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PDBsum entry 3oup

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Lyase PDB id
3oup
Jmol
Contents
Protein chain
205 a.a.
Metals
_ZN
Waters ×63
HEADER    LYASE                                   15-SEP-10   3OUP
TITLE     CRYSTAL STRUCTURE OF THE GAMMA-CARBONIC ANHYDRASE W19N MUTANT FROM
TITLE    2 METHANOSARCINA THERMOPHILA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 35-247;
COMPND   5 SYNONYM: GAMMA-CARBONIC ANHYDRASE;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: METHANOSARCINA THERMOPHILA;
SOURCE   3 ORGANISM_TAXID: 2210;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    LYASE, LEFT-HANDED BETA HELIX, LIGANDS TO ZINC, TRIMER
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.F.DOMSIC,A.H.ROBBINS,R.MCKENNA
REVDAT   1   26-OCT-11 3OUP    0
JRNL        AUTH   J.F.DOMSIC,A.H.ROBBINS,R.MCKENNA
JRNL        TITL   CRYSTAL STRUCTURE OF THE GAMMA-CARBONIC ANHYDRASE W19N
JRNL        TITL 2 MUTANT FROM METHANOSARCINA THERMOPHILA
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_467)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : MLHL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.43
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 23543
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.138
REMARK   3   R VALUE            (WORKING SET) : 0.137
REMARK   3   FREE R VALUE                     : 0.158
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1200
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 26.4283 -  3.4305    0.97     2556   126  0.1357 0.1492
REMARK   3     2  3.4305 -  2.7238    1.00     2522   133  0.1446 0.1623
REMARK   3     3  2.7238 -  2.3797    1.00     2484   131  0.1412 0.1691
REMARK   3     4  2.3797 -  2.1622    1.00     2469   150  0.1208 0.1553
REMARK   3     5  2.1622 -  2.0073    1.00     2450   142  0.1202 0.1309
REMARK   3     6  2.0073 -  1.8890    1.00     2507   118  0.1140 0.1702
REMARK   3     7  1.8890 -  1.7944    1.00     2446   138  0.1304 0.1371
REMARK   3     8  1.7944 -  1.7163    1.00     2475   134  0.1636 0.2015
REMARK   3     9  1.7163 -  1.6503    0.99     2434   128  0.2136 0.2108
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : 0.39
REMARK   3   B_SOL              : 40.10
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.650
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.012           1660
REMARK   3   ANGLE     :  1.458           2282
REMARK   3   CHIRALITY :  0.109            260
REMARK   3   PLANARITY :  0.008            314
REMARK   3   DIHEDRAL  : 12.584            619
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3OUP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.0
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 RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : OSMIC
REMARK 200  OPTICS                         : MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23546
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 7.200
REMARK 200  R MERGE                    (I) : 0.03400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 32.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.24900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 8000 WITH 250 MM AMMONIUM
REMARK 280  SULFATE., PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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       5555   Z,X,Y
REMARK 290       6555   Z+1/2,-X+1/2,-Y
REMARK 290       7555   -Z+1/2,-X,Y+1/2
REMARK 290       8555   -Z,X+1/2,-Y+1/2
REMARK 290       9555   Y,Z,X
REMARK 290      10555   -Y,Z+1/2,-X+1/2
REMARK 290      11555   Y+1/2,-Z+1/2,-X
REMARK 290      12555   -Y+1/2,-Z,X+1/2
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       41.78150
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.78150
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.78150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.78150
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       41.78150
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.78150
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       41.78150
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       41.78150
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       41.78150
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       41.78150
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       41.78150
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       41.78150
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       41.78150
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       41.78150
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       41.78150
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       41.78150
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       41.78150
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       41.78150
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -142.0 KCAL/MOL
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 350   BIOMT1   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLN A     1
REMARK 465     GLU A     2
REMARK 465     ILE A     3
REMARK 465     THR A     4
REMARK 465     VAL A     5
REMARK 465     ASP A     6
REMARK 465     GLU A     7
REMARK 465     PHE A     8
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    ASN A  20       86.66   -153.48
REMARK 500    MET A  64      151.40     77.51
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                              ZN A 214  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 122   NE2
REMARK 620 2 HIS A  81   ND1 116.9
REMARK 620 3 HOH A 215   O   107.2 109.9
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 214
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OTM   RELATED DB: PDB
REMARK 900 SAME PROTEIN AS WILD-TYPE
REMARK 900 RELATED ID: 3OTZ   RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH W19A MUTATION
REMARK 900 RELATED ID: 3OU9   RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH W19F MUTATION
DBREF  3OUP A    1   213  UNP    P40881   CAH_METTE       36    248
SEQADV 3OUP ASN A   19  UNP  P40881    TRP    54 ENGINEERED MUTATION
SEQRES   1 A  213  GLN GLU ILE THR VAL ASP GLU PHE SER ASN ILE ARG GLU
SEQRES   2 A  213  ASN PRO VAL THR PRO ASN ASN PRO GLU PRO SER ALA PRO
SEQRES   3 A  213  VAL ILE ASP PRO THR ALA TYR ILE ASP PRO GLN ALA SER
SEQRES   4 A  213  VAL ILE GLY GLU VAL THR ILE GLY ALA ASN VAL MET VAL
SEQRES   5 A  213  SER PRO MET ALA SER ILE ARG SER ASP GLU GLY MET PRO
SEQRES   6 A  213  ILE PHE VAL GLY ASP ARG SER ASN VAL GLN ASP GLY VAL
SEQRES   7 A  213  VAL LEU HIS ALA LEU GLU THR ILE ASN GLU GLU GLY GLU
SEQRES   8 A  213  PRO ILE GLU ASP ASN ILE VAL GLU VAL ASP GLY LYS GLU
SEQRES   9 A  213  TYR ALA VAL TYR ILE GLY ASN ASN VAL SER LEU ALA HIS
SEQRES  10 A  213  GLN SER GLN VAL HIS GLY PRO ALA ALA VAL GLY ASP ASP
SEQRES  11 A  213  THR PHE ILE GLY MET GLN ALA PHE VAL PHE LYS SER LYS
SEQRES  12 A  213  VAL GLY ASN ASN CYS VAL LEU GLU PRO ARG SER ALA ALA
SEQRES  13 A  213  ILE GLY VAL THR ILE PRO ASP GLY ARG TYR ILE PRO ALA
SEQRES  14 A  213  GLY MET VAL VAL THR SER GLN ALA GLU ALA ASP LYS LEU
SEQRES  15 A  213  PRO GLU VAL THR ASP ASP TYR ALA TYR SER HIS THR ASN
SEQRES  16 A  213  GLU ALA VAL VAL TYR VAL ASN VAL HIS LEU ALA GLU GLY
SEQRES  17 A  213  TYR LYS GLU THR SER
HET     ZN  A 214       1
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *63(H2 O)
HELIX    1   1 ILE A   93  ILE A   97  5                                   5
HELIX    2   2 SER A  175  LYS A  181  1                                   7
HELIX    3   3 HIS A  193  GLU A  211  1                                  19
SHEET    1   A 7 ILE A  11  ARG A  12  0
SHEET    2   A 7 SER A  39  GLY A  42  1  O  GLY A  42   N  ARG A  12
SHEET    3   A 7 SER A  57  SER A  60  1  O  ILE A  58   N  SER A  39
SHEET    4   A 7 VAL A  79  ALA A  82  1  O  LEU A  80   N  ARG A  59
SHEET    5   A 7 GLN A 120  VAL A 127  1  O  GLY A 123   N  HIS A  81
SHEET    6   A 7 PHE A 138  VAL A 144  1  O  VAL A 139   N  HIS A 122
SHEET    7   A 7 THR A 160  ILE A 161  1  O  ILE A 161   N  LYS A 143
SHEET    1   B 8 VAL A  27  ILE A  28  0
SHEET    2   B 8 VAL A  44  ILE A  46  1  O  VAL A  44   N  VAL A  27
SHEET    3   B 8 ILE A  66  VAL A  68  1  O  VAL A  68   N  THR A  45
SHEET    4   B 8 VAL A 107  ILE A 109  1  O  VAL A 107   N  PHE A  67
SHEET    5   B 8 GLN A 120  VAL A 127  1  O  VAL A 127   N  TYR A 108
SHEET    6   B 8 PHE A 138  VAL A 144  1  O  VAL A 139   N  HIS A 122
SHEET    7   B 8 ALA A 155  ILE A 157  1  O  ALA A 156   N  PHE A 138
SHEET    8   B 8 VAL A 172  VAL A 173  1  O  VAL A 173   N  ALA A 155
SHEET    1   C 7 TYR A  33  ILE A  34  0
SHEET    2   C 7 MET A  51  VAL A  52  1  O  VAL A  52   N  TYR A  33
SHEET    3   C 7 ASN A  73  VAL A  74  1  O  VAL A  74   N  MET A  51
SHEET    4   C 7 SER A 114  LEU A 115  1  O  LEU A 115   N  ASN A  73
SHEET    5   C 7 PHE A 132  ILE A 133  1  O  ILE A 133   N  SER A 114
SHEET    6   C 7 VAL A 149  LEU A 150  1  O  LEU A 150   N  PHE A 132
SHEET    7   C 7 TYR A 166  ILE A 167  1  O  ILE A 167   N  VAL A 149
SHEET    1   D 2 VAL A  98  VAL A 100  0
SHEET    2   D 2 LYS A 103  TYR A 105 -1  O  TYR A 105   N  VAL A  98
LINK         NE2 HIS A 122                ZN    ZN A 214     1555   1555  2.03
LINK         ND1 HIS A  81                ZN    ZN A 214     1555   1555  2.04
LINK        ZN    ZN A 214                 O   HOH A 215     1555   1555  2.23
CISPEP   1 GLY A  123    PRO A  124          0         0.28
SITE     1 AC1  4 HIS A  81  HIS A 117  HIS A 122  HOH A 215
CRYST1   83.563   83.563   83.563  90.00  90.00  90.00 P 21 3       12
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      0.011967  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011967  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011967        0.00000
      
PROCHECK
Go to PROCHECK summary
 References