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PDBsum entry 3f7b

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3f7b
Jmol
Contents
Protein chain
257 a.a.
Ligands
AG5 ×2
Metals
_ZN ×2
Waters ×263
HEADER    LYASE                                   07-NOV-08   3F7B
TITLE     CRYSTAL STRUCTURE OF SOLUBLE DOMAIN OF CA4 IN COMPLEX WITH SMALL
TITLE    2 MOLECULE.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 4;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: SOLUBLE DOMAIN;
COMPND   5 SYNONYM: CARBONIC ANHYDRASE IV, CA-IV, CARBONATE DEHYDRATASE IV;
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: CA4;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    STRUCTURE-BASED DRUG DESIGN. SMALL MOLECULE COMPLEX. CO-CRYSTAL.,
KEYWDS   2 CELL MEMBRANE, DISEASE MUTATION, GLYCOPROTEIN, GPI-ANCHOR,
KEYWDS   3 LIPOPROTEIN, LYASE, MEMBRANE, METAL-BINDING, RETINITIS PIGMENTOSA,
KEYWDS   4 SENSORY TRANSDUCTION, VISION, ZINC
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.E.GREASLEY,R.A.A.FERRE,T.A.PAULY,R.PAZ
REVDAT   2   12-MAY-10 3F7B    1       JRNL
REVDAT   1   22-SEP-09 3F7B    0
JRNL        AUTH   W.VERNIER,W.CHONG,D.REWOLINSKI,S.GREASLEY,T.PAULY,M.SHAW,
JRNL        AUTH 2 D.DINH,R.A.FERRE,S.NUKUI,M.ORNELAS,E.REYNER
JRNL        TITL   THIOETHER BENZENESULFONAMIDE INHIBITORS OF CARBONIC
JRNL        TITL 2 ANHYDRASES II AND IV: STRUCTURE-BASED DRUG DESIGN,
JRNL        TITL 3 SYNTHESIS, AND BIOLOGICAL EVALUATION.
JRNL        REF    BIOORG.MED.CHEM.              V.  18  3307 2010
JRNL        REFN                   ISSN 0968-0896
JRNL        PMID   20363633
JRNL        DOI    10.1016/J.BMC.2010.03.014
REMARK   2
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0073
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) : 2.05
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.68
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6
REMARK   3   NUMBER OF REFLECTIONS             : 39564
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) : 0.194
REMARK   3   R VALUE            (WORKING SET) : 0.191
REMARK   3   FREE R VALUE                     : 0.252
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2094
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) : 2.05
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3045
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.66
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850
REMARK   3   BIN FREE R VALUE SET COUNT          : 147
REMARK   3   BIN FREE R VALUE                    : 0.3610
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4002
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 58
REMARK   3   SOLVENT ATOMS            : 263
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 33.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.16
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.16000
REMARK   3    B22 (A**2) : -0.61000
REMARK   3    B33 (A**2) : 0.69000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.69000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.180
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.179
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.915
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4156 ; 0.026 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5620 ; 2.072 ; 1.968
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   493 ; 7.287 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   186 ;36.501 ;25.000
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   719 ;17.280 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;11.268 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   608 ; 0.171 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3109 ; 0.011 ; 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):  2510 ; 1.371 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4050 ; 2.372 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1646 ; 3.673 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1570 ; 5.741 ; 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: NULL
REMARK   4
REMARK   4 3F7B COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 95
REMARK 200  PH                             : 4.5
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 RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41673
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.680
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7
REMARK 200  DATA REDUNDANCY                : 2.560
REMARK 200  R MERGE                    (I) : 0.05900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.32300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1ZNC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M NA ACETATE, 0.32M
REMARK 280  AMMONIUM SULFATE , PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       62.95500
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.27800
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       62.95500
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       64.27800
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 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: 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 491  LIES ON A SPECIAL POSITION.
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     ARG A   129
REMARK 465     ASN A   130
REMARK 465     VAL A   131
REMARK 465     LYS A   132
REMARK 465     GLU A   133
REMARK 465     ALA A   134
REMARK 465     GLN A   135
REMARK 465     ASP A   136
REMARK 465     ALA B     1
REMARK 465     GLU B     2
REMARK 465     SER B     3
REMARK 465     HIS B     4
REMARK 465     SER B    11C
REMARK 465     ASN B    11D
REMARK 465     TYR B    11E
REMARK 465     LYS B   125A
REMARK 465     GLY B   125B
REMARK 465     THR B   125C
REMARK 465     SER B   125D
REMARK 465     ARG B   125E
REMARK 465     ASN B   125F
REMARK 465     VAL B   125G
REMARK 465     LYS B   125H
REMARK 465     GLU B   125I
REMARK 465     ALA B   125J
REMARK 465     GLN B   125K
REMARK 465     ASP B   125L
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     ASN A  11D   CG   OD1  ND2
REMARK 470     TYR A  11E   CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     LYS A  42    CE   NZ
REMARK 470     LYS A  43    CD   CE   NZ
REMARK 470     LYS A 126    CG   CD   CE   NZ
REMARK 470     SER A 128    OG
REMARK 470     LYS A 187    CD   CE   NZ
REMARK 470     GLU A 187B   CD   OE1  OE2
REMARK 470     ARG A 189A   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 221    CD   OE1  OE2
REMARK 470     LYS B  42    CE   NZ
REMARK 470     LYS B  43    CE   NZ
REMARK 470     LYS B  53    CD   CE   NZ
REMARK 470     GLU B 138    CD   OE1  OE2
REMARK 470     LYS B 187    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   OD2  ASP B   110     O    HOH B   439              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    TRP A  16   C     GLY A  20   N       0.195
REMARK 500    ASN A  72   C     LYS A  76   N       0.196
REMARK 500    GLU A 171   CG    GLU A 171   CD      0.091
REMARK 500    TYR A 191   CE2   TYR A 191   CD2     0.092
REMARK 500    LYS A 233   C     GLU A 236   N       0.139
REMARK 500    TRP B  16   C     GLY B  20   N       0.159
REMARK 500    ASN B  72   C     LYS B  76   N       0.192
REMARK 500    LYS B 233   C     GLU B 236   N       0.143
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    TRP A  16   CA  -  C   -  N   ANGL. DEV. =  21.1 DEGREES
REMARK 500    TRP A  16   O   -  C   -  N   ANGL. DEV. = -20.8 DEGREES
REMARK 500    GLY A  20   C   -  N   -  CA  ANGL. DEV. =  22.5 DEGREES
REMARK 500    LEU A 218   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    LYS A 233   CA  -  C   -  N   ANGL. DEV. =  24.9 DEGREES
REMARK 500    LYS A 233   O   -  C   -  N   ANGL. DEV. = -26.8 DEGREES
REMARK 500    GLU A 236   C   -  N   -  CA  ANGL. DEV. =  23.7 DEGREES
REMARK 500    GLY B  20   C   -  N   -  CA  ANGL. DEV. = -20.7 DEGREES
REMARK 500    LYS B 233   O   -  C   -  N   ANGL. DEV. = -12.9 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    SER A  98     -163.78   -124.36
REMARK 500    LYS B  25     -164.79    -78.22
REMARK 500    ARG B  27       50.71   -119.33
REMARK 500    SER B  65     -178.13   -171.74
REMARK 500    GLU B 171      -14.33     81.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PRO A  137     GLU A  138                 -146.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLN A  10        23.4      L          L   OUTSIDE RANGE
REMARK 500    VAL A 245        24.2      L          L   OUTSIDE RANGE
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 A 555        DISTANCE =  5.14 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 A 300  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 111.7
REMARK 620 3 HIS A 119   ND1 116.1  99.3
REMARK 620 4 AG5 A 302   N9  101.7 112.7 115.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  94   NE2
REMARK 620 2 HIS B  96   NE2 103.0
REMARK 620 3 HIS B 119   ND1 111.9  98.5
REMARK 620 4 AG5 B 303   N9  109.5 110.7 121.2
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 A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AG5 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AG5 B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F7U   RELATED DB: PDB
REMARK 900 SMALL MOLECULE FROM SAME CHEMICAL SERIES.
REMARK 900 RELATED ID: 3FW3   RELATED DB: PDB
DBREF  3F7B A    1   259  UNP    P22748   CAH4_HUMAN      19    284
DBREF  3F7B B    1   259  UNP    P22748   CAH4_HUMAN      19    284
SEQRES   1 A  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER
SEQRES   2 A  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY
SEQRES   3 A  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL
SEQRES   4 A  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE
SEQRES   5 A  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL
SEQRES   6 A  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN
SEQRES   7 A  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR
SEQRES   8 A  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO
SEQRES   9 A  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE
SEQRES  10 A  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY
SEQRES  11 A  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP
SEQRES  12 A  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR
SEQRES  13 A  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU
SEQRES  14 A  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA
SEQRES  15 A  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS
SEQRES  16 A  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR
SEQRES  17 A  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG
SEQRES  18 A  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE
SEQRES  19 A  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER
SEQRES  20 A  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN
SEQRES  21 A  266  ARG THR VAL ILE LYS SER
SEQRES   1 B  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER
SEQRES   2 B  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY
SEQRES   3 B  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL
SEQRES   4 B  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE
SEQRES   5 B  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL
SEQRES   6 B  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN
SEQRES   7 B  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR
SEQRES   8 B  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO
SEQRES   9 B  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE
SEQRES  10 B  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY
SEQRES  11 B  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP
SEQRES  12 B  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR
SEQRES  13 B  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU
SEQRES  14 B  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA
SEQRES  15 B  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS
SEQRES  16 B  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR
SEQRES  17 B  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG
SEQRES  18 B  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE
SEQRES  19 B  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER
SEQRES  20 B  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN
SEQRES  21 B  266  ARG THR VAL ILE LYS SER
HET     ZN  A 300       1
HET    AG5  A 302      28
HET     ZN  B 301       1
HET    AG5  B 303      28
HETNAM      ZN ZINC ION
HETNAM     AG5 N-(2-PHENYLETHYL)-2-(PHENYLSULFANYL)-5-
HETNAM   2 AG5  SULFAMOYLPYRIDINE-3-CARBOXAMIDE
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  AG5    2(C20 H19 N3 O3 S2)
FORMUL   7  HOH   *263(H2 O)
HELIX    1   1 TYR A    7  SER A   11B 1                                   7
HELIX    2   2 VAL A   12  TRP A   16  5                                   5
HELIX    3   3 VAL A   34  ALA A   38  5                                   5
HELIX    4   4 ASN A  154  GLY A  156  5                                   3
HELIX    5   5 PHE A  157  SER A  165  1                                   9
HELIX    6   6 LEU A  181  LEU A  185  5                                   5
HELIX    7   7 LYS A  187  ARG A  189A 5                                   6
HELIX    8   8 ARG A  220  LEU A  229  1                                  11
HELIX    9   9 TYR B    7  SER B   11B 1                                   7
HELIX   10  10 VAL B   12  TRP B   16  5                                   5
HELIX   11  11 VAL B   34  ALA B   38  5                                   5
HELIX   12  12 ASN B  154  GLY B  156  5                                   3
HELIX   13  13 PHE B  157  LEU B  164  1                                   8
HELIX   14  14 SER B  165  ILE B  167  5                                   3
HELIX   15  15 SER B  180  LEU B  184  5                                   5
HELIX   16  16 LYS B  187  ARG B  189A 5                                   6
HELIX   17  17 ARG B  220  LEU B  229  1                                  11
SHEET    1   A 2 HIS A   4  TRP A   5  0
SHEET    2   A 2 CYS A  11G LEU A  11H 1  O  LEU A  11H  N  HIS A   4
SHEET    1   B 2 ASN A  32  ILE A  33  0
SHEET    2   B 2 SER A 108  LEU A 109  1  O  SER A 108   N  ILE A  33
SHEET    1   C10 LYS A  39  VAL A  40  0
SHEET    2   C10 ILE A 257  LYS A 258  1  O  LYS A 258   N  LYS A  39
SHEET    3   C10 TYR A 191  GLY A 196 -1  N  ARG A 193   O  ILE A 257
SHEET    4   C10 VAL A 207  PHE A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   C10 ILE A 141  GLY A 151  1  N  ILE A 141   O  VAL A 208
SHEET    6   C10 MET A 116  LYS A 124 -1  N  MET A 118   O  PHE A 146
SHEET    7   C10 TYR A  88  TRP A  97 -1  N  LYS A  91   O  VAL A 121
SHEET    8   C10 VAL A  66  LEU A  69 -1  N  MET A  68   O  LEU A  93
SHEET    9   C10 THR A  58  ASN A  61 -1  N  GLN A  60   O  MET A  67
SHEET   10   C10 SER A 173  THR A 175 -1  O  THR A 174   N  VAL A  59
SHEET    1   D 6 PHE A  47  SER A  50  0
SHEET    2   D 6 SER A  78  GLY A  81 -1  O  SER A  80   N  PHE A  48
SHEET    3   D 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  ILE A  79
SHEET    4   D 6 MET A 116  LYS A 124 -1  O  VAL A 121   N  LYS A  91
SHEET    5   D 6 ILE A 141  GLY A 151 -1  O  PHE A 146   N  MET A 118
SHEET    6   D 6 ILE A 216  HIS A 219  1  O  ILE A 216   N  LEU A 147
SHEET    1   E 2 ASN B  32  ILE B  33  0
SHEET    2   E 2 SER B 108  LEU B 109  1  O  SER B 108   N  ILE B  33
SHEET    1   F10 LYS B  39  VAL B  40  0
SHEET    2   F10 ILE B 257  LYS B 258  1  O  LYS B 258   N  LYS B  39
SHEET    3   F10 TYR B 191  GLY B 196 -1  N  ARG B 193   O  ILE B 257
SHEET    4   F10 VAL B 207  PHE B 212 -1  O  VAL B 207   N  GLY B 196
SHEET    5   F10 ILE B 141  GLY B 151  1  N  ALA B 145   O  THR B 210
SHEET    6   F10 MET B 116  LYS B 124 -1  N  MET B 118   O  PHE B 146
SHEET    7   F10 TYR B  88  TRP B  97 -1  N  LYS B  91   O  VAL B 121
SHEET    8   F10 VAL B  66  LEU B  69 -1  N  MET B  68   O  LEU B  93
SHEET    9   F10 THR B  58  ASN B  61 -1  N  GLN B  60   O  MET B  67
SHEET   10   F10 SER B 173  THR B 175 -1  O  THR B 174   N  VAL B  59
SHEET    1   G 6 PHE B  47  SER B  50  0
SHEET    2   G 6 SER B  78  GLY B  81 -1  O  SER B  80   N  PHE B  48
SHEET    3   G 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  ILE B  79
SHEET    4   G 6 MET B 116  LYS B 124 -1  O  VAL B 121   N  LYS B  91
SHEET    5   G 6 ILE B 141  GLY B 151 -1  O  PHE B 146   N  MET B 118
SHEET    6   G 6 ILE B 216  HIS B 219  1  O  ILE B 216   N  LEU B 147
SSBOND   1 CYS A    6    CYS A   11G                         1555   1555  2.07
SSBOND   2 CYS A   23    CYS A  203                          1555   1555  2.08
SSBOND   3 CYS B    6    CYS B   11G                         1555   1555  2.09
SSBOND   4 CYS B   23    CYS B  203                          1555   1555  2.06
LINK         NE2 HIS A  94                ZN    ZN A 300     1555   1555  2.03
LINK         NE2 HIS A  96                ZN    ZN A 300     1555   1555  2.08
LINK         ND1 HIS A 119                ZN    ZN A 300     1555   1555  2.09
LINK         NE2 HIS B  94                ZN    ZN B 301     1555   1555  2.12
LINK         NE2 HIS B  96                ZN    ZN B 301     1555   1555  2.18
LINK         ND1 HIS B 119                ZN    ZN B 301     1555   1555  1.97
LINK        ZN    ZN A 300                 N9  AG5 A 302     1555   1555  2.03
LINK        ZN    ZN B 301                 N9  AG5 B 303     1555   1555  1.97
CISPEP   1 SER A   29    PRO A   30          0         2.94
CISPEP   2 PRO A  201    THR A  202          0         9.32
CISPEP   3 SER B   29    PRO B   30          0         0.70
CISPEP   4 PRO B  201    THR B  202          0         5.85
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  AG5 A 302
SITE     1 AC2 16 TYR A   7  ASN A  62  HIS A  64  SER A  65
SITE     2 AC2 16 MET A  67  GLN A  92  HIS A  94  HIS A  96
SITE     3 AC2 16 HIS A 119  VAL A 121  ILE A 141  LEU A 198
SITE     4 AC2 16 THR A 199  THR A 200   ZN A 300  HOH A 564
SITE     1 AC3  4 HIS B  94  HIS B  96  HIS B 119  AG5 B 303
SITE     1 AC4 17 SER A 128  HOH A 470  TYR B   7  ASN B  62
SITE     2 AC4 17 HIS B  64  SER B  65  GLN B  92  HIS B  94
SITE     3 AC4 17 HIS B  96  HIS B 119  VAL B 121  ILE B 141
SITE     4 AC4 17 LEU B 198  THR B 199  THR B 200  TRP B 209
SITE     5 AC4 17  ZN B 301
CRYST1  125.910  128.556   46.365  90.00  99.88  90.00 C 1 2 1       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      0.007942  0.000000  0.001384        0.00000
SCALE2      0.000000  0.007779  0.000000        0.00000
SCALE3      0.000000  0.000000  0.021893        0.00000
      
PROCHECK
Go to PROCHECK summary
 References