.00 10.82 C
ATOM 69 N ASP A 11 35.460 39.786 26.862 1.00 18.63 N
ATOM 70 CA ASP A 11 34.938 40.984 27.440 1.00 24.11 C
ATOM 71 C ASP A 11 34.083 41.833 26.535 1.00 15.02 C
ATOM 72 O ASP A 11 33.922 42.989 26.799 1.00 18.02 O
ATOM 73 CB ASP A 11 35.998 41.758 28.189 1.00 44.82 C
ATOM 74 CG ASP A 11 36.381 41.036 29.465 1.00 64.32 C
ATOM 75 OD1 ASP A 11 35.614 40.288 30.073 1.00 68.25 O
ATOM 76 OD2 ASP A 11 37.599 41.340 29.878 1.00 73.28 O
ATOM 77 N ARG A 12 33.542 41.218 25.489 1.00 11.63 N
ATOM 78 CA ARG A 12 32.665 41.858 24.508 1.00 10.38 C
ATOM 79 C ARG A 12 33.385 42.921 23.761 1.00 11.97 C
ATOM 80 O ARG A 12 32.763 43.848 23.177 1.00 12.18 O
ATOM 81 CB ARG A 12 31.530 42.538 25.215 1.00 14.95 C
ATOM 82 CG ARG A 12 30.485 41.583 25.780 1.00 17.21 C
ATOM 83 CD ARG A 12 29.155 42.308 26.079 1.00 23.41 C
ATOM 84 NE ARG A 12 29.221 42.854 27.406 1.00 32.02 N
ATOM 85 CZ ARG A 12 29.215 44.085 27.831 1.00 35.08 C
ATOM 86 NH1 ARG A 12 29.106 45.157 27.072 1.00 35.56 N
ATOM 87 NH2 ARG A 12 29.316 44.222 29.131 1.00 43.00 N
ATOM 88 N VAL A 13 34.710 42.826 23.792 1.00 6.63 N
ATOM 89 CA VAL A 13 35.437 43.843 23.057 1.00 5.35 C
ATOM 90 C VAL A 13 35.122 43.718 21.577 1.00 13.49 C
ATOM 91 O VAL A 13 35.257 42.629 20.987 1.00 13.86 O
ATOM 92 CB VAL A 13 36.936 43.710 23.228 1.00 5.61 C
ATOM 93 CG1 VAL A 13 37.594 44.650 22.220 1.00 2.27 C
ATOM 94 CG2 VAL A 13 37.263 44.269 24.618 1.00 6.66 C
ATOM 95 N ILE A 14 34.707 44.820 20.957 1.00 10.74 N
ATOM 96 CA ILE A 14 34.438 44.736 19.527 1.00 8.46 C
ATOM 97 C ILE A 14 35.328 45.629 18.710 1.00 16.65 C
ATOM 98 O ILE A 14 35.407 45.508 17.474 1.00 17.50 O
ATOM 99 CB ILE A 14 33.042 45.028 19.111 1.00 7.97 C
ATOM 100 CG1 ILE A 14 32.698 46.489 19.363 1.00 9.01 C
ATOM 101 CG2 ILE A 14 32.059 44.107 19.766 1.00 4.37 C
ATOM 102 CD1 ILE A 14 31.178 46.683 19.212 1.00 12.37 C
ATOM 103 N GLY A 15 36.020 46.549 19.354 1.00 13.06 N
ATOM 104 CA GLY A 15 36.843 47.336 18.495 1.00 26.80 C
ATOM 105 C GLY A 15 37.921 48.061 19.251 1.00 36.55 C
ATOM 106 O GLY A 15 37.822 48.244 20.472 1.00 26.73 O
ATOM 107 N MET A 16 38.924 48.473 18.465 1.00 42.48 N
ATOM 108 CA MET A 16 40.037 49.194 18.991 1.00 43.75 C
ATOM 109 C MET A 16 40.583 50.187 17.994 1.00 39.48 C
ATOM 110 O MET A 16 41.205 49.869 16.931 1.00 27.91 O
ATOM 111 CB MET A 16 41.120 48.303 19.611 1.00 53.85 C
ATOM 112 CG MET A 16 42.282 48.003 18.691 1.00 68.47 C
ATOM 113 SD MET A 16 43.722 48.978 19.176 1.00 82.07 S
ATOM 114 CE MET A 16 44.771 48.861 17.682 1.00 85.31 C
ATOM 115 N GLU A 17 40.308 51.418 18.401 1.00 36.35 N
ATOM 116 CA GLU A 17 40.736 52.531 17.644 1.00 40.46 C
ATOM 117 C GLU A 17 40.355 52.404 16.207 1.00 44.11 C
ATOM 118 O GLU A 17 41.247 52.383 15.329 1.00 40.78 O
ATOM 119 CB GLU A 17 42.247 52.590 17.753 1.00 43.27 C
ATOM 120 CG GLU A 17 42.589 53.274 19.061 1.00 52.17 C
ATOM 121 CD GLU A 17 44.054 53.230 19.217 1.00 60.56 C
ATOM 122 OE1 GLU A 17 44.738 52.466 18.540 1.00 60.16 O
ATOM 123 OE2 GLU A 17 44.491 54.115 20.093 1.00 63.33 O
ATOM 124 N ASN A 18 39.032 52.299 16.021 1.00 46.92 N
ATOM 125 CA ASN A 18 38.356 52.158 14.718 1.00 51.58 C
ATOM 126 C ASN A 18 38.899 50.969 13.861 1.00 48.30 C
ATOM 127 O ASN A 18 38.915 50.994 12.637 1.00 45.85 O
ATOM 128 CB ASN A 18 37.987 53.530 14.010 1.00 52.13 C
ATOM 129 CG ASN A 18 36.694 53.661 13.158 1.00 55.75 C
ATOM 130 OD1 ASN A 18 36.555 54.623 12.350 1.00 56.86 O
ATOM 131 ND2 ASN A 18 35.721 52.755 13.338 1.00 53.71 N
ATOM 132 N ALA A 19 39.341 49.905 14.539 1.00 42.82 N
ATOM 133 CA ALA A 19 39.853 48.742 13.867 1.00 41.14 C
ATOM 134 C ALA A 19 39.546 47.508 14.694 1.00 41.18 C
ATOM 135 O ALA A 19 39.374 47.618 15.904 1.00 38.96 O
ATOM 136 CB ALA A 19 41.357 48.844 13.668 1.00 37.08 C
ATOM 137 N MET A 20 39.470 46.361 14.009 1.00 43.79 N
ATOM 138 CA MET A 20 39.226 45.072 14.630 1.00 53.02 C
ATOM 139 C MET A 20 40.667 44.532 14.672 1.00 58.97 C
ATOM 140 O MET A 20 41.306 44.497 13.622 1.00 65.54 O
ATOM 141 CB MET A 20 38.239 44.193 13.806 1.00 56.58 C
ATOM 142 CG MET A 20 36.793 44.724 13.684 1.00 58.40 C
ATOM 143 SD MET A 20 35.586 43.592 12.868 1.00 57.02 S
ATOM 144 CE MET A 20 36.600 42.902 11.541 1.00 57.06 C
ATOM 145 N PRO A 21 41.220 44.150 15.839 1.00 54.19 N
ATOM 146 CA PRO A 21 42.623 43.663 15.939 1.00 50.73 C
ATOM 147 C PRO A 21 43.089 42.335 15.300 1.00 54.88 C
ATOM 148 O PRO A 21 44.140 42.248 14.626 1.00 58.09 O
ATOM 149 CB PRO A 21 42.971 43.732 17.418 1.00 45.09 C
ATOM 150 CG PRO A 21 41.938 44.671 18.069 1.00 45.10 C
ATOM 151 CD PRO A 21 40.753 44.780 17.118 1.00 47.05 C
ATOM 152 N TRP A 22 42.296 41.307 15.520 1.00 51.23 N
ATOM 153 CA TRP A 22 42.516 39.943 15.042 1.00 49.43 C
ATOM 154 C TRP A 22 42.473 39.704 13.506 1.00 54.55 C
ATOM 155 O TRP A 22 42.222 40.612 12.726 1.00 59.56 O
ATOM 156 CB TRP A 22 41.422 39.147 15.770 1.00 36.82 C
ATOM 157 CG TRP A 22 40.052 39.671 15.461 1.00 27.70 C
ATOM 158 CD1 TRP A 22 39.379 39.534 14.280 1.00 30.79 C
ATOM 159 CD2 TRP A 22 39.183 40.396 16.314 1.00 23.04 C
ATOM 160 NE1 TRP A 22 38.123 40.113 14.351 1.00 32.49 N
ATOM 161 CE2 TRP A 22 37.980 40.644 15.592 1.00 29.91 C
ATOM 162 CE3 TRP A 22 39.311 40.851 17.610 1.00 22.91 C
ATOM 163 CZ2 TRP A 22 36.922 41.354 16.143 1.00 36.37 C
ATOM 164 CZ3 TRP A 22 38.255 41.537 18.170 1.00 28.62 C
ATOM 165 CH2 TRP A 22 37.070 41.796 17.458 1.00 34.42 C
ATOM 166 N ASN A 23 42.712 38.472 13.046 1.00 54.56 N
ATOM 167 CA ASN A 23 42.654 38.191 11.611 1.00 56.20 C
ATOM 168 C ASN A 23 41.872 36.904 11.464 1.00 43.84 C
ATOM 169 O ASN A 23 42.451 35.818 11.468 1.00 45.33 O
ATOM 170 CB ASN A 23 44.022 38.151 10.866 1.00 68.23 C
ATOM 171 CG ASN A 23 43.977 37.907 9.347 1.00 74.35 C
ATOM 172 OD1 ASN A 23 43.014 38.264 8.644 1.00 76.26 O
ATOM 173 ND2 ASN A 23 45.026 37.270 8.827 1.00 76.17 N
ATOM 174 N LEU A 24 40.546 37.064 11.343 1.00 32.11 N
ATOM 175 CA LEU A 24 39.669 35.936 11.217 1.00 21.07 C
ATOM 176 C LEU A 24 38.844 35.747 9.973 1.00 18.40 C
ATOM 177 O LEU A 24 37.631 35.949 9.904 1.00 18.32 O
ATOM 178 CB LEU A 24 38.706 35.883 12.349 1.00 19.65 C
ATOM 179 CG LEU A 24 39.229 35.329 13.621 1.00 25.40 C
ATOM 180 CD1 LEU A 24 37.989 35.393 14.458 1.00 33.80 C
ATOM 181 CD2 LEU A 24 39.511 33.849 13.508 1.00 20.03 C
ATOM 182 N PRO A 25 39.518 35.276 8.997 1.00 20.51 N
ATOM 183 CA PRO A 25 38.956 35.002 7.723 1.00 17.54 C
ATOM 184 C PRO A 25 37.696 34.112 7.750 1.00 22.99 C
ATOM 185 O PRO A 25 36.791 34.232 6.885 1.00 31.23 O
ATOM 186 CB PRO A 25 40.117 34.405 6.932 1.00 18.63 C
ATOM 187 CG PRO A 25 41.385 34.539 7.782 1.00 18.62 C
ATOM 188 CD PRO A 25 40.946 34.954 9.156 1.00 17.19 C
ATOM 189 N ALA A 26 37.595 33.193 8.713 1.00 14.15 N
ATOM 190 CA ALA A 26 36.387 32.376 8.698 1.00 12.51 C
ATOM 191 C ALA A 26 35.258 33.317 9.021 1.00 4.90 C
ATOM 192 O ALA A 26 34.143 33.183 8.572 1.00 14.39 O
ATOM 193 CB ALA A 26 36.510 31.227 9.691 1.00 15.43 C
ATOM 194 N ASP A 27 35.599 34.326 9.833 1.00 8.50 N
ATOM 195 CA ASP A 27 34.651 35.360 10.242 1.00 16.42 C
ATOM 196 C ASP A 27 34.218 36.233 9.056 1.00 10.54 C
ATOM 197 O ASP A 27 33.044 36.533 8.884 1.00 17.16 O
ATOM 198 CB ASP A 27 35.047 36.240 11.473 1.00 15.98 C
ATOM 199 CG ASP A 27 33.882 37.062 11.930 1.00 17.38 C
ATOM 200 OD1 ASP A 27 32.820 36.599 12.339 1.00 18.68 O
ATOM 201 OD2 ASP A 27 34.093 38.341 11.746 1.00 22.06 O
ATOM 202 N LEU A 28 35.158 36.627 8.223 1.00 12.10 N
ATOM 203 CA LEU A 28 34.748 37.441 7.067 1.00 17.92 C
ATOM 204 C LEU A 28 33.786 36.692 6.178 1.00 7.96 C
ATOM 205 O LEU A 28 32.831 37.253 5.634 1.00 10.72 O
ATOM 206 CB LEU A 28 35.970 37.975 6.269 1.00 28.75 C
ATOM 207 CG LEU A 28 36.945 38.581 7.266 1.00 37.35 C
ATOM 208 CD1 LEU A 28 38.341 38.800 6.695 1.00 39.65 C
ATOM 209 CD2 LEU A 28 36.376 39.881 7.840 1.00 42.21 C
ATOM 210 N ALA A 29 34.034 35.382 5.999 1.00 12.78 N
ATOM 211 CA ALA A 29 33.154 34.583 5.161 1.00 18.22 C
ATOM 212 C ALA A 29 31.783 34.458 5.823 1.00 16.80 C
ATOM 213 O ALA A 29 30.704 34.367 5.209 1.00 13.61 O
ATOM 214 CB ALA A 29 33.785 33.215 5.065 1.00 17.72 C
ATOM 215 N TRP A 30 31.798 34.426 7.141 1.00 11.12 N
ATOM 216 CA TRP A 30 30.504 34.321 7.799 1.00 6.26 C
ATOM 217 C TRP A 30 29.740 35.608 7.625 1.00 2.64 C
ATOM 218 O TRP A 30 28.561 35.632 7.262 1.00 4.52 O
ATOM 219 CB TRP A 30 30.727 34.032 9.274 1.00 8.59 C
ATOM 220 CG TRP A 30 29.602 34.176 10.254 1.00 9.24 C
ATOM 221 CD1 TRP A 30 29.421 35.232 11.076 1.00 12.50 C
ATOM 222 CD2 TRP A 30 28.580 33.259 10.575 1.00 13.76 C
ATOM 223 NE1 TRP A 30 28.356 35.035 11.879 1.00 9.99 N
ATOM 224 CE2 TRP A 30 27.812 33.836 11.581 1.00 11.11 C
ATOM 225 CE3 TRP A 30 28.262 32.006 10.108 1.00 12.25 C
ATOM 226 CZ2 TRP A 30 26.729 33.196 12.143 1.00 10.76 C
ATOM 227 CZ3 TRP A 30 27.189 31.395 10.639 1.00 12.69 C
ATOM 228 CH2 TRP A 30 26.437 31.960 11.647 1.00 9.21 C
ATOM 229 N PHE A 31 30.424 36.711 7.898 1.00 5.82 N
ATOM 230 CA PHE A 31 29.744 37.981 7.740 1.00 2.43 C
ATOM 231 C PHE A 31 29.153 38.163 6.326 1.00 9.87 C
ATOM 232 O PHE A 31 27.992 38.546 6.119 1.00 10.52 O
ATOM 233 CB PHE A 31 30.812 39.063 7.778 1.00 10.36 C
ATOM 234 CG PHE A 31 30.285 40.462 7.559 1.00 18.07 C
ATOM 235 CD1 PHE A 31 29.654 41.148 8.592 1.00 21.22 C
ATOM 236 CD2 PHE A 31 30.440 41.122 6.339 1.00 20.84 C
ATOM 237 CE1 PHE A 31 29.161 42.437 8.416 1.00 10.45 C
ATOM 238 CE2 PHE A 31 29.960 42.413 6.140 1.00 12.74 C
ATOM 239 CZ PHE A 31 29.323 43.070 7.186 1.00 15.82 C
ATOM 240 N LYS A 32 30.019 37.885 5.338 1.00 11.00 N
ATOM 241 CA LYS A 32 29.608 38.044 3.951 1.00 13.00 C
ATOM 242 C LYS A 32 28.388 37.291 3.659 1.00 18.67 C
ATOM 243 O LYS A 32 27.460 37.821 3.111 1.00 22.69 O
ATOM 244 CB LYS A 32 30.656 37.611 2.921 1.00 24.81 C
ATOM 245 CG LYS A 32 30.026 37.485 1.502 1.00 35.50 C
ATOM 246 CD LYS A 32 31.072 37.425 0.381 1.00 46.44 C
ATOM 247 CE LYS A 32 30.529 37.515 -1.045 1.00 56.01 C
ATOM 248 NZ LYS A 32 31.558 37.179 -2.057 1.00 60.23 N
ATOM 249 N ARG A 33 28.406 36.037 4.050 1.00 11.74 N
ATOM 250 CA ARG A 33 27.303 35.209 3.824 1.00 8.33 C
ATOM 251 C ARG A 33 26.060 35.625 4.498 1.00 11.53 C
ATOM 252 O ARG A 33 24.943 35.455 3.934 1.00 8.32 O
ATOM 253 CB ARG A 33 27.706 33.771 4.080 1.00 24.18 C
ATOM 254 CG ARG A 33 26.637 32.873 4.676 1.00 35.19 C
ATOM 255 CD ARG A 33 27.196 31.456 4.838 1.00 46.79 C
ATOM 256 NE ARG A 33 28.071 31.296 6.000 1.00 57.28 N
ATOM 257 CZ ARG A 33 29.401 31.219 5.963 1.00 66.01 C
ATOM 258 NH1 ARG A 33 30.074 31.278 4.813 1.00 71.09 N
ATOM 259 NH2 ARG A 33 30.079 31.065 7.109 1.00 64.63 N
ATOM 260 N ASN A 34 26.182 36.179 5.708 1.00 8.00 N
ATOM 261 CA ASN A 34 24.902 36.543 6.318 1.00 6.41 C
ATOM 262 C ASN A 34 24.383 37.902 5.877 1.00 10.70 C
ATOM 263 O ASN A 34 23.203 38.164 6.059 1.00 14.56 O
ATOM 264 CB ASN A 34 24.895 36.424 7.833 1.00 7.53 C
ATOM 265 CG ASN A 34 24.960 34.965 8.306 1.00 13.10 C
ATOM 266 OD1 ASN A 34 24.064 34.140 8.022 1.00 16.20 O
ATOM 267 ND2 ASN A 34 26.080 34.620 8.904 1.00 12.93 N
ATOM 268 N THR A 35 25.269 38.738 5.329 1.00 4.32 N
ATOM 269 CA THR A 35 24.865 40.078 4.886 1.00 8.95 C
ATOM 270 C THR A 35 24.490 40.270 3.377 1.00 15.27 C
ATOM 271 O THR A 35 23.764 41.189 2.955 1.00 8.22 O
ATOM 272 CB THR A 35 25.931 41.084 5.279 1.00 6.09 C
ATOM 273 OG1 THR A 35 27.208 40.686 4.813 1.00 11.44 O
ATOM 274 CG2 THR A 35 25.900 41.235 6.799 1.00 4.82 C
ATOM 275 N LEU A 36 25.009 39.402 2.555 1.00 7.65 N
ATOM 276 CA LEU A 36 24.768 39.428 1.121 1.00 18.56 C
ATOM 277 C LEU A 36 23.323 39.620 0.699 1.00 13.16 C
ATOM 278 O LEU A 36 22.418 38.862 1.080 1.00 13.79 O
ATOM 279 CB LEU A 36 25.232 38.120 0.451 1.00 23.93 C
ATOM 280 CG LEU A 36 25.449 38.383 -1.047 1.00 33.84 C
ATOM 281 CD1 LEU A 36 26.157 39.741 -1.252 1.00 33.11 C
ATOM 282 CD2 LEU A 36 26.267 37.263 -1.666 1.00 33.79 C
ATOM 283 N ASP A 37 23.115 40.642 -0.115 1.00 9.67 N
ATOM 284 CA ASP A 37 21.769 40.944 -0.633 1.00 7.26 C
ATOM 285 C ASP A 37 20.766 41.485 0.352 1.00 14.54 C
ATOM 286 O ASP A 37 19.539 41.349 0.148 1.00 17.33 O
ATOM 287 CB ASP A 37 21.180 39.775 -1.447 1.00 13.18 C
ATOM 288 CG ASP A 37 22.056 39.432 -2.614 1.00 22.37 C
ATOM 289 OD1 ASP A 37 22.666 40.280 -3.281 1.00 24.33 O
ATOM 290 OD2 ASP A 37 22.255 38.140 -2.701 1.00 25.45 O
ATOM 291 N LYS A 38 21.266 42.108 1.432 1.00 8.27 N
ATOM 292 CA LYS A 38 20.353 42.674 2.411 1.00 6.33 C
ATOM 293 C LYS A 38 20.884 44.038 2.662 1.00 6.70 C
ATOM 294 O LYS A 38 22.050 44.293 2.400 1.00 15.85 O
ATOM 295 CB LYS A 38 20.314 41.939 3.780 1.00 11.88 C
ATOM 296 CG LYS A 38 20.213 40.415 3.680 1.00 8.62 C
ATOM 297 CD LYS A 38 20.057 39.647 4.973 1.00 6.24 C
ATOM 298 CE LYS A 38 20.448 38.182 4.776 1.00 13.48 C
ATOM 299 NZ LYS A 38 20.491 37.337 6.026 1.00 17.55 N
ATOM 300 N PRO A 39 20.042 44.891 3.196 1.00 6.39 N
ATOM 301 CA PRO A 39 20.483 46.215 3.494 1.00 9.43 C
ATOM 302 C PRO A 39 21.269 46.152 4.789 1.00 14.83 C
ATOM 303 O PRO A 39 20.952 45.341 5.682 1.00 9.96 O
ATOM 304 CB PRO A 39 19.216 47.041 3.744 1.00 12.08 C
ATOM 305 CG PRO A 39 18.018 46.097 3.682 1.00 6.71 C
ATOM 306 CD PRO A 39 18.564 44.725 3.341 1.00 5.91 C
ATOM 307 N VAL A 40 22.273 47.011 4.887 1.00 9.82 N
ATOM 308 CA VAL A 40 23.087 47.077 6.064 1.00 4.85 C
ATOM 309 C VAL A 40 23.080 48.506 6.592 1.00 12.74 C
ATOM 310 O VAL A 40 23.211 49.462 5.805 1.00 8.79 O
ATOM 311 CB VAL A 40 24.527 46.695 5.790 1.00 2.70 C
ATOM 312 CG1 VAL A 40 24.635 45.242 5.534 1.00 5.31 C
ATOM 313 CG2 VAL A 40 25.175 47.378 4.605 1.00 9.85 C
ATOM 314 N ILE A 41 22.913 48.628 7.928 1.00 13.40 N
ATOM 315 CA ILE A 41 22.926 49.894 8.611 1.00 7.65 C
ATOM 316 C ILE A 41 24.199 49.926 9.396 1.00 6.53 C
ATOM 317 O ILE A 41 24.613 48.956 10.081 1.00 5.46 O
ATOM 318 CB ILE A 41 21.693 50.165 9.491 1.00 8.39 C
ATOM 319 CG1 ILE A 41 20.426 49.992 8.646 1.00 6.08 C
ATOM 320 CG2 ILE A 41 21.757 51.590 10.058 1.00 5.98 C
ATOM 321 CD1 ILE A 41 19.094 50.227 9.385 1.00 6.84 C
ATOM 322 N MET A 42 24.858 51.033 9.328 1.00 1.00 N
ATOM 323 CA MET A 42 26.100 51.184 10.060 1.00 1.00 C
ATOM 324 C MET A 42 26.233 52.667 10.501 1.00 10.91 C
ATOM 325 O MET A 42 25.522 53.593 9.992 1.00 7.56 O
ATOM 326 CB MET A 42 27.262 50.857 9.137 1.00 4.48 C
ATOM 327 CG MET A 42 27.607 51.923 8.106 1.00 2.50 C
ATOM 328 SD MET A 42 28.874 51.309 6.930 1.00 13.94 S
ATOM 329 CE MET A 42 27.703 50.538 5.764 1.00 15.62 C
ATOM 330 N GLY A 43 27.109 52.887 11.475 1.00 3.61 N
ATOM 331 CA GLY A 43 27.344 54.216 11.981 1.00 6.99 C
ATOM 332 C GLY A 43 28.457 54.870 11.168 1.00 10.52 C
ATOM 333 O GLY A 43 29.220 54.162 10.455 1.00 2.25 O
ATOM 334 N ARG A 44 28.573 56.211 11.273 1.00 10.28 N
ATOM 335 CA ARG A 44 29.617 56.932 10.555 1.00 9.02 C
ATOM 336 C ARG A 44 31.040 56.445 10.853 1.00 8.24 C
ATOM 337 O ARG A 44 31.876 56.348 9.978 1.00 8.88 O
ATOM 338 CB ARG A 44 29.476 58.450 10.669 1.00 15.18 C
ATOM 339 CG ARG A 44 30.415 59.202 9.698 1.00 26.97 C
ATOM 340 CD ARG A 44 30.437 60.740 9.901 1.00 27.43 C
ATOM 341 NE ARG A 44 30.675 61.130 11.311 1.00 29.36 N
ATOM 342 CZ ARG A 44 31.863 61.186 11.995 1.00 34.86 C
ATOM 343 NH1 ARG A 44 33.044 60.874 11.469 1.00 32.22 N
ATOM 344 NH2 ARG A 44 31.860 61.567 13.289 1.00 37.48 N
ATOM 345 N HIS A 45 31.404 56.097 12.081 1.00 9.65 N
ATOM 346 CA HIS A 45 32.791 55.648 12.246 1.00 14.10 C
ATOM 347 C HIS A 45 33.066 54.358 11.537 1.00 16.67 C
ATOM 348 O HIS A 45 34.162 54.157 11.010 1.00 8.36 O
ATOM 349 CB HIS A 45 33.197 55.423 13.694 1.00 21.95 C
ATOM 350 CG HIS A 45 32.974 56.676 14.399 1.00 31.93 C
ATOM 351 ND1 HIS A 45 33.777 57.781 14.128 1.00 39.76 N
ATOM 352 CD2 HIS A 45 32.048 57.011 15.314 1.00 35.21 C
ATOM 353 CE1 HIS A 45 33.337 58.756 14.904 1.00 38.29 C
ATOM 354 NE2 HIS A 45 32.305 58.330 15.623 1.00 36.15 N
ATOM 355 N THR A 46 32.043 53.512 11.535 1.00 15.00 N
ATOM 356 CA THR A 46 32.201 52.257 10.875 1.00 12.16 C
ATOM 357 C THR A 46 32.344 52.491 9.332 1.00 9.27 C
ATOM 358 O THR A 46 33.171 51.894 8.630 1.00 12.89 O
ATOM 359 CB THR A 46 31.041 51.328 11.316 1.00 13.96 C
ATOM 360 OG1 THR A 46 31.112 51.002 12.726 1.00 11.23 O
ATOM 361 CG2 THR A 46 31.028 50.081 10.452 1.00 15.68 C
ATOM 362 N TRP A 47 31.549 53.403 8.805 1.00 9.00 N
ATOM 363 CA TRP A 47 31.583 53.748 7.401 1.00 4.22 C
ATOM 364 C TRP A 47 32.983 54.168 7.014 1.00 8.12 C
ATOM 365 O TRP A 47 33.616 53.649 6.077 1.00 16.11 O
ATOM 366 CB TRP A 47 30.543 54.869 7.040 1.00 3.86 C
ATOM 367 CG TRP A 47 30.757 55.556 5.677 1.00 9.97 C
ATOM 368 CD1 TRP A 47 30.970 56.902 5.477 1.00 16.09 C
ATOM 369 CD2 TRP A 47 30.824 54.951 4.353 1.00 9.57 C
ATOM 370 NE1 TRP A 47 31.179 57.171 4.149 1.00 19.56 N
ATOM 371 CE2 TRP A 47 31.080 55.999 3.422 1.00 14.09 C
ATOM 372 CE3 TRP A 47 30.723 53.636 3.892 1.00 12.28 C
ATOM 373 CZ2 TRP A 47 31.222 55.767 2.054 1.00 8.58 C
ATOM 374 CZ3 TRP A 47 30.866 53.410 2.551 1.00 10.19 C
ATOM 375 CH2 TRP A 47 31.097 54.478 1.642 1.00 14.30 C
ATOM 376 N GLU A 48 33.498 55.129 7.757 1.00 9.92 N
ATOM 377 CA GLU A 48 34.827 55.617 7.475 1.00 15.76 C
ATOM 378 C GLU A 48 35.884 54.551 7.407 1.00 25.89 C
ATOM 379 O GLU A 48 36.727 54.520 6.489 1.00 29.86 O
ATOM 380 CB GLU A 48 35.223 56.836 8.342 1.00 15.09 C
ATOM 381 CG GLU A 48 34.118 57.910 8.225 1.00 17.90 C
ATOM 382 CD GLU A 48 34.350 59.175 9.022 1.00 28.88 C
ATOM 383 OE1 GLU A 48 35.039 59.226 10.033 1.00 31.19 O
ATOM 384 OE2 GLU A 48 33.591 60.174 8.603 1.00 33.57 O
ATOM 385 N SER A 49 35.855 53.658 8.376 1.00 26.31 N
ATOM 386 CA SER A 49 36.863 52.638 8.332 1.00 24.93 C
ATOM 387 C SER A 49 36.650 51.693 7.142 1.00 28.29 C
ATOM 388 O SER A 49 37.606 51.144 6.620 1.00 36.23 O
ATOM 389 CB SER A 49 36.999 51.867 9.633 1.00 22.67 C
ATOM 390 OG SER A 49 36.122 50.791 9.502 1.00 27.05 O
ATOM 391 N ILE A 50 35.421 51.467 6.673 1.00 23.78 N
ATOM 392 CA ILE A 50 35.326 50.560 5.547 1.00 15.38 C
ATOM 393 C ILE A 50 35.737 51.259 4.251 1.00 23.85 C
ATOM 394 O ILE A 50 36.291 50.656 3.353 1.00 30.06 O
ATOM 395 CB ILE A 50 34.135 49.601 5.553 1.00 19.53 C
ATOM 396 CG1 ILE A 50 33.383 49.673 4.276 1.00 30.25 C
ATOM 397 CG2 ILE A 50 33.130 49.924 6.641 1.00 26.90 C
ATOM 398 CD1 ILE A 50 31.969 50.164 4.524 1.00 34.87 C
ATOM 399 N GLY A 51 35.483 52.562 4.165 1.00 16.27 N
ATOM 400 CA GLY A 51 35.825 53.412 3.034 1.00 21.18 C
ATOM 401 C GLY A 51 35.125 53.270 1.670 1.00 32.29 C
ATOM 402 O GLY A 51 35.116 54.238 0.888 1.00 34.64 O
ATOM 403 N ARG A 52 34.552 52.084 1.368 1.00 32.70 N
ATOM 404 CA ARG A 52 33.850 51.814 0.118 1.00 30.41 C
ATOM 405 C ARG A 52 32.602 51.008 0.396 1.00 24.91 C
ATOM 406 O ARG A 52 32.616 50.108 1.249 1.00 21.08 O
ATOM 407 CB ARG A 52 34.683 50.944 -0.778 1.00 36.91 C
ATOM 408 CG ARG A 52 34.030 50.863 -2.125 1.00 55.48 C
ATOM 409 CD ARG A 52 34.987 50.244 -3.119 1.00 74.10 C
ATOM 410 NE ARG A 52 34.857 50.816 -4.451 1.00 85.29 N
ATOM 411 CZ ARG A 52 34.463 50.132 -5.516 1.00 89.05 C
ATOM 412 NH1 ARG A 52 34.157 48.840 -5.459 1.00 90.27 N
ATOM 413 NH2 ARG A 52 34.391 50.774 -6.668 1.00 89.75 N
ATOM 414 N PRO A 53 31.535 51.298 -0.319 1.00 16.34 N
ATOM 415 CA PRO A 53 30.309 50.549 -0.076 1.00 14.71 C
ATOM 416 C PRO A 53 30.438 49.031 -0.135 1.00 15.06 C
ATOM 417 O PRO A 53 31.223 48.467 -0.885 1.00 12.97 O
ATOM 418 CB PRO A 53 29.317 51.003 -1.147 1.00 18.86 C
ATOM 419 CG PRO A 53 29.926 52.233 -1.842 1.00 14.41 C
ATOM 420 CD PRO A 53 31.404 52.255 -1.473 1.00 12.79 C
ATOM 421 N LEU A 54 29.655 48.345 0.679 1.00 11.80 N
ATOM 422 CA LEU A 54 29.730 46.913 0.611 1.00 15.18 C
ATOM 423 C LEU A 54 28.889 46.585 -0.617 1.00 16.04 C
ATOM 424 O LEU A 54 27.765 47.018 -0.790 1.00 10.23 O
ATOM 425 CB LEU A 54 29.160 46.143 1.834 1.00 16.01 C
ATOM 426 CG LEU A 54 29.921 46.397 3.118 1.00 12.71 C
ATOM 427 CD1 LEU A 54 29.057 45.996 4.296 1.00 16.13 C
ATOM 428 CD2 LEU A 54 31.182 45.575 3.130 1.00 15.28 C
ATOM 429 N PRO A 55 29.452 45.794 -1.484 1.00 18.14 N
ATOM 430 CA PRO A 55 28.772 45.404 -2.701 1.00 12.87 C
ATOM 431 C PRO A 55 27.689 44.421 -2.494 1.00 13.22 C
ATOM 432 O PRO A 55 27.780 43.571 -1.631 1.00 21.73 O
ATOM 433 CB PRO A 55 29.799 44.681 -3.523 1.00 14.95 C
ATOM 434 CG PRO A 55 31.135 44.748 -2.782 1.00 22.68 C
ATOM 435 CD PRO A 55 30.903 45.495 -1.469 1.00 17.39 C
ATOM 436 N GLY A 56 26.693 44.543 -3.325 1.00 18.53 N
ATOM 437 CA GLY A 56 25.516 43.672 -3.333 1.00 25.60 C
ATOM 438 C GLY A 56 24.640 43.753 -2.089 1.00 30.11 C
ATOM 439 O GLY A 56 24.153 42.652 -1.615 1.00 16.08 O
ATOM 440 N ARG A 57 24.485 45.061 -1.620 1.00 25.83 N
ATOM 441 CA ARG A 57 23.687 45.435 -0.424 1.00 19.47 C
ATOM 442 C ARG A 57 23.371 46.924 -0.346 1.00 17.78 C
ATOM 443 O ARG A 57 24.232 47.753 -0.667 1.00 19.83 O
ATOM 444 CB ARG A 57 24.537 45.152 0.818 1.00 12.08 C
ATOM 445 CG ARG A 57 24.618 43.679 1.110 1.00 10.86 C
ATOM 446 CD ARG A 57 25.917 43.176 1.798 1.00 20.68 C
ATOM 447 NE ARG A 57 27.100 43.036 0.941 1.00 22.48 N
ATOM 448 CZ ARG A 57 28.304 42.606 1.357 1.00 27.14 C
ATOM 449 NH1 ARG A 57 28.548 42.237 2.615 1.00 31.64 N
ATOM 450 NH2 ARG A 57 29.315 42.532 0.492 1.00 25.75 N
ATOM 451 N LYS A 58 22.162 47.316 0.082 1.00 14.15 N
ATOM 452 CA LYS A 58 21.929 48.764 0.194 1.00 7.29 C
ATOM 453 C LYS A 58 22.691 49.245 1.447 1.00 14.92 C
ATOM 454 O LYS A 58 22.441 48.759 2.560 1.00 13.65 O
ATOM 455 CB LYS A 58 20.500 49.045 0.434 1.00 9.38 C
ATOM 456 CG LYS A 58 20.184 50.506 0.431 1.00 13.22 C
ATOM 457 CD LYS A 58 18.695 50.611 0.393 1.00 13.53 C
ATOM 458 CE LYS A 58 18.095 52.030 0.299 1.00 21.63 C
ATOM 459 NZ LYS A 58 16.648 51.915 -0.069 1.00 17.58 N
ATOM 460 N ASN A 59 23.628 50.175 1.307 1.00 17.05 N
ATOM 461 CA ASN A 59 24.385 50.696 2.461 1.00 17.36 C
ATOM 462 C ASN A 59 23.781 51.985 3.031 1.00 17.49 C
ATOM 463 O ASN A 59 23.827 53.002 2.325 1.00 16.05 O
ATOM 464 CB ASN A 59 25.829 51.051 2.105 1.00 6.27 C
ATOM 465 CG ASN A 59 26.639 49.873 1.595 1.00 5.60 C
ATOM 466 OD1 ASN A 59 27.806 49.828 1.809 1.00 11.33 O
ATOM 467 ND2 ASN A 59 26.116 49.087 0.686 1.00 8.63 N
ATOM 468 N ILE A 60 23.245 51.931 4.285 1.00 13.40 N
ATOM 469 CA ILE A 60 22.612 53.022 5.062 1.00 3.79 C
ATOM 470 C ILE A 60 23.527 53.482 6.171 1.00 12.62 C
ATOM 471 O ILE A 60 23.934 52.693 7.047 1.00 9.43 O
ATOM 472 CB ILE A 60 21.287 52.516 5.568 1.00 14.57 C
ATOM 473 CG1 ILE A 60 20.422 52.310 4.331 1.00 13.76 C
ATOM 474 CG2 ILE A 60 20.601 53.527 6.480 1.00 15.38 C
ATOM 475 CD1 ILE A 60 19.437 51.222 4.557 1.00 13.88 C
ATOM 476 N ILE A 61 23.908 54.761 6.122 1.00 6.28 N
ATOM 477 CA ILE A 61 24.812 55.294 7.124 1.00 10.58 C
ATOM 478 C ILE A 61 24.088 56.298 7.964 1.00 12.62 C
ATOM 479 O ILE A 61 23.476 57.168 7.377 1.00 7.49 O
ATOM 480 CB ILE A 61 25.925 56.043 6.446 1.00 9.16 C
ATOM 481 CG1 ILE A 61 26.459 55.285 5.223 1.00 1.00 C
ATOM 482 CG2 ILE A 61 27.001 56.442 7.426 1.00 8.69 C
ATOM 483 CD1 ILE A 61 27.132 53.993 5.604 1.00 13.61 C
ATOM 484 N LEU A 62 24.193 56.163 9.308 1.00 9.13 N
ATOM 485 CA LEU A 62 23.559 57.018 10.314 1.00 5.12 C
ATOM 486 C LEU A 62 24.565 58.094 10.752 1.00 13.44 C
ATOM 487 O LEU A 62 25.687 57.824 11.176 1.00 14.02 O
ATOM 488 CB LEU A 62 23.309 56.081 11.482 1.00 16.26 C
ATOM 489 CG LEU A 62 22.113 56.221 12.423 1.00 25.58 C
ATOM 490 CD1 LEU A 62 21.036 57.217 11.974 1.00 20.45 C
ATOM 491 CD2 LEU A 62 21.524 54.824 12.580 1.00 18.43 C
ATOM 492 N SER A 63 24.173 59.344 10.626 1.00 6.22 N
ATOM 493 CA SER A 63 25.064 60.400 11.035 1.00 14.99 C
ATOM 494 C SER A 63 24.151 61.566 11.273 1.00 14.94 C
ATOM 495 O SER A 63 23.074 61.643 10.669 1.00 13.06 O
ATOM 496 CB SER A 63 26.146 60.775 10.013 1.00 15.60 C
ATOM 497 OG SER A 63 26.518 62.190 10.114 1.00 17.77 O
ATOM 498 N SER A 64 24.553 62.451 12.157 1.00 21.04 N
ATOM 499 CA SER A 64 23.712 63.639 12.425 1.00 20.59 C
ATOM 500 C SER A 64 23.899 64.670 11.302 1.00 18.63 C
ATOM 501 O SER A 64 22.992 65.454 11.002 1.00 23.34 O
ATOM 502 CB SER A 64 24.118 64.290 13.731 1.00 13.26 C
ATOM 503 OG SER A 64 25.537 64.405 13.745 1.00 22.72 O
ATOM 504 N GLN A 65 25.095 64.602 10.701 1.00 22.89 N
ATOM 505 CA GLN A 65 25.551 65.457 9.600 1.00 36.35 C
ATOM 506 C GLN A 65 25.118 65.006 8.211 1.00 38.14 C
ATOM 507 O GLN A 65 24.847 63.832 7.960 1.00 37.72 O
ATOM 508 CB GLN A 65 27.069 65.763 9.644 1.00 40.68 C
ATOM 509 CG GLN A 65 27.576 66.169 11.054 1.00 55.67 C
ATOM 510 CD GLN A 65 27.034 67.494 11.597 1.00 70.44 C
ATOM 511 OE1 GLN A 65 26.166 68.170 11.005 1.00 71.65 O
ATOM 512 NE2 GLN A 65 27.594 67.905 12.732 1.00 79.39 N
ATOM 513 N PRO A 66 25.061 65.970 7.302 1.00 41.97 N
ATOM 514 CA PRO A 66 24.663 65.719 5.923 1.00 44.15 C
ATOM 515 C PRO A 66 25.604 64.677 5.304 1.00 33.44 C
ATOM 516 O PRO A 66 26.767 64.629 5.660 1.00 30.04 O
ATOM 517 CB PRO A 66 24.665 67.092 5.229 1.00 48.98 C
ATOM 518 CG PRO A 66 25.070 68.119 6.287 1.00 50.53 C
ATOM 519 CD PRO A 66 25.627 67.332 7.459 1.00 48.31 C
ATOM 520 N GLY A 67 25.140 63.816 4.401 1.00 25.60 N
ATOM 521 CA GLY A 67 26.104 62.862 3.920 1.00 20.52 C
ATOM 522 C GLY A 67 27.190 63.503 3.115 1.00 21.18 C
ATOM 523 O GLY A 67 27.079 64.645 2.737 1.00 27.62 O
ATOM 524 N THR A 68 28.235 62.757 2.823 1.00 20.32 N
ATOM 525 CA THR A 68 29.342 63.274 1.987 1.00 22.65 C
ATOM 526 C THR A 68 29.825 62.257 0.902 1.00 13.18 C
ATOM 527 O THR A 68 30.987 62.131 0.508 1.00 16.80 O
ATOM 528 CB THR A 68 30.476 63.699 2.890 1.00 29.61 C
ATOM 529 OG1 THR A 68 31.052 62.541 3.528 1.00 26.16 O
ATOM 530 CG2 THR A 68 29.840 64.672 3.898 1.00 33.79 C
ATOM 531 N ASP A 69 28.919 61.495 0.398 1.00 12.80 N
ATOM 532 CA ASP A 69 29.308 60.516 -0.605 1.00 12.18 C
ATOM 533 C ASP A 69 27.998 60.035 -1.105 1.00 11.35 C
ATOM 534 O ASP A 69 27.157 59.648 -0.290 1.00 12.94 O
ATOM 535 CB ASP A 69 30.078 59.415 0.080 1.00 12.52 C
ATOM 536 CG ASP A 69 30.498 58.400 -0.917 1.00 13.47 C
ATOM 537 OD1 ASP A 69 29.737 57.983 -1.742 1.00 11.72 O
ATOM 538 OD2 ASP A 69 31.734 57.985 -0.782 1.00 12.63 O
ATOM 539 N ASP A 70 27.805 60.107 -2.413 1.00 14.00 N
ATOM 540 CA ASP A 70 26.529 59.696 -3.031 1.00 8.45 C
ATOM 541 C ASP A 70 26.450 58.233 -3.299 1.00 10.78 C
ATOM 542 O ASP A 70 25.447 57.727 -3.816 1.00 12.70 O
ATOM 543 CB ASP A 70 26.098 60.468 -4.278 1.00 17.27 C
ATOM 544 CG ASP A 70 25.569 61.821 -3.873 1.00 39.02 C
ATOM 545 OD1 ASP A 70 25.223 62.095 -2.725 1.00 43.16 O
ATOM 546 OD2 ASP A 70 25.582 62.695 -4.851 1.00 50.77 O
ATOM 547 N ARG A 71 27.489 57.520 -2.962 1.00 4.80 N
ATOM 548 CA ARG A 71 27.328 56.098 -3.256 1.00 9.97 C
ATOM 549 C ARG A 71 26.456 55.396 -2.202 1.00 10.38 C
ATOM 550 O ARG A 71 25.994 54.290 -2.431 1.00 12.41 O
ATOM 551 CB ARG A 71 28.585 55.268 -3.495 1.00 12.17 C
ATOM 552 CG ARG A 71 29.717 55.877 -4.332 1.00 10.90 C
ATOM 553 CD ARG A 71 30.897 56.133 -3.391 1.00 15.34 C
ATOM 554 NE ARG A 71 31.988 55.304 -3.641 1.00 18.65 N
ATOM 555 CZ ARG A 71 33.029 55.226 -2.911 1.00 19.16 C
ATOM 556 NH1 ARG A 71 33.191 55.931 -1.790 1.00 16.85 N
ATOM 557 NH2 ARG A 71 33.939 54.373 -3.349 1.00 28.25 N
ATOM 558 N VAL A 72 26.236 56.048 -1.060 1.00 10.25 N
ATOM 559 CA VAL A 72 25.458 55.438 0.003 1.00 7.98 C
ATOM 560 C VAL A 72 24.312 56.322 0.452 1.00 7.12 C
ATOM 561 O VAL A 72 24.297 57.457 0.122 1.00 11.50 O
ATOM 562 CB VAL A 72 26.432 55.146 1.156 1.00 10.39 C
ATOM 563 CG1 VAL A 72 27.624 54.341 0.637 1.00 12.14 C
ATOM 564 CG2 VAL A 72 26.891 56.480 1.826 1.00 4.75 C
ATOM 565 N THR A 73 23.349 55.783 1.202 1.00 4.74 N
ATOM 566 CA THR A 73 22.192 56.479 1.716 1.00 8.66 C
ATOM 567 C THR A 73 22.402 56.891 3.105 1.00 14.07 C
ATOM 568 O THR A 73 22.625 55.993 3.907 1.00 8.56 O
ATOM 569 CB THR A 73 21.085 55.457 1.781 1.00 11.82 C
ATOM 570 OG1 THR A 73 20.787 55.021 0.466 1.00 21.83 O
ATOM 571 CG2 THR A 73 19.857 56.042 2.395 1.00 9.30 C
ATOM 572 N TRP A 74 22.307 58.211 3.331 1.00 13.06 N
ATOM 573 CA TRP A 74 22.499 58.859 4.610 1.00 12.34 C
ATOM 574 C TRP A 74 21.186 59.150 5.278 1.00 13.57 C
ATOM 575 O TRP A 74 20.283 59.677 4.619 1.00 9.58 O
ATOM 576 CB TRP A 74 23.234 60.175 4.335 1.00 11.54 C
ATOM 577 CG TRP A 74 24.640 59.997 3.802 1.00 1.00 C
ATOM 578 CD1 TRP A 74 25.010 59.892 2.494 1.00 9.96 C
ATOM 579 CD2 TRP A 74 25.839 59.934 4.536 1.00 6.82 C
ATOM 580 NE1 TRP A 74 26.371 59.776 2.375 1.00 5.01 N
ATOM 581 CE2 TRP A 74 26.904 59.779 3.630 1.00 3.04 C
ATOM 582 CE3 TRP A 74 26.108 59.955 5.902 1.00 9.61 C
ATOM 583 CZ2 TRP A 74 28.209 59.634 4.038 1.00 6.08 C
ATOM 584 CZ3 TRP A 74 27.409 59.833 6.290 1.00 4.70 C
ATOM 585 CH2 TRP A 74 28.455 59.708 5.392 1.00 7.07 C
ATOM 586 N VAL A 75 21.083 58.789 6.584 1.00 3.72 N
ATOM 587 CA VAL A 75 19.855 58.984 7.392 1.00 6.44 C
ATOM 588 C VAL A 75 20.248 59.617 8.733 1.00 10.77 C
ATOM 589 O VAL A 75 21.400 59.575 9.173 1.00 11.66 O
ATOM 590 CB VAL A 75 19.108 57.693 7.622 1.00 5.02 C
ATOM 591 CG1 VAL A 75 18.449 57.240 6.313 1.00 6.12 C
ATOM 592 CG2 VAL A 75 20.142 56.667 8.185 1.00 5.84 C
ATOM 593 N LYS A 76 19.303 60.234 9.407 1.00 12.55 N
ATOM 594 CA LYS A 76 19.748 60.860 10.641 1.00 16.28 C
ATOM 595 C LYS A 76 18.986 60.393 11.857 1.00 17.94 C
ATOM 596 O LYS A 76 18.915 61.093 12.863 1.00 8.53 O
ATOM 597 CB LYS A 76 19.556 62.385 10.522 1.00 21.95 C
ATOM 598 CG LYS A 76 20.094 62.992 9.233 1.00 29.33 C
ATOM 599 CD LYS A 76 20.332 64.493 9.344 1.00 35.08 C
ATOM 600 CE LYS A 76 20.339 65.153 7.977 1.00 43.46 C
ATOM 601 NZ LYS A 76 20.624 66.605 8.055 1.00 56.42 N
ATOM 602 N SER A 77 18.388 59.233 11.798 1.00 5.50 N
ATOM 603 CA SER A 77 17.672 58.823 12.970 1.00 3.29 C
ATOM 604 C SER A 77 17.431 57.397 12.788 1.00 6.59 C
ATOM 605 O SER A 77 17.477 56.898 11.659 1.00 10.55 O
ATOM 606 CB SER A 77 16.414 59.607 13.217 1.00 6.51 C
ATOM 607 OG SER A 77 15.307 59.122 12.476 1.00 15.04 O
ATOM 608 N VAL A 78 17.198 56.716 13.859 1.00 12.80 N
ATOM 609 CA VAL A 78 17.005 55.295 13.766 1.00 5.35 C
ATOM 610 C VAL A 78 15.777 54.995 12.948 1.00 10.47 C
ATOM 611 O VAL A 78 15.729 54.089 12.068 1.00 9.71 O
ATOM 612 CB VAL A 78 16.875 54.677 15.192 1.00 11.80 C
ATOM 613 CG1 VAL A 78 16.161 53.328 15.154 1.00 11.09 C
ATOM 614 CG2 VAL A 78 18.230 54.508 15.859 1.00 5.71 C
ATOM 615 N ASP A 79 14.748 55.739 13.248 1.00 9.83 N
ATOM 616 CA ASP A 79 13.566 55.436 12.520 1.00 10.68 C
ATOM 617 C ASP A 79 13.707 55.662 11.006 1.00 9.55 C
ATOM 618 O ASP A 79 13.113 54.957 10.180 1.00 10.49 O
ATOM 619 CB ASP A 79 12.256 55.892 13.239 1.00 30.32 C
ATOM 620 CG ASP A 79 11.831 55.109 14.499 1.00 44.37 C
ATOM 621 OD1 ASP A 79 11.431 53.930 14.521 1.00 45.52 O
ATOM 622 OD2 ASP A 79 11.825 55.860 15.582 1.00 52.96 O
ATOM 623 N GLU A 80 14.515 56.652 10.658 1.00 9.21 N
ATOM 624 CA GLU A 80 14.721 56.947 9.289 1.00 8.47 C
ATOM 625 C GLU A 80 15.501 55.812 8.637 1.00 12.97 C
ATOM 626 O GLU A 80 15.256 55.430 7.443 1.00 9.73 O
ATOM 627 CB GLU A 80 15.510 58.284 9.122 1.00 11.70 C
ATOM 628 CG GLU A 80 15.150 59.054 7.862 1.00 16.58 C
ATOM 629 CD GLU A 80 16.217 59.990 7.326 1.00 23.85 C
ATOM 630 OE1 GLU A 80 16.852 60.637 8.269 1.00 20.66 O
ATOM 631 OE2 GLU A 80 16.376 60.217 6.108 1.00 21.08 O
ATOM 632 N ALA A 81 16.466 55.289 9.400 1.00 4.53 N
ATOM 633 CA ALA A 81 17.234 54.249 8.794 1.00 6.25 C
ATOM 634 C ALA A 81 16.415 53.000 8.537 1.00 11.00 C
ATOM 635 O ALA A 81 16.649 52.229 7.609 1.00 9.75 O
ATOM 636 CB ALA A 81 18.565 54.011 9.436 1.00 12.76 C
ATOM 637 N ILE A 82 15.432 52.773 9.350 1.00 6.37 N
ATOM 638 CA ILE A 82 14.606 51.569 9.151 1.00 6.98 C
ATOM 639 C ILE A 82 13.683 51.825 7.958 1.00 17.44 C
ATOM 640 O ILE A 82 13.510 51.009 7.040 1.00 12.18 O
ATOM 641 CB ILE A 82 13.780 51.383 10.399 1.00 9.38 C
ATOM 642 CG1 ILE A 82 14.753 51.102 11.550 1.00 15.99 C
ATOM 643 CG2 ILE A 82 12.775 50.268 10.211 1.00 10.62 C
ATOM 644 CD1 ILE A 82 14.021 50.668 12.817 1.00 15.75 C
ATOM 645 N ALA A 83 13.084 53.002 7.957 1.00 11.91 N
ATOM 646 CA ALA A 83 12.212 53.310 6.835 1.00 12.41 C
ATOM 647 C ALA A 83 12.957 53.252 5.492 1.00 13.22 C
ATOM 648 O ALA A 83 12.387 52.884 4.476 1.00 21.13 O
ATOM 649 CB ALA A 83 11.608 54.686 7.012 1.00 4.62 C
ATOM 650 N ALA A 84 14.219 53.619 5.453 1.00 9.49 N
ATOM 651 CA ALA A 84 14.943 53.593 4.198 1.00 7.32 C
ATOM 652 C ALA A 84 15.166 52.195 3.648 1.00 14.06 C
ATOM 653 O ALA A 84 15.428 52.043 2.471 1.00 15.25 O
ATOM 654 CB ALA A 84 16.290 54.287 4.317 1.00 2.65 C
ATOM 655 N CYS A 85 15.067 51.173 4.491 1.00 11.56 N
ATOM 656 CA CYS A 85 15.293 49.834 4.022 1.00 13.25 C
ATOM 657 C CYS A 85 14.111 49.274 3.261 1.00 20.73 C
ATOM 658 O CYS A 85 14.190 48.261 2.531 1.00 30.13 O
ATOM 659 CB CYS A 85 15.544 48.941 5.267 1.00 8.70 C
ATOM 660 SG CYS A 85 17.142 49.276 6.026 1.00 10.90 S
ATOM 661 N GLY A 86 12.986 49.906 3.461 1.00 25.44 N
ATOM 662 CA GLY A 86 11.769 49.440 2.825 1.00 29.94 C
ATOM 663 C GLY A 86 11.215 48.224 3.610 1.00 33.02 C
ATOM 664 O GLY A 86 11.449 48.027 4.846 1.00 25.40 O
ATOM 665 N ASP A 87 10.474 47.404 2.851 1.00 38.82 N
ATOM 666 CA ASP A 87 9.823 46.195 3.315 1.00 44.83 C
ATOM 667 C ASP A 87 10.608 44.861 3.099 1.00 36.05 C
ATOM 668 O ASP A 87 10.032 43.840 2.748 1.00 42.23 O
ATOM 669 CB ASP A 87 8.338 46.191 2.839 1.00 66.05 C
ATOM 670 CG ASP A 87 7.521 44.952 3.167 1.00 85.19 C
ATOM 671 OD1 ASP A 87 7.838 44.431 4.336 1.00 91.22 O
ATOM 672 OD2 ASP A 87 6.713 44.438 2.388 1.00 90.88 O
ATOM 673 N VAL A 88 11.929 44.827 3.307 1.00 19.73 N
ATOM 674 CA VAL A 88 12.703 43.599 3.142 1.00 8.52 C
ATOM 675 C VAL A 88 12.469 42.613 4.279 1.00 16.33 C
ATOM 676 O VAL A 88 11.991 42.974 5.320 1.00 15.40 O
ATOM 677 CB VAL A 88 14.122 43.889 3.011 1.00 12.37 C
ATOM 678 CG1 VAL A 88 14.105 44.749 1.773 1.00 18.21 C
ATOM 679 CG2 VAL A 88 14.508 44.743 4.257 1.00 14.90 C
ATOM 680 N PRO A 89 12.781 41.365 4.078 1.00 15.63 N
ATOM 681 CA PRO A 89 12.566 40.393 5.099 1.00 19.68 C
ATOM 682 C PRO A 89 13.527 40.508 6.323 1.00 20.14 C
ATOM 683 O PRO A 89 13.163 40.124 7.432 1.00 25.02 O
ATOM 684 CB PRO A 89 12.613 39.055 4.379 1.00 20.59 C
ATOM 685 CG PRO A 89 12.948 39.340 2.941 1.00 24.22 C
ATOM 686 CD PRO A 89 13.448 40.770 2.921 1.00 26.56 C
ATOM 687 N GLU A 90 14.739 41.070 6.140 1.00 10.40 N
ATOM 688 CA GLU A 90 15.687 41.225 7.212 1.00 9.30 C
ATOM 689 C GLU A 90 16.724 42.316 6.899 1.00 10.50 C
ATOM 690 O GLU A 90 17.371 42.368 5.818 1.00 10.55 O
ATOM 691 CB GLU A 90 16.408 39.923 7.456 1.00 7.53 C
ATOM 692 CG GLU A 90 17.582 39.956 8.480 1.00 8.61 C
ATOM 693 CD GLU A 90 18.206 38.557 8.575 1.00 13.88 C
ATOM 694 OE1 GLU A 90 18.290 37.770 7.600 1.00 11.73 O
ATOM 695 OE2 GLU A 90 18.537 38.205 9.784 1.00 11.55 O
ATOM 696 N ILE A 91 16.892 43.165 7.894 1.00 6.45 N
ATOM 697 CA ILE A 91 17.814 44.295 7.896 1.00 5.91 C
ATOM 698 C ILE A 91 19.040 43.978 8.732 1.00 5.99 C
ATOM 699 O ILE A 91 18.919 43.560 9.872 1.00 12.25 O
ATOM 700 CB ILE A 91 17.034 45.467 8.548 1.00 6.77 C
ATOM 701 CG1 ILE A 91 15.886 45.839 7.624 1.00 9.43 C
ATOM 702 CG2 ILE A 91 17.985 46.636 8.745 1.00 4.41 C
ATOM 703 CD1 ILE A 91 14.965 46.917 8.145 1.00 3.32 C
ATOM 704 N MET A 92 20.241 44.134 8.232 1.00 1.00 N
ATOM 705 CA MET A 92 21.399 43.813 9.039 1.00 1.39 C
ATOM 706 C MET A 92 22.043 45.022 9.679 1.00 11.66 C
ATOM 707 O MET A 92 22.483 45.864 8.932 1.00 15.35 O
ATOM 708 CB MET A 92 22.531 43.124 8.253 1.00 4.44 C
ATOM 709 CG MET A 92 22.035 41.863 7.554 1.00 6.12 C
ATOM 710 SD MET A 92 21.394 40.596 8.700 1.00 12.39 S
ATOM 711 CE MET A 92 22.981 40.144 9.472 1.00 10.77 C
ATOM 712 N VAL A 93 22.120 45.121 11.038 1.00 7.72 N
ATOM 713 CA VAL A 93 22.797 46.260 11.675 1.00 1.00 C
ATOM 714 C VAL A 93 24.246 45.819 11.850 1.00 5.94 C
ATOM 715 O VAL A 93 24.559 44.797 12.529 1.00 3.13 O
ATOM 716 CB VAL A 93 22.107 46.625 12.946 1.00 1.09 C
ATOM 717 CG1 VAL A 93 22.830 47.761 13.643 1.00 1.00 C
ATOM 718 CG2 VAL A 93 20.695 46.988 12.593 1.00 1.00 C
ATOM 719 N ILE A 94 25.198 46.537 11.252 1.00 5.81 N
ATOM 720 CA ILE A 94 26.606 46.109 11.353 1.00 4.26 C
ATOM 721 C ILE A 94 27.638 46.787 12.235 1.00 10.53 C
ATOM 722 O ILE A 94 28.849 46.463 12.196 1.00 8.35 O
ATOM 723 CB ILE A 94 27.130 45.863 9.951 1.00 11.22 C
ATOM 724 CG1 ILE A 94 27.269 47.213 9.230 1.00 14.96 C
ATOM 725 CG2 ILE A 94 26.059 45.054 9.266 1.00 5.89 C
ATOM 726 CD1 ILE A 94 28.168 47.163 7.986 1.00 14.92 C
ATOM 727 N GLY A 95 27.203 47.718 13.050 1.00 4.88 N
ATOM 728 CA GLY A 95 28.197 48.359 13.926 1.00 15.71 C
ATOM 729 C GLY A 95 28.203 49.868 13.699 1.00 10.26 C
ATOM 730 O GLY A 95 27.554 50.344 12.744 1.00 8.30 O
ATOM 731 N GLY A 96 28.903 50.618 14.549 1.00 5.97 N
ATOM 732 CA GLY A 96 29.657 50.098 15.654 1.00 7.78 C
ATOM 733 C GLY A 96 28.865 50.070 16.953 1.00 9.94 C
ATOM 734 O GLY A 96 27.630 49.903 17.028 1.00 9.00 O
ATOM 735 N GLY A 97 29.616 50.248 18.007 1.00 5.33 N
ATOM 736 CA GLY A 97 28.999 50.206 19.327 1.00 9.51 C
ATOM 737 C GLY A 97 27.808 51.082 19.586 1.00 6.48 C
ATOM 738 O GLY A 97 26.768 50.620 20.059 1.00 6.95 O
ATOM 739 N ARG A 98 27.977 52.364 19.292 1.00 13.32 N
ATOM 740 CA ARG A 98 26.892 53.291 19.517 1.00 12.61 C
ATOM 741 C ARG A 98 25.698 52.831 18.743 1.00 11.76 C
ATOM 742 O ARG A 98 24.618 52.895 19.257 1.00 14.11 O
ATOM 743 CB ARG A 98 27.225 54.777 19.312 1.00 20.34 C
ATOM 744 CG ARG A 98 25.988 55.616 19.668 1.00 48.53 C
ATOM 745 CD ARG A 98 26.047 57.144 19.458 1.00 67.81 C
ATOM 746 NE ARG A 98 24.710 57.774 19.490 1.00 80.17 N
ATOM 747 CZ ARG A 98 24.361 58.871 18.795 1.00 91.16 C
ATOM 748 NH1 ARG A 98 25.219 59.507 17.986 1.00 94.35 N
ATOM 749 NH2 ARG A 98 23.110 59.345 18.903 1.00 94.99 N
ATOM 750 N VAL A 99 25.900 52.336 17.511 1.00 4.11 N
ATOM 751 CA VAL A 99 24.758 51.851 16.721 1.00 7.52 C
ATOM 752 C VAL A 99 24.065 50.574 17.219 1.00 1.00 C
ATOM 753 O VAL A 99 22.829 50.446 17.233 1.00 2.06 O
ATOM 754 CB VAL A 99 25.224 51.696 15.266 1.00 10.50 C
ATOM 755 CG1 VAL A 99 24.187 51.000 14.390 1.00 1.07 C
ATOM 756 CG2 VAL A 99 25.493 53.106 14.760 1.00 5.75 C
ATOM 757 N TYR A 100 24.868 49.639 17.648 1.00 4.04 N
ATOM 758 CA TYR A 100 24.288 48.429 18.115 1.00 4.03 C
ATOM 759 C TYR A 100 23.432 48.679 19.332 1.00 9.48 C
ATOM 760 O TYR A 100 22.359 48.097 19.542 1.00 7.58 O
ATOM 761 CB TYR A 100 25.418 47.487 18.576 1.00 8.68 C
ATOM 762 CG TYR A 100 26.220 46.782 17.533 1.00 5.18 C
ATOM 763 CD1 TYR A 100 25.626 46.145 16.444 1.00 1.00 C
ATOM 764 CD2 TYR A 100 27.595 46.707 17.696 1.00 8.46 C
ATOM 765 CE1 TYR A 100 26.443 45.489 15.507 1.00 1.00 C
ATOM 766 CE2 TYR A 100 28.416 46.044 16.772 1.00 8.40 C
ATOM 767 CZ TYR A 100 27.829 45.432 15.664 1.00 8.34 C
ATOM 768 OH TYR A 100 28.659 44.789 14.728 1.00 9.52 O
ATOM 769 N GLU A 101 23.918 49.570 20.206 1.00 8.87 N
ATOM 770 CA GLU A 101 23.160 49.849 21.439 1.00 4.16 C
ATOM 771 C GLU A 101 21.805 50.346 21.108 1.00 6.83 C
ATOM 772 O GLU A 101 20.789 50.098 21.750 1.00 11.10 O
ATOM 773 CB GLU A 101 23.938 50.989 22.119 1.00 14.73 C
ATOM 774 CG GLU A 101 23.849 51.037 23.634 1.00 30.30 C
ATOM 775 CD GLU A 101 23.949 52.438 24.217 1.00 39.35 C
ATOM 776 OE1 GLU A 101 25.161 52.941 24.200 1.00 34.86 O
ATOM 777 OE2 GLU A 101 23.001 53.001 24.741 1.00 44.25 O
ATOM 778 N GLN A 102 21.771 51.119 20.078 1.00 8.62 N
ATOM 779 CA GLN A 102 20.493 51.664 19.693 1.00 8.84 C
ATOM 780 C GLN A 102 19.570 50.725 18.983 1.00 12.63 C
ATOM 781 O GLN A 102 18.353 50.800 19.183 1.00 12.30 O
ATOM 782 CB GLN A 102 20.661 52.866 18.781 1.00 12.79 C
ATOM 783 CG GLN A 102 21.120 54.079 19.569 1.00 14.59 C
ATOM 784 CD GLN A 102 21.543 55.160 18.632 1.00 23.97 C
ATOM 785 OE1 GLN A 102 20.773 56.072 18.397 1.00 31.87 O
ATOM 786 NE2 GLN A 102 22.760 55.060 18.090 1.00 21.99 N
ATOM 787 N PHE A 103 20.112 49.849 18.157 1.00 9.34 N
ATOM 788 CA PHE A 103 19.216 48.927 17.476 1.00 8.31 C
ATOM 789 C PHE A 103 18.774 47.756 18.317 1.00 7.82 C
ATOM 790 O PHE A 103 17.729 47.119 18.048 1.00 13.29 O
ATOM 791 CB PHE A 103 19.917 48.397 16.207 1.00 7.08 C
ATOM 792 CG PHE A 103 19.671 49.467 15.177 1.00 10.00 C
ATOM 793 CD1 PHE A 103 18.507 49.421 14.398 1.00 10.45 C
ATOM 794 CD2 PHE A 103 20.558 50.532 15.012 1.00 6.00 C
ATOM 795 CE1 PHE A 103 18.215 50.419 13.463 1.00 13.29 C
ATOM 796 CE2 PHE A 103 20.273 51.518 14.073 1.00 2.89 C
ATOM 797 CZ PHE A 103 19.115 51.469 13.301 1.00 7.14 C
ATOM 798 N LEU A 104 19.612 47.436 19.328 1.00 7.11 N
ATOM 799 CA LEU A 104 19.333 46.282 20.237 1.00 9.49 C
ATOM 800 C LEU A 104 17.905 46.040 20.655 1.00 11.17 C
ATOM 801 O LEU A 104 17.367 44.945 20.460 1.00 8.35 O
ATOM 802 CB LEU A 104 20.350 46.117 21.394 1.00 11.62 C
ATOM 803 CG LEU A 104 20.241 44.858 22.305 1.00 20.39 C
ATOM 804 CD1 LEU A 104 20.630 43.582 21.597 1.00 16.07 C
ATOM 805 CD2 LEU A 104 21.229 44.989 23.462 1.00 24.67 C
ATOM 806 N PRO A 105 17.272 47.046 21.247 1.00 9.96 N
ATOM 807 CA PRO A 105 15.903 46.865 21.664 1.00 12.23 C
ATOM 808 C PRO A 105 14.933 46.582 20.537 1.00 12.23 C
ATOM 809 O PRO A 105 13.788 46.144 20.761 1.00 16.23 O
ATOM 810 CB PRO A 105 15.426 48.177 22.288 1.00 5.87 C
ATOM 811 CG PRO A 105 16.506 49.206 21.979 1.00 10.61 C
ATOM 812 CD PRO A 105 17.694 48.449 21.386 1.00 8.17 C
ATOM 813 N LYS A 106 15.356 46.869 19.323 1.00 12.73 N
ATOM 814 CA LYS A 106 14.438 46.640 18.234 1.00 15.31 C
ATOM 815 C LYS A 106 14.701 45.309 17.510 1.00 17.04 C
ATOM 816 O LYS A 106 13.892 44.786 16.736 1.00 15.96 O
ATOM 817 CB LYS A 106 14.713 47.748 17.254 1.00 15.88 C
ATOM 818 CG LYS A 106 14.104 49.080 17.675 1.00 22.81 C
ATOM 819 CD LYS A 106 14.088 50.052 16.524 1.00 29.83 C
ATOM 820 CE LYS A 106 12.765 50.746 16.439 1.00 33.06 C
ATOM 821 NZ LYS A 106 12.409 51.291 17.742 1.00 27.77 N
ATOM 822 N ALA A 107 15.876 44.799 17.774 1.00 12.39 N
ATOM 823 CA ALA A 107 16.295 43.582 17.145 1.00 12.75 C
ATOM 824 C ALA A 107 15.629 42.297 17.539 1.00 10.04 C
ATOM 825 O ALA A 107 15.230 42.086 18.703 1.00 9.34 O
ATOM 826 CB ALA A 107 17.803 43.453 17.297 1.00 10.21 C
ATOM 827 N GLN A 108 15.527 41.404 16.549 1.00 11.05 N
ATOM 828 CA GLN A 108 14.932 40.069 16.799 1.00 15.03 C
ATOM 829 C GLN A 108 15.973 38.917 16.708 1.00 13.70 C
ATOM 830 O GLN A 108 15.704 37.756 17.060 1.00 11.78 O
ATOM 831 CB GLN A 108 13.785 39.762 15.844 1.00 17.43 C
ATOM 832 CG GLN A 108 12.499 40.536 16.129 1.00 36.97 C
ATOM 833 CD GLN A 108 11.407 39.642 16.747 1.00 57.53 C
ATOM 834 OE1 GLN A 108 11.035 38.580 16.177 1.00 65.29 O
ATOM 835 NE2 GLN A 108 10.864 40.063 17.906 1.00 61.53 N
ATOM 836 N LYS A 109 17.173 39.208 16.222 1.00 6.60 N
ATOM 837 CA LYS A 109 18.151 38.175 16.100 1.00 1.00 C
ATOM 838 C LYS A 109 19.547 38.701 16.145 1.00 5.87 C
ATOM 839 O LYS A 109 19.747 39.837 15.704 1.00 5.66 O
ATOM 840 CB LYS A 109 18.115 37.846 14.670 1.00 8.55 C
ATOM 841 CG LYS A 109 17.428 36.609 14.322 1.00 21.19 C
ATOM 842 CD LYS A 109 18.189 36.038 13.138 1.00 19.72 C
ATOM 843 CE LYS A 109 17.396 34.967 12.439 1.00 24.74 C
ATOM 844 NZ LYS A 109 18.133 34.338 11.346 1.00 31.80 N
ATOM 845 N LEU A 110 20.490 37.877 16.665 1.00 1.97 N
ATOM 846 CA LEU A 110 21.847 38.286 16.758 1.00 1.00 C
ATOM 847 C LEU A 110 22.682 37.216 16.181 1.00 8.15 C
ATOM 848 O LEU A 110 22.455 36.032 16.386 1.00 6.67 O
ATOM 849 CB LEU A 110 22.283 38.373 18.228 1.00 7.61 C
ATOM 850 CG LEU A 110 21.405 39.259 19.118 1.00 9.21 C
ATOM 851 CD1 LEU A 110 21.987 39.302 20.548 1.00 4.87 C
ATOM 852 CD2 LEU A 110 21.322 40.659 18.542 1.00 8.66 C
ATOM 853 N TYR A 111 23.669 37.620 15.464 1.00 4.37 N
ATOM 854 CA TYR A 111 24.524 36.678 14.888 1.00 6.60 C
ATOM 855 C TYR A 111 25.845 37.057 15.508 1.00 8.91 C
ATOM 856 O TYR A 111 26.386 38.130 15.211 1.00 4.47 O
ATOM 857 CB TYR A 111 24.637 36.969 13.368 1.00 10.24 C
ATOM 858 CG TYR A 111 23.430 36.724 12.456 1.00 9.27 C
ATOM 859 CD1 TYR A 111 22.345 37.592 12.427 1.00 11.71 C
ATOM 860 CD2 TYR A 111 23.372 35.637 11.590 1.00 7.46 C
ATOM 861 CE1 TYR A 111 21.251 37.420 11.587 1.00 6.21 C
ATOM 862 CE2 TYR A 111 22.286 35.418 10.750 1.00 6.53 C
ATOM 863 CZ TYR A 111 21.223 36.319 10.732 1.00 14.20 C
ATOM 864 OH TYR A 111 20.115 36.124 9.913 1.00 16.73 O
ATOM 865 N LEU A 112 26.391 36.199 16.367 1.00 3.20 N
ATOM 866 CA LEU A 112 27.655 36.588 16.950 1.00 5.20 C
ATOM 867 C LEU A 112 28.769 35.610 16.732 1.00 5.91 C
ATOM 868 O LEU A 112 28.540 34.416 16.634 1.00 9.72 O
ATOM 869 CB LEU A 112 27.488 36.699 18.460 1.00 5.07 C
ATOM 870 CG LEU A 112 26.202 37.429 18.867 1.00 11.76 C
ATOM 871 CD1 LEU A 112 26.108 37.517 20.372 1.00 4.81 C
ATOM 872 CD2 LEU A 112 26.177 38.881 18.352 1.00 11.17 C
ATOM 873 N THR A 113 29.938 36.173 16.633 1.00 1.00 N
ATOM 874 CA THR A 113 31.112 35.401 16.489 1.00 4.39 C
ATOM 875 C THR A 113 31.862 35.655 17.794 1.00 13.56 C
ATOM 876 O THR A 113 32.266 36.798 18.084 1.00 6.81 O
ATOM 877 CB THR A 113 31.981 35.803 15.341 1.00 10.31 C
ATOM 878 OG1 THR A 113 31.296 35.651 14.090 1.00 10.83 O
ATOM 879 CG2 THR A 113 33.247 34.976 15.406 1.00 1.00 C
ATOM 880 N HIS A 114 32.044 34.592 18.608 1.00 12.04 N
ATOM 881 CA HIS A 114 32.758 34.763 19.865 1.00 6.47 C
ATOM 882 C HIS A 114 34.156 34.329 19.536 1.00 8.63 C
ATOM 883 O HIS A 114 34.423 33.181 19.126 1.00 8.99 O
ATOM 884 CB HIS A 114 32.090 33.872 21.018 1.00 2.94 C
ATOM 885 CG HIS A 114 30.665 34.161 21.308 1.00 1.00 C
ATOM 886 ND1 HIS A 114 30.256 35.299 22.012 1.00 10.41 N
ATOM 887 CD2 HIS A 114 29.541 33.478 20.932 1.00 1.00 C
ATOM 888 CE1 HIS A 114 28.872 35.249 22.095 1.00 9.70 C
ATOM 889 NE2 HIS A 114 28.426 34.148 21.411 1.00 6.60 N
ATOM 890 N ILE A 115 35.061 35.235 19.711 1.00 2.21 N
ATOM 891 CA ILE A 115 36.422 34.965 19.431 1.00 1.00 C
ATOM 892 C ILE A 115 37.259 34.798 20.699 1.00 13.33 C
ATOM 893 O ILE A 115 37.190 35.660 21.572 1.00 12.27 O
ATOM 894 CB ILE A 115 37.030 36.141 18.684 1.00 1.00 C
ATOM 895 CG1 ILE A 115 36.099 36.480 17.479 1.00 9.22 C
ATOM 896 CG2 ILE A 115 38.486 35.801 18.249 1.00 4.89 C
ATOM 897 CD1 ILE A 115 36.743 37.303 16.376 1.00 12.15 C
ATOM 898 N ASP A 116 38.051 33.731 20.760 1.00 12.94 N
ATOM 899 CA ASP A 116 38.895 33.485 21.915 1.00 11.35 C
ATOM 900 C ASP A 116 40.193 34.252 21.777 1.00 12.80 C
ATOM 901 O ASP A 116 41.275 33.722 21.540 1.00 15.09 O
ATOM 902 CB ASP A 116 39.109 31.980 22.162 1.00 11.03 C
ATOM 903 CG ASP A 116 37.808 31.302 22.598 1.00 21.60 C
ATOM 904 OD1 ASP A 116 37.045 31.806 23.403 1.00 25.68 O
ATOM 905 OD2 ASP A 116 37.527 30.154 21.986 1.00 14.13 O
ATOM 906 N ALA A 117 40.081 35.561 21.933 1.00 18.49 N
ATOM 907 CA ALA A 117 41.247 36.416 21.816 1.00 12.04 C
ATOM 908 C ALA A 117 41.220 37.442 22.926 1.00 12.20 C
ATOM 909 O ALA A 117 40.179 37.959 23.332 1.00 11.94 O
ATOM 910 CB ALA A 117 41.175 37.132 20.476 1.00 10.48 C
ATOM 911 N GLU A 118 42.367 37.716 23.445 1.00 12.34 N
ATOM 912 CA GLU A 118 42.362 38.685 24.480 1.00 15.77 C
ATOM 913 C GLU A 118 42.924 39.981 23.934 1.00 14.20 C
ATOM 914 O GLU A 118 44.118 40.088 23.643 1.00 20.91 O
ATOM 915 CB GLU A 118 43.194 38.197 25.681 1.00 32.31 C
ATOM 916 CG GLU A 118 43.350 39.384 26.648 1.00 51.92 C
ATOM 917 CD GLU A 118 44.505 39.313 27.610 1.00 64.86 C
ATOM 918 OE1 GLU A 118 45.355 38.315 27.376 1.00 67.24 O
ATOM 919 OE2 GLU A 118 44.632 40.140 28.500 1.00 67.94 O
ATOM 920 N VAL A 119 42.111 41.001 23.776 1.00 26.65 N
ATOM 921 CA VAL A 119 42.642 42.283 23.267 1.00 28.34 C
ATOM 922 C VAL A 119 42.015 43.461 23.999 1.00 27.08 C
ATOM 923 O VAL A 119 40.921 43.405 24.583 1.00 22.42 O
ATOM 924 CB VAL A 119 42.283 42.563 21.820 1.00 26.61 C
ATOM 925 CG1 VAL A 119 42.578 41.413 20.877 1.00 28.06 C
ATOM 926 CG2 VAL A 119 40.821 42.910 21.790 1.00 31.19 C
ATOM 927 N GLU A 120 42.703 44.548 23.950 1.00 34.99 N
ATOM 928 CA GLU A 120 42.138 45.677 24.581 1.00 46.81 C
ATOM 929 C GLU A 120 41.483 46.434 23.432 1.00 38.33 C
ATOM 930 O GLU A 120 41.924 46.346 22.287 1.00 31.81 O
ATOM 931 CB GLU A 120 43.195 46.479 25.378 1.00 67.75 C
ATOM 932 CG GLU A 120 42.771 46.835 26.829 1.00 82.69 C
ATOM 933 CD GLU A 120 43.958 46.954 27.742 1.00 92.90 C
ATOM 934 OE1 GLU A 120 44.750 46.051 27.921 1.00 94.78 O
ATOM 935 OE2 GLU A 120 44.124 48.162 28.216 1.00100.00 O
ATOM 936 N GLY A 121 40.423 47.160 23.731 1.00 38.34 N
ATOM 937 CA GLY A 121 39.725 47.929 22.731 1.00 38.53 C
ATOM 938 C GLY A 121 39.036 49.052 23.473 1.00 41.24 C
ATOM 939 O GLY A 121 39.081 49.089 24.718 1.00 40.59 O
ATOM 940 N ASP A 122 38.425 49.961 22.712 1.00 36.12 N
ATOM 941 CA ASP A 122 37.736 51.073 23.287 1.00 32.42 C
ATOM 942 C ASP A 122 36.269 50.913 23.182 1.00 29.21 C
ATOM 943 O ASP A 122 35.520 51.742 23.670 1.00 37.31 O
ATOM 944 CB ASP A 122 38.158 52.413 22.674 1.00 43.18 C
ATOM 945 CG ASP A 122 38.575 52.340 21.237 1.00 46.95 C
ATOM 946 OD1 ASP A 122 37.936 51.754 20.399 1.00 49.61 O
ATOM 947 OD2 ASP A 122 39.758 52.864 21.029 1.00 45.86 O
ATOM 948 N THR A 123 35.858 49.843 22.538 1.00 13.69 N
ATOM 949 CA THR A 123 34.445 49.624 22.367 1.00 15.14 C
ATOM 950 C THR A 123 34.096 48.206 22.604 1.00 9.20 C
ATOM 951 O THR A 123 34.840 47.279 22.229 1.00 13.40 O
ATOM 952 CB THR A 123 34.078 49.913 20.904 1.00 22.20 C
ATOM 953 OG1 THR A 123 34.991 50.867 20.434 1.00 22.58 O
ATOM 954 CG2 THR A 123 32.666 50.445 20.866 1.00 29.40 C
ATOM 955 N HIS A 124 32.938 48.131 23.174 1.00 6.33 N
ATOM 956 CA HIS A 124 32.274 46.971 23.600 1.00 13.13 C
ATOM 957 C HIS A 124 30.854 46.883 23.122 1.00 16.25 C
ATOM 958 O HIS A 124 30.111 47.894 22.942 1.00 19.83 O
ATOM 959 CB HIS A 124 32.144 47.089 25.128 1.00 16.22 C
ATOM 960 CG HIS A 124 33.487 47.258 25.707 1.00 18.25 C
ATOM 961 ND1 HIS A 124 34.145 46.159 26.283 1.00 18.29 N
ATOM 962 CD2 HIS A 124 34.296 48.366 25.775 1.00 12.92 C
ATOM 963 CE1 HIS A 124 35.349 46.614 26.688 1.00 15.69 C
ATOM 964 NE2 HIS A 124 35.471 47.917 26.385 1.00 13.62 N
ATOM 965 N PHE A 125 30.503 45.605 22.922 1.00 9.14 N
ATOM 966 CA PHE A 125 29.171 45.258 22.478 1.00 13.33 C
ATOM 967 C PHE A 125 28.264 45.571 23.661 1.00 16.39 C
ATOM 968 O PHE A 125 28.699 45.601 24.811 1.00 16.89 O
ATOM 969 CB PHE A 125 29.118 43.739 22.178 1.00 5.63 C
ATOM 970 CG PHE A 125 27.851 43.361 21.421 1.00 9.13 C
ATOM 971 CD1 PHE A 125 27.719 43.709 20.079 1.00 4.28 C
ATOM 972 CD2 PHE A 125 26.811 42.643 22.017 1.00 9.21 C
ATOM 973 CE1 PHE A 125 26.576 43.393 19.347 1.00 4.07 C
ATOM 974 CE2 PHE A 125 25.665 42.296 21.289 1.00 10.13 C
ATOM 975 CZ PHE A 125 25.548 42.665 19.949 1.00 5.84 C
ATOM 976 N PRO A 126 27.030 45.807 23.409 1.00 14.28 N
ATOM 977 CA PRO A 126 26.122 46.086 24.472 1.00 15.85 C
ATOM 978 C PRO A 126 25.839 44.889 25.368 1.00 23.77 C
ATOM 979 O PRO A 126 25.700 43.757 24.915 1.00 26.62 O
ATOM 980 CB PRO A 126 24.791 46.430 23.840 1.00 11.22 C
ATOM 981 CG PRO A 126 24.997 46.494 22.340 1.00 15.18 C
ATOM 982 CD PRO A 126 26.487 46.239 22.104 1.00 19.04 C
ATOM 983 N ASP A 127 25.731 45.151 26.662 1.00 31.61 N
ATOM 984 CA ASP A 127 25.449 44.088 27.591 1.00 39.15 C
ATOM 985 C ASP A 127 23.984 43.657 27.455 1.00 30.77 C
ATOM 986 O ASP A 127 23.093 44.324 27.964 1.00 35.03 O
ATOM 987 CB ASP A 127 25.740 44.512 29.067 1.00 48.67 C
ATOM 988 CG ASP A 127 25.909 43.329 30.044 1.00 61.28 C
ATOM 989 OD1 ASP A 127 26.311 42.212 29.701 1.00 68.06 O
ATOM 990 OD2 ASP A 127 25.611 43.614 31.308 1.00 62.01 O
ATOM 991 N TYR A 128 23.691 42.556 26.797 1.00 20.22 N
ATOM 992 CA TYR A 128 22.279 42.178 26.712 1.00 22.92 C
ATOM 993 C TYR A 128 21.835 41.125 27.706 1.00 27.05 C
ATOM 994 O TYR A 128 22.652 40.325 28.106 1.00 28.43 O
ATOM 995 CB TYR A 128 21.943 41.562 25.385 1.00 21.39 C
ATOM 996 CG TYR A 128 22.775 40.343 25.070 1.00 23.14 C
ATOM 997 CD1 TYR A 128 24.062 40.534 24.570 1.00 18.68 C
ATOM 998 CD2 TYR A 128 22.300 39.038 25.225 1.00 17.86 C
ATOM 999 CE1 TYR A 128 24.888 39.459 24.245 1.00 16.04 C
ATOM 1000 CE2 TYR A 128 23.103 37.951 24.869 1.00 19.13 C
ATOM 1001 CZ TYR A 128 24.399 38.164 24.394 1.00 16.10 C
ATOM 1002 OH TYR A 128 25.219 37.146 24.075 1.00 22.80 O
ATOM 1003 N GLU A 129 20.534 41.135 28.061 1.00 28.79 N
ATOM 1004 CA GLU A 129 19.888 40.185 28.996 1.00 23.64 C
ATOM 1005 C GLU A 129 19.843 38.790 28.354 1.00 15.42 C
ATOM 1006 O GLU A 129 19.101 38.504 27.455 1.00 17.52 O
ATOM 1007 CB GLU A 129 18.484 40.693 29.464 1.00 28.20 C
ATOM 1008 CG GLU A 129 17.699 39.738 30.430 1.00 42.29 C
ATOM 1009 CD GLU A 129 18.464 39.217 31.647 1.00 47.87 C
ATOM 1010 OE1 GLU A 129 18.955 39.961 32.519 1.00 50.07 O
ATOM 1011 OE2 GLU A 129 18.544 37.882 31.659 1.00 41.89 O
ATOM 1012 N PRO A 130 20.641 37.882 28.814 1.00 15.52 N
ATOM 1013 CA PRO A 130 20.638 36.597 28.219 1.00 16.13 C
ATOM 1014 C PRO A 130 19.379 35.844 28.397 1.00 21.34 C
ATOM 1015 O PRO A 130 19.194 34.802 27.756 1.00 25.05 O
ATOM 1016 CB PRO A 130 21.764 35.822 28.873 1.00 21.52 C
ATOM 1017 CG PRO A 130 22.043 36.546 30.163 1.00 19.75 C
ATOM 1018 CD PRO A 130 21.621 37.962 29.923 1.00 19.15 C
ATOM 1019 N ASP A 131 18.513 36.314 29.278 1.00 14.47 N
ATOM 1020 CA ASP A 131 17.282 35.574 29.436 1.00 11.93 C
ATOM 1021 C ASP A 131 16.344 35.889 28.267 1.00 18.74 C
ATOM 1022 O ASP A 131 15.468 35.116 27.914 1.00 16.01 O
ATOM 1023 CB ASP A 131 16.517 35.979 30.714 1.00 13.31 C
ATOM 1024 CG ASP A 131 17.115 35.382 31.970 1.00 17.76 C
ATOM 1025 OD1 ASP A 131 18.209 34.638 31.778 1.00 15.27 O
ATOM 1026 OD2 ASP A 131 16.657 35.639 33.061 1.00 15.84 O
ATOM 1027 N ASP A 132 16.493 37.064 27.666 1.00 19.59 N
ATOM 1028 CA ASP A 132 15.587 37.383 26.547 1.00 27.90 C
ATOM 1029 C ASP A 132 15.862 36.648 25.200 1.00 17.50 C
ATOM 1030 O ASP A 132 15.064 36.669 24.246 1.00 12.10 O
ATOM 1031 CB ASP A 132 15.666 38.915 26.278 1.00 33.78 C
ATOM 1032 CG ASP A 132 14.932 39.771 27.296 1.00 48.45 C
ATOM 1033 OD1 ASP A 132 14.250 39.325 28.208 1.00 50.02 O
ATOM 1034 OD2 ASP A 132 15.073 41.055 27.058 1.00 58.00 O
ATOM 1035 N TRP A 133 17.011 36.047 25.122 1.00 14.62 N
ATOM 1036 CA TRP A 133 17.448 35.372 23.921 1.00 11.77 C
ATOM 1037 C TRP A 133 17.618 33.865 23.954 1.00 19.49 C
ATOM 1038 O TRP A 133 18.058 33.244 24.925 1.00 22.54 O
ATOM 1039 CB TRP A 133 18.806 35.967 23.543 1.00 12.97 C
ATOM 1040 CG TRP A 133 18.702 37.438 23.412 1.00 16.01 C
ATOM 1041 CD1 TRP A 133 18.881 38.342 24.408 1.00 14.63 C
ATOM 1042 CD2 TRP A 133 18.320 38.186 22.207 1.00 19.22 C
ATOM 1043 NE1 TRP A 133 18.672 39.622 23.893 1.00 19.96 N
ATOM 1044 CE2 TRP A 133 18.316 39.558 22.563 1.00 18.41 C
ATOM 1045 CE3 TRP A 133 18.026 37.831 20.857 1.00 14.92 C
ATOM 1046 CZ2 TRP A 133 18.026 40.560 21.621 1.00 15.13 C
ATOM 1047 CZ3 TRP A 133 17.702 38.812 19.924 1.00 14.09 C
ATOM 1048 CH2 TRP A 133 17.717 40.172 20.308 1.00 10.59 C
ATOM 1049 N GLU A 134 17.293 33.248 22.848 1.00 12.50 N
ATOM 1050 CA GLU A 134 17.440 31.817 22.769 1.00 12.34 C
ATOM 1051 C GLU A 134 18.533 31.457 21.788 1.00 12.96 C
ATOM 1052 O GLU A 134 18.539 31.948 20.642 1.00 11.42 O
ATOM 1053 CB GLU A 134 16.125 31.162 22.384 1.00 17.27 C
ATOM 1054 CG GLU A 134 16.283 29.650 22.255 1.00 22.71 C
ATOM 1055 CD GLU A 134 15.045 29.032 21.727 1.00 36.51 C
ATOM 1056 OE1 GLU A 134 14.157 29.665 21.173 1.00 40.47 O
ATOM 1057 OE2 GLU A 134 15.013 27.755 21.995 1.00 46.14 O
ATOM 1058 N SER A 135 19.471 30.614 22.206 1.00 13.99 N
ATOM 1059 CA SER A 135 20.535 30.258 21.269 1.00 13.89 C
ATOM 1060 C SER A 135 20.100 29.173 20.320 1.00 16.99 C
ATOM 1061 O SER A 135 20.033 28.055 20.727 1.00 19.50 O
ATOM 1062 CB SER A 135 21.769 29.827 21.985 1.00 16.68 C
ATOM 1063 OG SER A 135 22.668 29.279 21.061 1.00 19.76 O
ATOM 1064 N VAL A 136 19.791 29.490 19.066 1.00 13.09 N
ATOM 1065 CA VAL A 136 19.322 28.507 18.093 1.00 12.44 C
ATOM 1066 C VAL A 136 20.385 27.916 17.178 1.00 19.55 C
ATOM 1067 O VAL A 136 20.143 26.970 16.392 1.00 22.04 O
ATOM 1068 CB VAL A 136 18.241 29.158 17.286 1.00 14.99 C
ATOM 1069 CG1 VAL A 136 17.198 29.683 18.266 1.00 5.25 C
ATOM 1070 CG2 VAL A 136 18.812 30.316 16.470 1.00 12.36 C
ATOM 1071 N PHE A 137 21.600 28.442 17.274 1.00 9.01 N
ATOM 1072 CA PHE A 137 22.622 27.905 16.428 1.00 4.74 C
ATOM 1073 C PHE A 137 23.933 28.220 17.031 1.00 11.30 C
ATOM 1074 O PHE A 137 24.152 29.359 17.456 1.00 17.35 O
ATOM 1075 CB PHE A 137 22.525 28.589 15.065 1.00 13.11 C
ATOM 1076 CG PHE A 137 23.686 28.111 14.273 1.00 17.10 C
ATOM 1077 CD1 PHE A 137 23.611 26.870 13.635 1.00 17.14 C
ATOM 1078 CD2 PHE A 137 24.848 28.876 14.195 1.00 11.47 C
ATOM 1079 CE1 PHE A 137 24.686 26.381 12.888 1.00 20.77 C
ATOM 1080 CE2 PHE A 137 25.928 28.414 13.442 1.00 15.79 C
ATOM 1081 CZ PHE A 137 25.837 27.176 12.794 1.00 24.09 C
ATOM 1082 N SER A 138 24.799 27.226 17.081 1.00 10.47 N
ATOM 1083 CA SER A 138 26.106 27.425 17.688 1.00 17.76 C
ATOM 1084 C SER A 138 27.100 26.403 17.184 1.00 18.18 C
ATOM 1085 O SER A 138 26.904 25.218 17.397 1.00 17.85 O
ATOM 1086 CB SER A 138 25.890 27.199 19.181 1.00 21.02 C
ATOM 1087 OG SER A 138 27.101 27.139 19.910 1.00 33.06 O
ATOM 1088 N GLU A 139 28.166 26.864 16.535 1.00 16.47 N
ATOM 1089 CA GLU A 139 29.213 26.009 15.984 1.00 9.59 C
ATOM 1090 C GLU A 139 30.600 26.538 16.360 1.00 12.66 C
ATOM 1091 O GLU A 139 31.024 27.642 15.992 1.00 10.17 O
ATOM 1092 CB GLU A 139 28.950 25.747 14.473 1.00 27.36 C
ATOM 1093 CG GLU A 139 29.730 26.688 13.540 1.00 39.04 C
ATOM 1094 CD GLU A 139 29.858 26.228 12.080 1.00 44.84 C
ATOM 1095 OE1 GLU A 139 29.294 25.174 11.711 1.00 54.46 O
ATOM 1096 OE2 GLU A 139 30.531 26.935 11.290 1.00 27.86 O
ATOM 1097 N PHE A 140 31.331 25.756 17.165 1.00 5.56 N
ATOM 1098 CA PHE A 140 32.661 26.104 17.632 1.00 9.94 C
ATOM 1099 C PHE A 140 33.741 25.579 16.674 1.00 16.00 C
ATOM 1100 O PHE A 140 33.601 24.530 16.095 1.00 26.09 O
ATOM 1101 CB PHE A 140 32.904 25.442 19.029 1.00 12.43 C
ATOM 1102 CG PHE A 140 34.332 25.557 19.523 1.00 18.51 C
ATOM 1103 CD1 PHE A 140 34.807 26.744 20.079 1.00 15.36 C
ATOM 1104 CD2 PHE A 140 35.221 24.489 19.426 1.00 22.23 C
ATOM 1105 CE1 PHE A 140 36.118 26.864 20.532 1.00 16.07 C
ATOM 1106 CE2 PHE A 140 36.539 24.584 19.873 1.00 20.51 C
ATOM 1107 CZ PHE A 140 36.991 25.780 20.429 1.00 21.35 C
ATOM 1108 N HIS A 141 34.824 26.290 16.558 1.00 10.78 N
ATOM 1109 CA HIS A 141 35.969 25.959 15.740 1.00 12.67 C
ATOM 1110 C HIS A 141 37.285 26.296 16.340 1.00 14.49 C
ATOM 1111 O HIS A 141 37.473 27.375 16.940 1.00 17.58 O
ATOM 1112 CB HIS A 141 36.029 26.773 14.459 1.00 13.32 C
ATOM 1113 CG HIS A 141 34.797 26.597 13.741 1.00 13.21 C
ATOM 1114 ND1 HIS A 141 34.706 25.663 12.744 1.00 18.93 N
ATOM 1115 CD2 HIS A 141 33.615 27.259 13.891 1.00 20.16 C
ATOM 1116 CE1 HIS A 141 33.453 25.764 12.286 1.00 24.87 C
ATOM 1117 NE2 HIS A 141 32.776 26.721 12.956 1.00 26.36 N
ATOM 1118 N ASP A 142 38.203 25.354 16.142 1.00 13.08 N
ATOM 1119 CA ASP A 142 39.574 25.483 16.604 1.00 15.29 C
ATOM 1120 C ASP A 142 40.331 26.332 15.625 1.00 17.78 C
ATOM 1121 O ASP A 142 40.031 26.395 14.431 1.00 22.90 O
ATOM 1122 CB ASP A 142 40.351 24.132 16.558 1.00 25.03 C
ATOM 1123 CG ASP A 142 40.050 23.318 17.750 1.00 28.16 C
ATOM 1124 OD1 ASP A 142 40.348 23.695 18.870 1.00 32.07 O
ATOM 1125 OD2 ASP A 142 39.216 22.349 17.484 1.00 31.39 O
ATOM 1126 N ALA A 143 41.336 26.971 16.161 1.00 18.57 N
ATOM 1127 CA ALA A 143 42.180 27.802 15.384 1.00 17.32 C
ATOM 1128 C ALA A 143 42.759 26.947 14.268 1.00 22.45 C
ATOM 1129 O ALA A 143 42.777 25.737 14.369 1.00 20.52 O
ATOM 1130 CB ALA A 143 43.341 28.041 16.297 1.00 11.56 C
ATOM 1131 N ASP A 144 43.241 27.555 13.220 1.00 20.72 N
ATOM 1132 CA ASP A 144 43.836 26.775 12.189 1.00 21.99 C
ATOM 1133 C ASP A 144 44.931 27.617 11.605 1.00 27.79 C
ATOM 1134 O ASP A 144 45.257 28.685 12.134 1.00 24.05 O
ATOM 1135 CB ASP A 144 42.902 26.162 11.152 1.00 23.41 C
ATOM 1136 CG ASP A 144 42.062 27.150 10.377 1.00 21.90 C
ATOM 1137 OD1 ASP A 144 42.464 28.239 10.034 1.00 21.63 O
ATOM 1138 OD2 ASP A 144 40.837 26.711 10.166 1.00 17.73 O
ATOM 1139 N ALA A 145 45.497 27.151 10.517 1.00 27.81 N
ATOM 1140 CA ALA A 145 46.564 27.885 9.871 1.00 23.39 C
ATOM 1141 C ALA A 145 46.098 29.203 9.328 1.00 18.91 C
ATOM 1142 O ALA A 145 46.914 30.069 9.084 1.00 17.54 O
ATOM 1143 CB ALA A 145 46.984 27.099 8.626 1.00 24.62 C
ATOM 1144 N GLN A 146 44.798 29.308 9.101 1.00 20.05 N
ATOM 1145 CA GLN A 146 44.253 30.546 8.544 1.00 25.85 C
ATOM 1146 C GLN A 146 43.732 31.500 9.603 1.00 25.80 C
ATOM 1147 O GLN A 146 43.877 32.729 9.473 1.00 25.61 O
ATOM 1148 CB GLN A 146 43.095 30.270 7.572 1.00 27.29 C
ATOM 1149 CG GLN A 146 43.444 29.299 6.448 1.00 43.01 C
ATOM 1150 CD GLN A 146 42.306 29.249 5.451 1.00 57.13 C
ATOM 1151 OE1 GLN A 146 41.984 28.178 4.894 1.00 63.89 O
ATOM 1152 NE2 GLN A 146 41.697 30.424 5.219 1.00 57.52 N
ATOM 1153 N ASN A 147 43.105 30.885 10.622 1.00 20.92 N
ATOM 1154 CA ASN A 147 42.524 31.559 11.751 1.00 15.91 C
ATOM 1155 C ASN A 147 43.387 31.295 12.952 1.00 13.85 C
ATOM 1156 O ASN A 147 43.493 30.186 13.409 1.00 15.38 O
ATOM 1157 CB ASN A 147 41.101 31.062 11.968 1.00 20.13 C
ATOM 1158 CG ASN A 147 40.272 31.233 10.694 1.00 18.53 C
ATOM 1159 OD1 ASN A 147 39.806 32.352 10.343 1.00 11.41 O
ATOM 1160 ND2 ASN A 147 40.302 30.174 9.881 1.00 7.11 N
ATOM 1161 N SER A 148 43.984 32.323 13.460 1.00 16.97 N
ATOM 1162 CA SER A 148 44.859 32.232 14.623 1.00 23.63 C
ATOM 1163 C SER A 148 44.150 32.144 15.982 1.00 25.02 C
ATOM 1164 O SER A 148 44.823 32.192 17.000 1.00 31.71 O
ATOM 1165 CB SER A 148 45.729 33.447 14.625 1.00 32.92 C
ATOM 1166 OG SER A 148 44.869 34.472 14.139 1.00 49.95 O
ATOM 1167 N HIS A 149 42.824 32.023 16.035 1.00 18.48 N
ATOM 1168 CA HIS A 149 42.143 31.932 17.312 1.00 13.97 C
ATOM 1169 C HIS A 149 40.997 31.026 17.175 1.00 17.69 C
ATOM 1170 O HIS A 149 40.458 30.843 16.106 1.00 20.70 O
ATOM 1171 CB HIS A 149 41.453 33.214 17.869 1.00 16.33 C
ATOM 1172 CG HIS A 149 42.384 34.329 18.155 1.00 12.93 C
ATOM 1173 ND1 HIS A 149 43.143 34.354 19.297 1.00 14.55 N
ATOM 1174 CD2 HIS A 149 42.662 35.416 17.427 1.00 8.06 C
ATOM 1175 CE1 HIS A 149 43.881 35.440 19.240 1.00 13.67 C
ATOM 1176 NE2 HIS A 149 43.621 36.083 18.128 1.00 11.93 N
ATOM 1177 N SER A 150 40.591 30.487 18.272 1.00 12.93 N
ATOM 1178 CA SER A 150 39.452 29.656 18.132 1.00 18.75 C
ATOM 1179 C SER A 150 38.249 30.575 18.139 1.00 14.34 C
ATOM 1180 O SER A 150 38.309 31.703 18.699 1.00 7.25 O
ATOM 1181 CB SER A 150 39.364 28.638 19.248 1.00 25.27 C
ATOM 1182 OG SER A 150 39.887 29.236 20.407 1.00 26.77 O
ATOM 1183 N TYR A 151 37.145 30.086 17.526 1.00 9.30 N
ATOM 1184 CA TYR A 151 35.960 30.937 17.518 1.00 11.07 C
ATOM 1185 C TYR A 151 34.725 30.101 17.444 1.00 14.01 C
ATOM 1186 O TYR A 151 34.768 28.911 17.077 1.00 16.06 O
ATOM 1187 CB TYR A 151 36.003 31.940 16.302 1.00 8.13 C
ATOM 1188 CG TYR A 151 36.241 31.141 15.059 1.00 6.63 C
ATOM 1189 CD1 TYR A 151 37.511 30.674 14.737 1.00 11.20 C
ATOM 1190 CD2 TYR A 151 35.166 30.845 14.235 1.00 6.10 C
ATOM 1191 CE1 TYR A 151 37.731 29.911 13.592 1.00 13.64 C
ATOM 1192 CE2 TYR A 151 35.373 30.087 13.097 1.00 10.73 C
ATOM 1193 CZ TYR A 151 36.641 29.647 12.774 1.00 9.84 C
ATOM 1194 OH TYR A 151 36.792 28.910 11.665 1.00 21.32 O
ATOM 1195 N CYS A 152 33.618 30.741 17.785 1.00 13.78 N
ATOM 1196 CA CYS A 152 32.345 30.084 17.770 1.00 8.02 C
ATOM 1197 C CYS A 152 31.315 30.988 17.115 1.00 13.15 C
ATOM 1198 O CYS A 152 31.210 32.181 17.459 1.00 15.15 O
ATOM 1199 CB CYS A 152 31.897 29.763 19.227 1.00 7.81 C
ATOM 1200 SG CYS A 152 30.294 28.889 19.455 1.00 23.20 S
ATOM 1201 N PHE A 153 30.549 30.415 16.162 1.00 7.50 N
ATOM 1202 CA PHE A 153 29.525 31.197 15.511 1.00 2.21 C
ATOM 1203 C PHE A 153 28.309 30.955 16.297 1.00 5.62 C
ATOM 1204 O PHE A 153 28.024 29.792 16.635 1.00 7.44 O
ATOM 1205 CB PHE A 153 29.239 30.751 14.062 1.00 2.17 C
ATOM 1206 CG PHE A 153 30.411 31.074 13.198 1.00 6.80 C
ATOM 1207 CD1 PHE A 153 30.926 32.373 13.147 1.00 7.08 C
ATOM 1208 CD2 PHE A 153 31.030 30.084 12.430 1.00 9.18 C
ATOM 1209 CE1 PHE A 153 32.042 32.683 12.363 1.00 7.28 C
ATOM 1210 CE2 PHE A 153 32.149 30.386 11.641 1.00 3.85 C
ATOM 1211 CZ PHE A 153 32.655 31.688 11.599 1.00 7.81 C
ATOM 1212 N GLU A 154 27.559 32.027 16.569 1.00 10.82 N
ATOM 1213 CA GLU A 154 26.365 31.747 17.315 1.00 10.05 C
ATOM 1214 C GLU A 154 25.190 32.562 16.831 1.00 12.98 C
ATOM 1215 O GLU A 154 25.374 33.764 16.495 1.00 9.60 O
ATOM 1216 CB GLU A 154 26.578 32.173 18.759 1.00 9.98 C
ATOM 1217 CG GLU A 154 25.339 31.740 19.582 1.00 9.37 C
ATOM 1218 CD GLU A 154 25.429 31.987 21.088 1.00 17.27 C
ATOM 1219 OE1 GLU A 154 26.249 32.946 21.481 1.00 9.37 O
ATOM 1220 OE2 GLU A 154 24.675 31.459 21.865 1.00 20.63 O
ATOM 1221 N ILE A 155 24.000 31.924 16.833 1.00 1.33 N
ATOM 1222 CA ILE A 155 22.808 32.679 16.425 1.00 7.13 C
ATOM 1223 C ILE A 155 21.762 32.645 17.498 1.00 10.92 C
ATOM 1224 O ILE A 155 21.347 31.544 17.945 1.00 9.46 O
ATOM 1225 CB ILE A 155 22.136 32.181 15.169 1.00 8.95 C
ATOM 1226 CG1 ILE A 155 23.129 32.191 14.001 1.00 1.03 C
ATOM 1227 CG2 ILE A 155 20.861 32.980 14.865 1.00 12.64 C
ATOM 1228 CD1 ILE A 155 22.439 31.692 12.702 1.00 11.01 C
ATOM 1229 N LEU A 156 21.318 33.858 17.892 1.00 3.94 N
ATOM 1230 CA LEU A 156 20.297 34.054 18.925 1.00 4.88 C
ATOM 1231 C LEU A 156 19.049 34.726 18.370 1.00 4.85 C
ATOM 1232 O LEU A 156 19.115 35.642 17.573 1.00 11.76 O
ATOM 1233 CB LEU A 156 20.727 35.026 20.099 1.00 2.28 C
ATOM 1234 CG LEU A 156 22.069 34.892 20.889 1.00 10.74 C
ATOM 1235 CD1 LEU A 156 21.902 34.347 22.281 1.00 17.61 C
ATOM 1236 CD2 LEU A 156 23.005 33.974 20.187 1.00 17.38 C
ATOM 1237 N GLU A 157 17.910 34.308 18.862 1.00 5.43 N
ATOM 1238 CA GLU A 157 16.639 34.854 18.486 1.00 10.71 C
ATOM 1239 C GLU A 157 15.877 35.293 19.712 1.00 19.30 C
ATOM 1240 O GLU A 157 15.698 34.495 20.643 1.00 17.02 O
ATOM 1241 CB GLU A 157 15.813 33.734 17.908 1.00 14.95 C
ATOM 1242 CG GLU A 157 16.543 33.151 16.690 1.00 22.36 C
ATOM 1243 CD GLU A 157 15.535 32.469 15.828 1.00 33.21 C
ATOM 1244 OE1 GLU A 157 14.553 31.919 16.295 1.00 41.40 O
ATOM 1245 OE2 GLU A 157 15.764 32.625 14.545 1.00 30.70 O
ATOM 1246 N ARG A 158 15.404 36.550 19.730 1.00 8.57 N
ATOM 1247 CA ARG A 158 14.638 37.058 20.899 1.00 12.83 C
ATOM 1248 C ARG A 158 13.423 36.169 21.326 1.00 13.88 C
ATOM 1249 O ARG A 158 12.618 35.748 20.524 1.00 16.46 O
ATOM 1250 CB ARG A 158 14.155 38.444 20.581 1.00 15.36 C
ATOM 1251 CG ARG A 158 13.420 39.027 21.752 1.00 20.00 C
ATOM 1252 CD ARG A 158 13.030 40.466 21.503 1.00 21.49 C
ATOM 1253 NE ARG A 158 14.100 41.362 21.111 1.00 23.14 N
ATOM 1254 CZ ARG A 158 14.867 42.040 21.985 1.00 25.02 C
ATOM 1255 NH1 ARG A 158 14.697 41.905 23.289 1.00 24.81 N
ATOM 1256 NH2 ARG A 158 15.834 42.867 21.547 1.00 27.24 N
ATOM 1257 N ARG A 159 13.239 35.866 22.587 1.00 9.91 N
ATOM 1258 CA ARG A 159 12.127 35.027 22.922 1.00 10.04 C
ATOM 1259 C ARG A 159 10.772 35.630 22.735 1.00 8.76 C
ATOM 1260 O ARG A 159 10.625 36.718 23.194 1.00 9.64 O
ATOM 1261 CB ARG A 159 12.244 34.474 24.315 1.00 13.93 C
ATOM 1262 CG ARG A 159 13.262 33.373 24.480 1.00 24.70 C
ATOM 1263 CD ARG A 159 13.401 33.051 25.969 1.00 29.51 C
ATOM 1264 NE ARG A 159 14.691 32.482 26.323 1.00 30.41 N
ATOM 1265 CZ ARG A 159 14.954 31.215 26.045 1.00 27.76 C
ATOM 1266 NH1 ARG A 159 14.034 30.441 25.437 1.00 20.59 N
ATOM 1267 NH2 ARG A 159 16.139 30.724 26.389 1.00 29.35 N
ATOM 1268 OXT ARG A 159 9.767 34.928 22.444 1.00 7.89 O
TER 1269 ARG A 159
HETATM 1270 CA CA A 300 8.936 32.829 21.403 1.00 16.88 CA
HETATM 1271 PA NAP A 164 29.750 53.799 15.038 1.00 15.09 P
HETATM 1272 O1A NAP A 164 28.649 53.272 15.873 1.00 10.21 O
HETATM 1273 O2A NAP A 164 30.269 53.213 13.782 1.00 11.32 O
HETATM 1274 O5B NAP A 164 29.416 55.302 14.632 1.00 23.21 O
HETATM 1275 C5B NAP A 164 28.634 56.198 15.464 1.00 20.11 C
HETATM 1276 C4B NAP A 164 28.348 57.492 14.729 1.00 21.18 C
HETATM 1277 O4B NAP A 164 27.204 57.249 13.886 1.00 13.27 O
HETATM 1278 C3B NAP A 164 27.877 58.682 15.553 1.00 23.70 C
HETATM 1279 O3B NAP A 164 28.980 59.520 15.788 1.00 30.36 O
HETATM 1280 C2B NAP A 164 26.960 59.497 14.647 1.00 23.08 C
HETATM 1281 O2B NAP A 164 27.754 60.179 13.697 1.00 27.55 O
HETATM 1282 C1B NAP A 164 26.362 58.377 13.803 1.00 14.57 C
HETATM 1283 N9A NAP A 164 25.151 58.070 14.545 1.00 16.35 N
HETATM 1284 C8A NAP A 164 25.019 57.128 15.497 1.00 11.53 C
HETATM 1285 N7A NAP A 164 23.774 57.117 15.965 1.00 15.67 N
HETATM 1286 C5A NAP A 164 23.096 58.122 15.275 1.00 19.16 C
HETATM 1287 C6A NAP A 164 21.749 58.610 15.294 1.00 20.79 C
HETATM 1288 N6A NAP A 164 20.758 58.167 16.113 1.00 22.12 N
HETATM 1289 N1A NAP A 164 21.455 59.611 14.449 1.00 14.60 N
HETATM 1290 C2A NAP A 164 22.395 60.078 13.665 1.00 17.51 C
HETATM 1291 N3A NAP A 164 23.664 59.706 13.559 1.00 19.47 N
HETATM 1292 C4A NAP A 164 23.952 58.732 14.403 1.00 15.79 C
HETATM 1293 O3 NAP A 164 31.000 54.149 15.997 1.00 16.41 O
HETATM 1294 PN NAP A 164 31.670 53.552 17.361 1.00 19.74 P
HETATM 1295 O1N NAP A 164 30.535 53.374 18.312 1.00 11.32 O
HETATM 1296 O2N NAP A 164 32.913 54.287 17.733 1.00 27.30 O
HETATM 1297 O5D NAP A 164 32.162 52.116 16.883 1.00 25.33 O
HETATM 1298 C5D NAP A 164 33.440 52.105 16.087 1.00 33.02 C
HETATM 1299 C4D NAP A 164 34.257 50.774 16.339 1.00 37.39 C
HETATM 1300 O4D NAP A 164 33.356 49.639 16.094 1.00 35.87 O
HETATM 1301 C3D NAP A 164 35.564 50.389 15.552 1.00 38.16 C
HETATM 1302 O3D NAP A 164 36.720 50.135 16.254 1.00 34.87 O
HETATM 1303 C2D NAP A 164 35.261 49.085 14.737 1.00 37.50 C
HETATM 1304 O2D NAP A 164 36.458 48.425 14.531 1.00 28.18 O
HETATM 1305 C1D NAP A 164 34.094 48.557 15.421 1.00 38.77 C
HETATM 1306 N1N NAP A 164 33.066 47.586 14.805 1.00 37.76 N
HETATM 1307 C2N NAP A 164 33.149 46.219 15.096 1.00 40.91 C
HETATM 1308 C3N NAP A 164 32.329 45.301 14.614 1.00 38.15 C
HETATM 1309 C7N NAP A 164 32.604 43.928 15.040 1.00 36.47 C
HETATM 1310 O7N NAP A 164 31.934 42.976 14.556 1.00 31.87 O
HETATM 1311 N7N NAP A 164 33.575 43.634 15.912 1.00 34.84 N
HETATM 1312 C4N NAP A 164 31.155 45.702 13.666 1.00 34.57 C
HETATM 1313 C5N NAP A 164 31.202 47.218 13.454 1.00 32.65 C
HETATM 1314 C6N NAP A 164 32.060 48.013 13.974 1.00 29.38 C
HETATM 1315 P2B NAP A 164 27.900 61.768 13.749 1.00 22.60 P
HETATM 1316 O1X NAP A 164 28.315 61.969 12.250 1.00 31.54 O
HETATM 1317 O2X NAP A 164 26.554 62.174 14.275 1.00 21.05 O
HETATM 1318 O3X NAP A 164 29.135 61.978 14.594 1.00 20.88 O
HETATM 1319 O HOH A 301 33.257 30.709 7.450 1.00 26.34 O
HETATM 1320 O HOH A 302 29.121 37.266 13.767 1.00 12.76 O
HETATM 1321 O HOH A 303 39.429 27.779 12.544 1.00 32.53 O
HETATM 1322 O HOH A 305 14.254 57.403 15.806 1.00 17.55 O
HETATM 1323 O HOH A 307 39.408 41.270 25.265 1.00 14.01 O
HETATM 1324 O HOH A 309 16.510 37.016 5.539 1.00 24.00 O
HETATM 1325 O HOH A 310 26.216 55.060 25.495 1.00 13.04 O
HETATM 1326 O HOH A 314 16.446 41.019 3.616 1.00 18.16 O
HETATM 1327 O HOH A 316 21.290 60.065 0.838 1.00 5.99 O
HETATM 1328 O HOH A 317 22.467 53.365 -1.394 1.00 41.56 O
HETATM 1329 O HOH A 319 18.486 42.153 25.683 1.00 6.79 O
HETATM 1330 O HOH A 320 28.863 48.124 26.574 1.00 41.42 O
HETATM 1331 O HOH A 321 36.559 39.827 12.274 1.00 24.95 O
HETATM 1332 O HOH A 322 12.365 44.105 8.175 1.00 47.07 O
HETATM 1333 O HOH A 323 23.163 61.840 7.670 1.00 13.65 O
HETATM 1334 O HOH A 324 31.275 48.567 -3.995 1.00 43.88 O
HETATM 1335 O HOH A 325 26.736 49.015 -2.762 1.00 32.59 O
HETATM 1336 O HOH A 326 35.980 53.917 -2.470 1.00 7.69 O
HETATM 1337 O HOH A 327 10.238 38.278 21.268 1.00 23.50 O
HETATM 1338 O HOH A 328 40.219 23.836 13.318 1.00 38.28 O
HETATM 1339 O HOH A 329 46.977 30.688 12.381 1.00 51.02 O
HETATM 1340 O HOH A 332 15.486 61.523 10.290 1.00 18.69 O
HETATM 1341 O HOH A 334 12.892 43.165 14.494 1.00 31.99 O
HETATM 1342 O HOH A 335 16.810 44.389 24.466 1.00 17.11 O
HETATM 1343 O HOH A 336 21.693 34.943 7.322 1.00 32.80 O
HETATM 1344 O HOH A 340 16.520 41.970 1.029 1.00 22.57 O
HETATM 1345 O HOH A 341 35.094 35.494 23.346 1.00 25.47 O
HETATM 1346 O HOH A 343 13.571 55.087 18.382 1.00 67.45 O
HETATM 1347 O HOH A 344 21.013 33.551 25.960 1.00 21.53 O
HETATM 1348 O HOH A 346 26.465 30.579 7.462 1.00 34.94 O
HETATM 1349 O HOH A 347 38.644 39.272 11.296 1.00 62.28 O
HETATM 1350 O HOH A 348 22.829 31.685 9.047 1.00 65.34 O
HETATM 1351 O HOH A 349 18.831 26.605 23.239 1.00 28.44 O
HETATM 1352 O HOH A 350 32.216 59.896 3.157 1.00 44.51 O
HETATM 1353 O HOH A 354 19.068 29.413 25.008 1.00 31.81 O
HETATM 1354 O HOH A 356 25.375 51.555 -1.686 1.00 37.26 O
HETATM 1355 O HOH A 357 26.063 23.424 18.954 1.00 19.30 O
HETATM 1356 O HOH A 358 40.539 23.519 10.320 1.00 45.54 O
HETATM 1357 O HOH A 361 32.415 45.964 9.328 1.00 36.96 O
HETATM 1358 O HOH A 362 31.041 41.972 12.205 1.00 18.01 O
HETATM 1359 O HOH A 363 31.068 38.783 12.243 1.00 24.96 O
HETATM 1360 O HOH A 364 31.859 41.296 2.671 1.00 30.19 O
HETATM 1361 O HOH A 365 40.076 48.926 5.905 1.00 54.69 O
HETATM 1362 O HOH A 368 40.222 51.022 8.870 1.00 57.01 O
HETATM 1363 O HOH A 370 42.446 30.825 20.435 1.00 7.74 O
HETATM 1364 O HOH A 371 31.572 50.548 24.000 1.00 47.12 O
HETATM 1365 O HOH A 372 12.334 37.867 25.072 1.00 15.12 O
HETATM 1366 O HOH A 373 34.905 30.642 21.202 1.00 22.06 O
HETATM 1367 O HOH A 374 19.642 50.220 24.167 1.00 38.61 O
HETATM 1368 O HOH A 375 32.014 37.088 23.508 1.00 40.99 O
HETATM 1369 O HOH A 377 10.567 53.590 10.387 1.00 22.28 O
HETATM 1370 O HOH A 378 27.853 63.326 7.867 1.00 31.26 O
HETATM 1371 O HOH A 379 16.589 38.601 3.355 1.00 17.20 O
HETATM 1372 O HOH A 380 11.748 49.087 6.850 1.00 26.67 O
HETATM 1373 O HOH A 381 12.580 40.596 25.070 1.00 21.68 O
HETATM 1374 O HOH A 382 22.253 63.733 3.355 1.00 42.68 O
HETATM 1375 O HOH A 383 15.451 38.244 33.334 1.00 47.41 O
HETATM 1376 O HOH A 384 34.481 36.974 28.294 1.00 60.16 O
HETATM 1377 O HOH A 385 32.305 43.904 10.270 1.00 52.47 O
HETATM 1378 O HOH A 386 37.612 22.744 14.058 1.00 30.98 O
HETATM 1379 O HOH A 387 17.656 35.238 8.073 1.00 32.38 O
HETATM 1380 O HOH A 388 18.939 34.720 5.169 1.00 39.36 O
HETATM 1381 O HOH A 389 22.812 36.509 3.216 1.00 34.23 O
HETATM 1382 O HOH A 390 10.703 32.838 20.062 1.00 28.72 O
HETATM 1383 O HOH A 391 10.543 31.335 22.282 1.00 23.39 O
HETATM 1384 O HOH A 392 20.843 62.385 5.473 1.00 31.04 O
HETATM 1385 O HOH A 393 22.797 62.876 1.123 1.00 43.62 O
HETATM 1386 O HOH A 395 16.279 54.082 -0.714 1.00 31.87 O
HETATM 1387 O HOH A 396 22.001 26.258 24.378 1.00 42.52 O
HETATM 1388 O HOH A 397 39.261 30.016 6.569 1.00 41.45 O
HETATM 1389 O HOH A 398 38.477 20.685 16.096 1.00 58.71 O
HETATM 1390 O HOH A 399 12.837 34.313 17.484 1.00 59.12 O
HETATM 1391 O HOH A 400 22.823 63.748 -3.131 1.00 36.62 O
HETATM 1392 O HOH A 401 11.205 46.048 8.520 1.00 42.69 O
HETATM 1393 O HOH A 402 32.904 41.227 10.831 1.00 32.94 O
HETATM 1394 O HOH A 403 35.350 52.572 26.455 1.00 46.31 O
HETATM 1395 O HOH A 404 31.681 41.533 0.098 1.00 48.09 O
HETATM 1396 O HOH A 405 12.331 40.292 29.474 1.00 34.38 O
HETATM 1397 O HOH A 406 25.869 33.994 23.959 1.00 36.71 O
HETATM 1398 O HOH A 407 20.668 31.433 24.684 1.00 48.24 O
HETATM 1399 O HOH A 408 12.823 60.090 12.809 1.00 51.40 O
HETATM 1400 O HOH A 409 26.245 62.381 -0.049 1.00 43.80 O
HETATM 1401 O HOH A 410 23.063 57.764 -4.192 1.00 54.28 O
HETATM 1402 O HOH A 411 22.792 59.377 -0.939 1.00 44.20 O
HETATM 1403 O HOH A 412 39.176 28.138 23.072 1.00 55.67 O
HETATM 1404 O HOH A 413 40.236 42.465 27.023 1.00 54.05 O
HETATM 1405 O HOH A 415 29.665 44.029 11.708 1.00 39.26 O
HETATM 1406 O HOH A 416 18.461 46.707 25.088 1.00 42.02 O
HETATM 1407 O HOH A 417 19.764 45.259 -0.520 1.00 31.48 O
HETATM 1408 O HOH A 418 17.926 32.364 27.620 1.00 49.37 O
HETATM 1409 O HOH A 419 11.850 42.180 26.966 1.00 39.39 O
HETATM 1410 O HOH A 420 35.126 28.262 9.641 1.00 36.25 O
HETATM 1411 O HOH A 421 11.354 42.471 18.823 1.00 35.90 O
HETATM 1412 O HOH A 422 32.990 43.322 29.730 1.00 47.33 O
HETATM 1413 O HOH A 423 26.520 63.408 -7.583 1.00 42.82 O
HETATM 1414 O HOH A 424 35.358 54.444 22.708 1.00 39.35 O
HETATM 1415 O HOH A 425 16.192 25.931 19.937 1.00 37.42 O
HETATM 1416 O HOH A 426 19.958 25.836 13.743 1.00 53.54 O
HETATM 1417 O HOH A 427 27.638 51.904 23.765 1.00 48.24 O
HETATM 1418 O HOH A 428 33.616 39.001 -0.972 1.00 56.93 O
HETATM 1419 O HOH A 429 37.501 52.444 18.251 1.00 56.39 O
HETATM 1420 O HOH A 430 42.168 50.230 21.609 1.00 27.30 O
HETATM 1421 O HOH A 431 43.900 46.175 20.995 1.00 55.29 O
HETATM 1422 O HOH A 432 35.999 55.120 17.370 1.00 43.50 O
HETATM 1423 O HOH A 433 37.974 56.586 5.290 1.00 48.81 O
HETATM 1424 O HOH A 434 33.538 47.577 0.907 1.00 43.42 O
HETATM 1425 O HOH A 435 27.931 56.110 23.799 1.00 51.14 O
HETATM 1426 O HOH A 436 30.837 51.604 -5.572 1.00 47.50 O
HETATM 1427 O HOH A 437 23.429 35.079 25.909 1.00 52.63 O
HETATM 1428 O HOH A 438 35.499 30.302 25.117 1.00 50.72 O
HETATM 1429 O HOH A 439 28.966 63.352 16.769 1.00 47.73 O
HETATM 1430 O HOH A 440 35.903 48.054 2.510 1.00 58.85 O
HETATM 1431 O HOH A 441 38.681 47.483 4.427 1.00 60.84 O
HETATM 1432 O HOH A 442 36.197 57.432 15.931 1.00 44.41 O
HETATM 1433 O HOH A 443 47.139 33.343 10.894 1.00 49.60 O
HETATM 1434 O HOH A 444 35.809 33.099 25.064 1.00 49.43 O
HETATM 1435 O HOH A 445 14.338 38.578 30.864 1.00 52.51 O
HETATM 1436 O HOH A 446 35.596 48.487 11.512 1.00 51.77 O
CONECT 1268 1270
CONECT 1270 1268 1382 1383
CONECT 1271 1272 1273 1274 1293
CONECT 1272 1271
CONECT 1273 1271
CONECT 1274 1271 1275
CONECT 1275 1274 1276
CONECT 1276 1275 1277 1278
CONECT 1277 1276 1282
CONECT 1278 1276 1279 1280
CONECT 1279 1278
CONECT 1280 1278 1281 1282
CONECT 1281 1280 1315
CONECT 1282 1277 1280 1283
CONECT 1283 1282 1284 1292
CONECT 1284 1283 1285
CONECT 1285 1284 1286
CONECT 1286 1285 1287 1292
CONECT 1287 1286 1288 1289
CONECT 1288 1287
CONECT 1289 1287 1290
CONECT 1290 1289 1291
CONECT 1291 1290 1292
CONECT 1292 1283 1286 1291
CONECT 1293 1271 1294
CONECT 1294 1293 1295 1296 1297
CONECT 1295 1294
CONECT 1296 1294
CONECT 1297 1294 1298
CONECT 1298 1297 1299
CONECT 1299 1298 1300 1301
CONECT 1300 1299 1305
CONECT 1301 1299 1302 1303
CONECT 1302 1301
CONECT 1303 1301 1304 1305
CONECT 1304 1303
CONECT 1305 1300 1303 1306
CONECT 1306 1305 1307 1314
CONECT 1307 1306 1308
CONECT 1308 1307 1309 1312
CONECT 1309 1308 1310 1311
CONECT 1310 1309
CONECT 1311 1309
CONECT 1312 1308 1313
CONECT 1313 1312 1314
CONECT 1314 1306 1313
CONECT 1315 1281 1316 1317 1318
CONECT 1316 1315
CONECT 1317 1315
CONECT 1318 1315
CONECT 1382 1270
CONECT 1383 1270
MASTER 299 0 2 4 8 0 9 6 1435 1 52 13
END
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