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PDBsum entry 3s71

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Lyase PDB id
3s71
Jmol
Contents
Protein chain
258 a.a.
Ligands
EVD ×2
Metals
_ZN
Waters ×367
HEADER    LYASE                                   26-MAY-11   3S71
TITLE     THE ORIGIN OF THE HYDROPHOBIC EFFECT IN THE MOLECULAR RECOGNITION OF
TITLE    2 ARYLSULFONAMIDES BY CARBONIC ANHYDRASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: B;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND   5 CARBONIC ANHYDRASE II, CA-II;
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: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    ALPHA BETA, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.W.SNYDER,A.HEROUX,G.W.WHITESIDES
REVDAT   2   21-DEC-11 3S71    1       JRNL
REVDAT   1   19-OCT-11 3S71    0
JRNL        AUTH   P.W.SNYDER,J.MECINOVIC,D.T.MOUSTAKAS,S.W.THOMAS,M.HARDER,
JRNL        AUTH 2 E.T.MACK,M.R.LOCKETT,A.HEROUX,W.SHERMAN,G.M.WHITESIDES
JRNL        TITL   MECHANISM OF THE HYDROPHOBIC EFFECT IN THE BIOMOLECULAR
JRNL        TITL 2 RECOGNITION OF ARYLSULFONAMIDES BY CARBONIC ANHYDRASE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 17889 2011
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   22011572
JRNL        DOI    10.1073/PNAS.1114107108
REMARK   2
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.64
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.9
REMARK   3   NUMBER OF REFLECTIONS             : 61057
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 + TEST SET) : 0.158
REMARK   3   R VALUE            (WORKING SET) : 0.157
REMARK   3   FREE R VALUE                     : 0.181
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3088
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.25
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.28
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2107
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 44.62
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920
REMARK   3   BIN FREE R VALUE SET COUNT          : 104
REMARK   3   BIN FREE R VALUE                    : 0.3270
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2054
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 27
REMARK   3   SOLVENT ATOMS            : 367
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.82
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  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.050
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.028
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.615
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2263 ; 0.029 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3102 ; 2.640 ; 1.961
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   287 ; 6.793 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;36.410 ;24.717
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   368 ;12.427 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;24.504 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   320 ; 0.161 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1784 ; 0.017 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1362 ; 1.389 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2221 ; 2.252 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   901 ; 2.945 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   874 ; 4.454 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES      : REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3S71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB065841.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X25
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61155
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : 0.05100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.27
REMARK 200  COMPLETENESS FOR SHELL     (%) : 41.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500
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   (%): 41.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-CL, 1.15 M SODIUM CITRATE,
REMARK 280  PH 7.8, VAPOR DIFFUSION, TEMPERATURE 277K, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.69800
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS B 261    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OE2  GLU B    26     O    HOH B   276              1.94
REMARK 500   OE2  GLU B   214     O    HOH B   538              1.95
REMARK 500   OD1  ASP B   165     O    HOH B   291              1.96
REMARK 500   O    HOH B   579     O    HOH B   628              1.97
REMARK 500   O    HOH B   288     O    HOH B   334              1.99
REMARK 500   O    HOH B   318     O    HOH B   321              2.06
REMARK 500   O    HOH B   299     O    HOH B   326              2.11
REMARK 500   O    HOH B   572     O    HOH B   587              2.13
REMARK 500   N    HIS B     3     O    HOH B   460              2.17
REMARK 500   CE1  HIS B     3     O    HOH B   344              2.18
REMARK 500   O    HOH B   541     O    HOH B   584              2.19
REMARK 500
REMARK 500 REMARK: NULL
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 B  14   CD    GLU B  14   OE2     0.073
REMARK 500    TYR B  40   CB    TYR B  40   CG     -0.109
REMARK 500    VAL B 161   CA    VAL B 161   CB      0.144
REMARK 500    GLU B 214   CD    GLU B 214   OE1    -0.111
REMARK 500    ASN B 253   C     ASN B 253   O       0.127
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    ARG B  27   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ASP B  32   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    LEU B  47   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES
REMARK 500    LEU B  47   CB  -  CG  -  CD2 ANGL. DEV. = -18.6 DEGREES
REMARK 500    ASP B  75   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG B  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ASP B 130   OD1 -  CG  -  OD2 ANGL. DEV. = -11.5 DEGREES
REMARK 500    ASP B 130   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP B 139   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    LEU B 141   CB  -  CG  -  CD1 ANGL. DEV. =  14.4 DEGREES
REMARK 500    GLU B 214   OE1 -  CD  -  OE2 ANGL. DEV. = -11.1 DEGREES
REMARK 500    GLU B 221   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.8 DEGREES
REMARK 500    PHE B 226   CB  -  CG  -  CD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    PHE B 226   CB  -  CG  -  CD1 ANGL. DEV. =   6.8 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    ASN B  11       23.09   -140.37
REMARK 500    LYS B 111       -2.96     74.91
REMARK 500    ASN B 244       44.73    -94.76
REMARK 500    LYS B 252     -132.26     56.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 491        DISTANCE =  5.60 ANGSTROMS
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 B 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 EVD B   1   N
REMARK 620 2 HIS B  94   NE2 109.4
REMARK 620 3 HIS B  96   NE2 114.2 103.5
REMARK 620 4 HIS B 119   ND1 114.7 113.9 100.5
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVD B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EVD B 263
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S72   RELATED DB: PDB
REMARK 900 RELATED ID: 3S73   RELATED DB: PDB
REMARK 900 RELATED ID: 3S74   RELATED DB: PDB
REMARK 900 RELATED ID: 3S75   RELATED DB: PDB
REMARK 900 RELATED ID: 3S76   RELATED DB: PDB
REMARK 900 RELATED ID: 3S77   RELATED DB: PDB
REMARK 900 RELATED ID: 3S78   RELATED DB: PDB
DBREF  3S71 B    3   261  UNP    P00918   CAH2_HUMAN       3    260
SEQRES   1 B  258  HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS
SEQRES   2 B  258  TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN
SEQRES   3 B  258  SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP
SEQRES   4 B  258  PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA
SEQRES   5 B  258  THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN
SEQRES   6 B  258  VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS
SEQRES   7 B  258  GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE
SEQRES   8 B  258  HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU
SEQRES   9 B  258  HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS
SEQRES  10 B  258  LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS
SEQRES  11 B  258  ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE
SEQRES  12 B  258  PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS
SEQRES  13 B  258  VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS
SEQRES  14 B  258  SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU
SEQRES  15 B  258  PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU
SEQRES  16 B  258  THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL
SEQRES  17 B  258  LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU
SEQRES  18 B  258  LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO
SEQRES  19 B  258  GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO
SEQRES  20 B  258  LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  B 262       1
HET    EVD  B   1      13
HET    EVD  B 263      13
HETNAM      ZN ZINC ION
HETNAM     EVD 1-BENZOFURAN-2-SULFONAMIDE
FORMUL   2   ZN    ZN 2+
FORMUL   3  EVD    2(C8 H7 N O3 S)
FORMUL   5  HOH   *367(H2 O)
HELIX    1   1 GLY B   12  ASP B   19  5                                   8
HELIX    2   2 PHE B   20  GLY B   25  5                                   6
HELIX    3   3 LYS B  127  GLY B  129  5                                   3
HELIX    4   4 ASP B  130  VAL B  135  1                                   6
HELIX    5   5 LYS B  154  GLY B  156  5                                   3
HELIX    6   6 LEU B  157  LEU B  164  1                                   8
HELIX    7   7 ASP B  165  ILE B  167  5                                   3
HELIX    8   8 ASP B  180  LEU B  185  5                                   6
HELIX    9   9 SER B  220  ARG B  227  1                                   8
SHEET    1   A 2 ASP B  32  ILE B  33  0
SHEET    2   A 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33
SHEET    1   B10 LYS B  39  TYR B  40  0
SHEET    2   B10 LYS B 257  ALA B 258  1  O  ALA B 258   N  LYS B  39
SHEET    3   B10 TYR B 191  GLY B 196 -1  N  THR B 193   O  LYS B 257
SHEET    4   B10 VAL B 207  LEU B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   B10 LEU B 141  GLY B 151  1  N  GLY B 145   O  ILE B 210
SHEET    6   B10 ALA B 116  ASN B 124 -1  N  LEU B 118   O  ILE B 146
SHEET    7   B10 TYR B  88  TRP B  97 -1  N  HIS B  94   O  HIS B 119
SHEET    8   B10 PHE B  66  PHE B  70 -1  N  VAL B  68   O  PHE B  93
SHEET    9   B10 SER B  56  ASN B  61 -1  N  LEU B  57   O  GLU B  69
SHEET   10   B10 SER B 173  ASP B 175 -1  O  ALA B 174   N  ILE B  59
SHEET    1   C 6 LEU B  47  SER B  50  0
SHEET    2   C 6 VAL B  78  GLY B  81 -1  O  VAL B  78   N  SER B  50
SHEET    3   C 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  LEU B  79
SHEET    4   C 6 ALA B 116  ASN B 124 -1  O  HIS B 119   N  HIS B  94
SHEET    5   C 6 LEU B 141  GLY B 151 -1  O  ILE B 146   N  LEU B 118
SHEET    6   C 6 ILE B 216  SER B 219  1  O  VAL B 218   N  GLY B 151
LINK        ZN    ZN B 262                 N   EVD B   1     1555   1555  1.97
LINK         NE2 HIS B  94                ZN    ZN B 262     1555   1555  1.99
LINK         NE2 HIS B  96                ZN    ZN B 262     1555   1555  2.01
LINK         ND1 HIS B 119                ZN    ZN B 262     1555   1555  2.04
CISPEP   1 SER B   29    PRO B   30          0        -1.39
CISPEP   2 PRO B  201    PRO B  202          0        14.49
SITE     1 AC1  4 EVD B   1  HIS B  94  HIS B  96  HIS B 119
SITE     1 AC2 10 HIS B  94  HIS B  96  HIS B 119  VAL B 121
SITE     2 AC2 10 LEU B 198  THR B 199  THR B 200  TRP B 209
SITE     3 AC2 10  ZN B 262  HOH B 312
SITE     1 AC3  9 TRP B   5  HIS B  10  HIS B  15  TRP B  16
SITE     2 AC3  9 ASP B  19  ASP B 180  ARG B 182  GLY B 183
SITE     3 AC3  9 HOH B 476
CRYST1   42.366   41.396   72.471  90.00 104.69  90.00 P 1 21 1      2
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      0.023604  0.000000  0.006188        0.00000
SCALE2      0.000000  0.024157  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014265        0.00000
      
PROCHECK
Go to PROCHECK summary
 References