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PDBsum entry 2nn1

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2nn1
Jmol
Contents
Protein chains
258 a.a.
Ligands
M28 ×2
TRS
Metals
_ZN ×2
_NA
Waters ×525
HEADER    LYASE                                   23-OCT-06   2NN1
TITLE     STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE I, CARBONATE DEHYDRATASE I, CA-
COMPND   5 I;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 CODON PLUS(DE3)RIL;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET20B
KEYWDS    ZINC METALLOENZYME, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.W.CHRISTIANSON,K.M.JUDE
REVDAT   3   24-FEB-09 2NN1    1       VERSN
REVDAT   2   08-MAY-07 2NN1    1       JRNL
REVDAT   1   24-APR-07 2NN1    0
JRNL        AUTH   D.K.SRIVASTAVA,K.M.JUDE,A.L.BANERJEE,M.HALDAR,
JRNL        AUTH 2 S.MANOKARAN,J.KOOREN,S.MALLIK,D.W.CHRISTIANSON
JRNL        TITL   STRUCTURAL ANALYSIS OF CHARGE DISCRIMINATION IN
JRNL        TITL 2 THE BINDING OF INHIBITORS TO HUMAN CARBONIC
JRNL        TITL 3 ANHYDRASES I AND II
JRNL        REF    J.AM.CHEM.SOC.                V. 129  5528 2007
JRNL        REFN                   ISSN 0002-7863
JRNL        PMID   17407288
JRNL        DOI    10.1021/JA068359W
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.63
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 66298.062
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.7
REMARK   3   NUMBER OF REFLECTIONS             : 61854
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.222
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 2516
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9199
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780
REMARK   3   BIN FREE R VALUE                    : 0.2950
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.10
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 398
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4069
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 41
REMARK   3   SOLVENT ATOMS            : 525
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.62
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.26000
REMARK   3    B22 (A**2) : 6.58000
REMARK   3    B33 (A**2) : -4.32000
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  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19
REMARK   3   ESD FROM SIGMAA              (A) : 0.16
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.83
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.060 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.680 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.860 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.870 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.32
REMARK   3   BSOL        : 39.96
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : MH128.PAR
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : CCN.PAR
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : MH128.TOP
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : CCN.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2NN1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-06.
REMARK 100 THE RCSB ID CODE IS RCSB040061.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 5.0.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.4
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65427
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.630
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5
REMARK 200  DATA REDUNDANCY                : 6.000
REMARK 200  R MERGE                    (I) : 0.09900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.6000
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     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.45100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.100
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: PDB ENTRY 2FOY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NACL, HEPES, TRIS, PH
REMARK 280  7.0, VAPOR DIFFUSION, TEMPERATURE 277K
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       31.21050
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.98250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.90900
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.98250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.21050
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.90900
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THERE ARE 2 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 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     ALA A     1
REMARK 465     SER A     2
REMARK 465     ALA B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
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    LYS A  57      -59.08   -126.53
REMARK 500    SER A  65     -166.66   -170.69
REMARK 500    ASN A  75       39.62    -95.18
REMARK 500    ASN A 124       92.61    -69.26
REMARK 500    ASN A 244       32.34   -159.02
REMARK 500    LYS B  57      -62.09   -126.04
REMARK 500    SER B  65     -163.08   -171.62
REMARK 500    ASN B  75       40.01    -94.41
REMARK 500    ASN B 244       35.51   -156.92
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 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  96   NE2
REMARK 620 2 HIS A 119   ND1 102.3
REMARK 620 3 HIS A  94   NE2 106.0 110.1
REMARK 620 4 M28 A 311   N3  105.2 116.0 115.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 302  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  96   NE2
REMARK 620 2 M28 B 312   N3  105.8
REMARK 620 3 HIS B  94   NE2 108.1 112.7
REMARK 620 4 HIS B 119   ND1 102.3 115.3 111.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA B 351  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 688   O
REMARK 620 2 HOH B 468   O   161.4
REMARK 620 3 HOH B 548   O    92.8  83.4
REMARK 620 4 HOH B 469   O    90.9  94.5 174.3
REMARK 620 5 SER B 259   O    98.5  97.6  71.7 103.5
REMARK 620 6 HOH B 665   O    77.0  86.1 103.2  81.8 173.2
REMARK 620 N                    1     2     3     4     5
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 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 302
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 351
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M28 A 311
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M28 B 312
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 341
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NMX   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NN7   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NNG   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE I
REMARK 900 RELATED ID: 2NNO   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NNS   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
REMARK 900 RELATED ID: 2NNV   RELATED DB: PDB
REMARK 900 STRUCTURE OF INHIBITOR BINDING TO CARBONIC ANHYDRASE II
DBREF  2NN1 A    1   260  UNP    P00915   CAH1_HUMAN       1    260
DBREF  2NN1 B    1   260  UNP    P00915   CAH1_HUMAN       1    260
SEQRES   1 A  260  ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES   2 A  260  GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES   3 A  260  ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES   4 A  260  HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES   5 A  260  PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES   6 A  260  PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 A  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 A  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 A  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 A  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 A  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 A  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 A  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 A  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 A  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 A  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 A  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
SEQRES   1 B  260  ALA SER PRO ASP TRP GLY TYR ASP ASP LYS ASN GLY PRO
SEQRES   2 B  260  GLU GLN TRP SER LYS LEU TYR PRO ILE ALA ASN GLY ASN
SEQRES   3 B  260  ASN GLN SER PRO VAL ASP ILE LYS THR SER GLU THR LYS
SEQRES   4 B  260  HIS ASP THR SER LEU LYS PRO ILE SER VAL SER TYR ASN
SEQRES   5 B  260  PRO ALA THR ALA LYS GLU ILE ILE ASN VAL GLY HIS SER
SEQRES   6 B  260  PHE HIS VAL ASN PHE GLU ASP ASN ASP ASN ARG SER VAL
SEQRES   7 B  260  LEU LYS GLY GLY PRO PHE SER ASP SER TYR ARG LEU PHE
SEQRES   8 B  260  GLN PHE HIS PHE HIS TRP GLY SER THR ASN GLU HIS GLY
SEQRES   9 B  260  SER GLU HIS THR VAL ASP GLY VAL LYS TYR SER ALA GLU
SEQRES  10 B  260  LEU HIS VAL ALA HIS TRP ASN SER ALA LYS TYR SER SER
SEQRES  11 B  260  LEU ALA GLU ALA ALA SER LYS ALA ASP GLY LEU ALA VAL
SEQRES  12 B  260  ILE GLY VAL LEU MET LYS VAL GLY GLU ALA ASN PRO LYS
SEQRES  13 B  260  LEU GLN LYS VAL LEU ASP ALA LEU GLN ALA ILE LYS THR
SEQRES  14 B  260  LYS GLY LYS ARG ALA PRO PHE THR ASN PHE ASP PRO SER
SEQRES  15 B  260  THR LEU LEU PRO SER SER LEU ASP PHE TRP THR TYR PRO
SEQRES  16 B  260  GLY SER LEU THR HIS PRO PRO LEU TYR GLU SER VAL THR
SEQRES  17 B  260  TRP ILE ILE CYS LYS GLU SER ILE SER VAL SER SER GLU
SEQRES  18 B  260  GLN LEU ALA GLN PHE ARG SER LEU LEU SER ASN VAL GLU
SEQRES  19 B  260  GLY ASP ASN ALA VAL PRO MET GLN HIS ASN ASN ARG PRO
SEQRES  20 B  260  THR GLN PRO LEU LYS GLY ARG THR VAL ARG ALA SER PHE
HET     ZN  A 301       1
HET     ZN  B 302       1
HET     NA  B 351       1
HET    M28  A 311      15
HET    M28  B 312      15
HET    TRS  A 341       8
HETNAM      ZN ZINC ION
HETNAM      NA SODIUM ION
HETNAM     M28 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN     M28 P-CARBOXYETHYLBENZENESULFONAMIDE
HETSYN     TRS TRIS BUFFER
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5   NA    NA 1+
FORMUL   6  M28    2(C9 H11 N O4 S)
FORMUL   8  TRS    C4 H12 N O3 1+
FORMUL   9  HOH   *525(H2 O)
HELIX    1   1 GLY A   12  LEU A   19  5                                   8
HELIX    2   2 TYR A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A   34  THR A   38  5                                   5
HELIX    4   4 ASN A   52  ALA A   54  5                                   3
HELIX    5   5 SER A  130  ALA A  135  1                                   6
HELIX    6   6 ASN A  154  LYS A  156  5                                   3
HELIX    7   7 LEU A  157  LEU A  164  1                                   8
HELIX    8   8 GLN A  165  ILE A  167  5                                   3
HELIX    9   9 ASP A  180  LEU A  185  5                                   6
HELIX   10  10 SER A  219  SER A  228  1                                  10
HELIX   11  11 GLY B   12  LEU B   19  5                                   8
HELIX   12  12 TYR B   20  GLY B   25  5                                   6
HELIX   13  13 LYS B   34  THR B   38  5                                   5
HELIX   14  14 ASN B   52  ALA B   54  5                                   3
HELIX   15  15 SER B  130  ALA B  135  1                                   6
HELIX   16  16 ASN B  154  LYS B  156  5                                   3
HELIX   17  17 LEU B  157  LEU B  164  1                                   8
HELIX   18  18 GLN B  165  ILE B  167  5                                   3
HELIX   19  19 ASP B  180  LEU B  185  5                                   6
HELIX   20  20 SER B  219  SER B  228  1                                  10
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  HIS A  40  0
SHEET    2   B10 ARG A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 PHE A 191  GLY A 196 -1  N  THR A 193   O  ARG A 257
SHEET    4   B10 VAL A 207  CYS A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  ALA A 116   O  MET A 148
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  PHE A  70   O  PHE A  91
SHEET    9   B10 ALA A  56  ASN A  61 -1  N  GLU A  58   O  ASN A  69
SHEET   10   B10 ARG A 173  PRO A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 ILE A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  LYS A  80   N  SER A  48
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  MET A 148   N  ALA A 116
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  LYS A 149
SHEET    1   D 2 ASP B  32  ILE B  33  0
SHEET    2   D 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   E10 LYS B  39  HIS B  40  0
SHEET    2   E10 ARG B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   E10 PHE B 191  GLY B 196 -1  N  THR B 193   O  ARG B 257
SHEET    4   E10 VAL B 207  CYS B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   E10 LEU B 141  VAL B 150  1  N  GLY B 145   O  ILE B 210
SHEET    6   E10 ALA B 116  TRP B 123 -1  N  LEU B 118   O  VAL B 146
SHEET    7   E10 TYR B  88  TRP B  97 -1  N  ARG B  89   O  TRP B 123
SHEET    8   E10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET    9   E10 ALA B  56  ASN B  61 -1  N  GLU B  58   O  ASN B  69
SHEET   10   E10 ARG B 173  PRO B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   F 6 ILE B  47  SER B  50  0
SHEET    2   F 6 VAL B  78  GLY B  81 -1  O  LYS B  80   N  SER B  48
SHEET    3   F 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   F 6 ALA B 116  TRP B 123 -1  O  TRP B 123   N  ARG B  89
SHEET    5   F 6 LEU B 141  VAL B 150 -1  O  VAL B 146   N  LEU B 118
SHEET    6   F 6 ILE B 216  VAL B 218  1  O  ILE B 216   N  LYS B 149
LINK        ZN    ZN A 301                 NE2 HIS A  96     1555   1555  2.18
LINK        ZN    ZN A 301                 ND1 HIS A 119     1555   1555  2.11
LINK        ZN    ZN A 301                 NE2 HIS A  94     1555   1555  2.10
LINK        ZN    ZN A 301                 N3  M28 A 311     1555   1555  2.21
LINK        ZN    ZN B 302                 NE2 HIS B  96     1555   1555  2.16
LINK        ZN    ZN B 302                 N3  M28 B 312     1555   1555  2.14
LINK        ZN    ZN B 302                 NE2 HIS B  94     1555   1555  2.12
LINK        ZN    ZN B 302                 ND1 HIS B 119     1555   1555  2.11
LINK        NA    NA B 351                 O   HOH B 688     1555   1555  2.53
LINK        NA    NA B 351                 O   HOH B 468     1555   1555  2.43
LINK        NA    NA B 351                 O   HOH B 548     1555   1555  2.56
LINK        NA    NA B 351                 O   HOH B 469     1555   1555  2.34
LINK        NA    NA B 351                 O   SER B 259     1555   1555  2.28
LINK        NA    NA B 351                 O   HOH B 665     1555   1555  2.63
CISPEP   1 SER A   29    PRO A   30          0        -0.01
CISPEP   2 PRO A  201    PRO A  202          0         0.75
CISPEP   3 SER B   29    PRO B   30          0         0.21
CISPEP   4 PRO B  201    PRO B  202          0         0.21
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  M28 A 311
SITE     1 AC2  4 HIS B  94  HIS B  96  HIS B 119  M28 B 312
SITE     1 AC3  6 SER B 259  HOH B 468  HOH B 469  HOH B 548
SITE     2 AC3  6 HOH B 665  HOH B 688
SITE     1 AC4  9 HIS A  94  HIS A  96  HIS A 119  VAL A 143
SITE     2 AC4  9 LEU A 198  THR A 199  HIS A 200  TRP A 209
SITE     3 AC4  9  ZN A 301
SITE     1 AC5  9 GLN B  92  HIS B  94  HIS B  96  HIS B 119
SITE     2 AC5  9 LEU B 198  THR B 199  HIS B 200  TRP B 209
SITE     3 AC5  9  ZN B 302
SITE     1 AC6  4 ALA A 135  TYR A 204  ALA B 135  TYR B 204
CRYST1   62.421   71.818  121.965  90.00  90.00  90.00 P 21 21 21    8
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      0.016020  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013924  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008199        0.00000
      
PROCHECK
Go to PROCHECK summary
 References