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PDBsum entry 2a5v

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
2a5v
Jmol
Contents
Protein chains
210 a.a.
Ligands
SCN ×4
Metals
_ZN ×11
Waters ×311
HEADER    LYASE                                   01-JUL-05   2A5V
TITLE     CRYSTAL STRUCTURE OF M. TUBERCULOSIS BETA CARBONIC ANHYDRASE, RV3588C,
TITLE    2 TETRAMERIC FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE (CARBONATE DEHYDRATASE) (CARBONIC
COMPND   3 DEHYDRATASE);
COMPND   4 CHAIN: A, B, C, D;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE   3 ORGANISM_TAXID: 83332;
SOURCE   4 STRAIN: H37RV;
SOURCE   5 GENE: RV3588C;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    TETRAMER, CARBOXYLATE SHIFT, OPEN, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.S.COVARRUBIAS,T.BERGFORS,T.A.JONES,M.HOGBOM
REVDAT   4   13-JUL-11 2A5V    1       VERSN
REVDAT   3   24-FEB-09 2A5V    1       VERSN
REVDAT   2   07-MAR-06 2A5V    1       JRNL
REVDAT   1   20-SEP-05 2A5V    0
JRNL        AUTH   A.S.COVARRUBIAS,T.BERGFORS,T.A.JONES,M.HOGBOM
JRNL        TITL   STRUCTURAL MECHANICS OF THE PH-DEPENDENT ACTIVITY OF
JRNL        TITL 2 BETA-CARBONIC ANHYDRASE FROM MYCOBACTERIUM TUBERCULOSIS
JRNL        REF    J.BIOL.CHEM.                  V. 281  4993 2006
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   16321983
JRNL        DOI    10.1074/JBC.M510756200
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4
REMARK   3   NUMBER OF REFLECTIONS             : 38347
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) : 0.165
REMARK   3   R VALUE            (WORKING SET) : 0.162
REMARK   3   FREE R VALUE                     : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2016
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) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.25
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2709
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.62
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320
REMARK   3   BIN FREE R VALUE SET COUNT          : 132
REMARK   3   BIN FREE R VALUE                    : 0.3510
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6160
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 23
REMARK   3   SOLVENT ATOMS            : 311
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.95
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.13000
REMARK   3    B22 (A**2) : -0.18000
REMARK   3    B33 (A**2) : 0.11000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.51000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.263
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.197
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.752
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6278 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8527 ; 1.367 ; 1.938
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   826 ; 6.042 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   280 ;34.316 ;22.893
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   953 ;14.470 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;15.926 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   986 ; 0.090 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4826 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3072 ; 0.225 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4337 ; 0.299 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   378 ; 0.155 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     8 ; 0.156 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.205 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.166 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     2 ; 0.074 ; 0.200
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):  4093 ; 0.608 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6530 ; 1.144 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2185 ; 2.052 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1997 ; 3.269 ; 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  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     5        A   200
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7440  37.9760  36.7020
REMARK   3    T TENSOR
REMARK   3      T11:   -.0693 T22:    .0339
REMARK   3      T33:   -.1518 T12:   -.0678
REMARK   3      T13:    .0002 T23:   -.0514
REMARK   3    L TENSOR
REMARK   3      L11:   2.4203 L22:   1.3864
REMARK   3      L33:   1.4170 L12:   -.2706
REMARK   3      L13:   -.5582 L23:    .0562
REMARK   3    S TENSOR
REMARK   3      S11:    .1189 S12:   -.1954 S13:    .3154
REMARK   3      S21:    .0996 S22:    .0020 S23:   -.1805
REMARK   3      S31:   -.2634 S32:    .2928 S33:   -.1209
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     5        B   200
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8400  22.8310  39.9920
REMARK   3    T TENSOR
REMARK   3      T11:   -.0941 T22:    .0305
REMARK   3      T33:   -.2026 T12:   -.0113
REMARK   3      T13:   -.0047 T23:    .0026
REMARK   3    L TENSOR
REMARK   3      L11:   1.6696 L22:   1.5888
REMARK   3      L33:   2.1534 L12:   -.0024
REMARK   3      L13:   -.6014 L23:   -.2154
REMARK   3    S TENSOR
REMARK   3      S11:   -.0128 S12:   -.1071 S13:   -.0569
REMARK   3      S21:    .1535 S22:   -.0022 S23:    .0280
REMARK   3      S31:    .0430 S32:   -.0081 S33:    .0150
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     5        C   200
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7790  27.0290   2.0030
REMARK   3    T TENSOR
REMARK   3      T11:    .0013 T22:    .1097
REMARK   3      T33:   -.3208 T12:    .0317
REMARK   3      T13:   -.0126 T23:    .0133
REMARK   3    L TENSOR
REMARK   3      L11:    .8733 L22:   1.5802
REMARK   3      L33:   3.8998 L12:   -.0039
REMARK   3      L13:   -.5065 L23:   -.1311
REMARK   3    S TENSOR
REMARK   3      S11:   -.0028 S12:    .2461 S13:    .0005
REMARK   3      S21:   -.4453 S22:    .0494 S23:   -.0211
REMARK   3      S31:   -.1100 S32:   -.5159 S33:   -.0466
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D     5        D   200
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7560  14.1970   6.8820
REMARK   3    T TENSOR
REMARK   3      T11:    .0131 T22:   -.0373
REMARK   3      T33:   -.1832 T12:    .0589
REMARK   3      T13:    .0980 T23:   -.0620
REMARK   3    L TENSOR
REMARK   3      L11:   2.1994 L22:   2.0344
REMARK   3      L33:   3.1926 L12:    .5535
REMARK   3      L13:   -.2538 L23:   -.0938
REMARK   3    S TENSOR
REMARK   3      S11:   -.1131 S12:    .1804 S13:   -.3406
REMARK   3      S21:   -.3605 S22:    .0619 S23:   -.3707
REMARK   3      S31:    .5052 S32:    .2008 S33:    .0512
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2A5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-05.
REMARK 100 THE RCSB ID CODE IS RCSB033525.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-OCT-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : MAX II
REMARK 200  BEAMLINE                       : I711
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.094
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38347
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05800
REMARK 200   FOR THE DATA SET  : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.36000
REMARK 200   FOR SHELL         : 2.690
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER V. 1.2
REMARK 200 STARTING MODEL: PDB ENTRY 1YM3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, NASCN, GLYCEROL, PH 7.5,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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       35.15100
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -191.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -195.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     GLU A   205
REMARK 465     GLU A   206
REMARK 465     VAL A   207
REMARK 465     HIS B    -5
REMARK 465     HIS B    -4
REMARK 465     VAL B   207
REMARK 465     HIS C    -5
REMARK 465     HIS C    -4
REMARK 465     HIS C    -3
REMARK 465     HIS C    -2
REMARK 465     HIS C    -1
REMARK 465     HIS C     0
REMARK 465     GLY C     1
REMARK 465     PRO C     2
REMARK 465     ASN C     3
REMARK 465     GLU C   205
REMARK 465     GLU C   206
REMARK 465     VAL C   207
REMARK 465     HIS D    -5
REMARK 465     GLU D   205
REMARK 465     GLU D   206
REMARK 465     VAL D   207
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     HIS A  -5    N
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   OH   TYR A   126     OH   TYR C   126              1.97
REMARK 500   O    HIS B     0     O    HOH B   599              2.15
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    VAL A  56       54.06   -114.32
REMARK 500    HIS A  77       53.04     38.13
REMARK 500    GLN B  30       21.95   -144.59
REMARK 500    ASP B  53      125.52    -36.10
REMARK 500    VAL B  56       56.38   -112.35
REMARK 500    HIS B  77       49.15     37.99
REMARK 500    ASP B  80     -159.22   -143.18
REMARK 500    SER B 147      -35.05   -133.43
REMARK 500    ASP C  53      124.70    -34.10
REMARK 500    VAL C  56       57.21   -114.65
REMARK 500    THR D   4     -173.66    -65.54
REMARK 500    GLN D  30       -0.48   -141.56
REMARK 500    LYS D  43       53.96   -143.82
REMARK 500    VAL D  56       58.95   -107.92
REMARK 500    HIS D  77       51.44     37.41
REMARK 500    ARG D 197      -64.77   -121.91
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 ILE B   79     ASP B   80                  145.28
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 400  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  -4   ND1
REMARK 620 2 HIS A  -2   NE2 120.8
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 401  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  51   SG
REMARK 620 2 CYS A 107   SG  127.7
REMARK 620 3 HIS A 104   NE2 111.1 111.7
REMARK 620 4 SCN A 501   N    94.7 106.1  99.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 405  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  -3   ND1
REMARK 620 2 HIS A   0   NE2 125.8
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 409  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 198   OD2
REMARK 620 2 HIS A 158   ND1 139.1
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 402  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B  51   SG
REMARK 620 2 HIS B 104   NE2 111.3
REMARK 620 3 CYS B 107   SG  127.3 111.4
REMARK 620 4 SCN B 502   N   103.4  92.2 104.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 408  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B   0   NE2
REMARK 620 2 HIS B  -2   ND1 103.6
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C 403  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 104   NE2
REMARK 620 2 CYS C 107   SG  109.3
REMARK 620 3 SCN C 503   N    97.1 113.2
REMARK 620 4 CYS C  51   SG  110.7 125.7  96.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN D 404  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 104   NE2
REMARK 620 2 CYS D 107   SG  110.3
REMARK 620 3 CYS D  51   SG  111.9 126.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN D 406  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D  -1   NE2
REMARK 620 2 HIS D  -3   ND1 121.8
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN D 407  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D   0   NE2
REMARK 620 2 HIS D  -2   ND1  88.0
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YM3   RELATED DB: PDB
REMARK 900 DIMERIC FORM
DBREF  2A5V A    2   207  UNP    O53573   O53573_MYCTU     2    207
DBREF  2A5V B    2   207  UNP    O53573   O53573_MYCTU     2    207
DBREF  2A5V C    2   207  UNP    O53573   O53573_MYCTU     2    207
DBREF  2A5V D    2   207  UNP    O53573   O53573_MYCTU     2    207
SEQADV 2A5V HIS A   -5  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS A   -4  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS A   -3  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS A   -2  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS A   -1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS A    0  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V GLY A    1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS B   -5  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS B   -4  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS B   -3  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS B   -2  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS B   -1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS B    0  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V GLY B    1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS C   -5  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS C   -4  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS C   -3  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS C   -2  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS C   -1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS C    0  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V GLY C    1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS D   -5  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS D   -4  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS D   -3  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS D   -2  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS D   -1  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V HIS D    0  UNP  O53573              CLONING ARTIFACT
SEQADV 2A5V GLY D    1  UNP  O53573              CLONING ARTIFACT
SEQRES   1 A  213  HIS HIS HIS HIS HIS HIS GLY PRO ASN THR ASN PRO VAL
SEQRES   2 A  213  ALA ALA TRP LYS ALA LEU LYS GLU GLY ASN GLU ARG PHE
SEQRES   3 A  213  VAL ALA GLY ARG PRO GLN HIS PRO SER GLN SER VAL ASP
SEQRES   4 A  213  HIS ARG ALA GLY LEU ALA ALA GLY GLN LYS PRO THR ALA
SEQRES   5 A  213  VAL ILE PHE GLY CYS ALA ASP SER ARG VAL ALA ALA GLU
SEQRES   6 A  213  ILE ILE PHE ASP GLN GLY LEU GLY ASP MET PHE VAL VAL
SEQRES   7 A  213  ARG THR ALA GLY HIS VAL ILE ASP SER ALA VAL LEU GLY
SEQRES   8 A  213  SER ILE GLU TYR ALA VAL THR VAL LEU ASN VAL PRO LEU
SEQRES   9 A  213  ILE VAL VAL LEU GLY HIS ASP SER CYS GLY ALA VAL ASN
SEQRES  10 A  213  ALA ALA LEU ALA ALA ILE ASN ASP GLY THR LEU PRO GLY
SEQRES  11 A  213  GLY TYR VAL ARG ASP VAL VAL GLU ARG VAL ALA PRO SER
SEQRES  12 A  213  VAL LEU LEU GLY ARG ARG ASP GLY LEU SER ARG VAL ASP
SEQRES  13 A  213  GLU PHE GLU GLN ARG HIS VAL HIS GLU THR VAL ALA ILE
SEQRES  14 A  213  LEU MET ALA ARG SER SER ALA ILE SER GLU ARG ILE ALA
SEQRES  15 A  213  GLY GLY SER LEU ALA ILE VAL GLY VAL THR TYR GLN LEU
SEQRES  16 A  213  ASP ASP GLY ARG ALA VAL LEU ARG ASP HIS ILE GLY ASN
SEQRES  17 A  213  ILE GLY GLU GLU VAL
SEQRES   1 B  213  HIS HIS HIS HIS HIS HIS GLY PRO ASN THR ASN PRO VAL
SEQRES   2 B  213  ALA ALA TRP LYS ALA LEU LYS GLU GLY ASN GLU ARG PHE
SEQRES   3 B  213  VAL ALA GLY ARG PRO GLN HIS PRO SER GLN SER VAL ASP
SEQRES   4 B  213  HIS ARG ALA GLY LEU ALA ALA GLY GLN LYS PRO THR ALA
SEQRES   5 B  213  VAL ILE PHE GLY CYS ALA ASP SER ARG VAL ALA ALA GLU
SEQRES   6 B  213  ILE ILE PHE ASP GLN GLY LEU GLY ASP MET PHE VAL VAL
SEQRES   7 B  213  ARG THR ALA GLY HIS VAL ILE ASP SER ALA VAL LEU GLY
SEQRES   8 B  213  SER ILE GLU TYR ALA VAL THR VAL LEU ASN VAL PRO LEU
SEQRES   9 B  213  ILE VAL VAL LEU GLY HIS ASP SER CYS GLY ALA VAL ASN
SEQRES  10 B  213  ALA ALA LEU ALA ALA ILE ASN ASP GLY THR LEU PRO GLY
SEQRES  11 B  213  GLY TYR VAL ARG ASP VAL VAL GLU ARG VAL ALA PRO SER
SEQRES  12 B  213  VAL LEU LEU GLY ARG ARG ASP GLY LEU SER ARG VAL ASP
SEQRES  13 B  213  GLU PHE GLU GLN ARG HIS VAL HIS GLU THR VAL ALA ILE
SEQRES  14 B  213  LEU MET ALA ARG SER SER ALA ILE SER GLU ARG ILE ALA
SEQRES  15 B  213  GLY GLY SER LEU ALA ILE VAL GLY VAL THR TYR GLN LEU
SEQRES  16 B  213  ASP ASP GLY ARG ALA VAL LEU ARG ASP HIS ILE GLY ASN
SEQRES  17 B  213  ILE GLY GLU GLU VAL
SEQRES   1 C  213  HIS HIS HIS HIS HIS HIS GLY PRO ASN THR ASN PRO VAL
SEQRES   2 C  213  ALA ALA TRP LYS ALA LEU LYS GLU GLY ASN GLU ARG PHE
SEQRES   3 C  213  VAL ALA GLY ARG PRO GLN HIS PRO SER GLN SER VAL ASP
SEQRES   4 C  213  HIS ARG ALA GLY LEU ALA ALA GLY GLN LYS PRO THR ALA
SEQRES   5 C  213  VAL ILE PHE GLY CYS ALA ASP SER ARG VAL ALA ALA GLU
SEQRES   6 C  213  ILE ILE PHE ASP GLN GLY LEU GLY ASP MET PHE VAL VAL
SEQRES   7 C  213  ARG THR ALA GLY HIS VAL ILE ASP SER ALA VAL LEU GLY
SEQRES   8 C  213  SER ILE GLU TYR ALA VAL THR VAL LEU ASN VAL PRO LEU
SEQRES   9 C  213  ILE VAL VAL LEU GLY HIS ASP SER CYS GLY ALA VAL ASN
SEQRES  10 C  213  ALA ALA LEU ALA ALA ILE ASN ASP GLY THR LEU PRO GLY
SEQRES  11 C  213  GLY TYR VAL ARG ASP VAL VAL GLU ARG VAL ALA PRO SER
SEQRES  12 C  213  VAL LEU LEU GLY ARG ARG ASP GLY LEU SER ARG VAL ASP
SEQRES  13 C  213  GLU PHE GLU GLN ARG HIS VAL HIS GLU THR VAL ALA ILE
SEQRES  14 C  213  LEU MET ALA ARG SER SER ALA ILE SER GLU ARG ILE ALA
SEQRES  15 C  213  GLY GLY SER LEU ALA ILE VAL GLY VAL THR TYR GLN LEU
SEQRES  16 C  213  ASP ASP GLY ARG ALA VAL LEU ARG ASP HIS ILE GLY ASN
SEQRES  17 C  213  ILE GLY GLU GLU VAL
SEQRES   1 D  213  HIS HIS HIS HIS HIS HIS GLY PRO ASN THR ASN PRO VAL
SEQRES   2 D  213  ALA ALA TRP LYS ALA LEU LYS GLU GLY ASN GLU ARG PHE
SEQRES   3 D  213  VAL ALA GLY ARG PRO GLN HIS PRO SER GLN SER VAL ASP
SEQRES   4 D  213  HIS ARG ALA GLY LEU ALA ALA GLY GLN LYS PRO THR ALA
SEQRES   5 D  213  VAL ILE PHE GLY CYS ALA ASP SER ARG VAL ALA ALA GLU
SEQRES   6 D  213  ILE ILE PHE ASP GLN GLY LEU GLY ASP MET PHE VAL VAL
SEQRES   7 D  213  ARG THR ALA GLY HIS VAL ILE ASP SER ALA VAL LEU GLY
SEQRES   8 D  213  SER ILE GLU TYR ALA VAL THR VAL LEU ASN VAL PRO LEU
SEQRES   9 D  213  ILE VAL VAL LEU GLY HIS ASP SER CYS GLY ALA VAL ASN
SEQRES  10 D  213  ALA ALA LEU ALA ALA ILE ASN ASP GLY THR LEU PRO GLY
SEQRES  11 D  213  GLY TYR VAL ARG ASP VAL VAL GLU ARG VAL ALA PRO SER
SEQRES  12 D  213  VAL LEU LEU GLY ARG ARG ASP GLY LEU SER ARG VAL ASP
SEQRES  13 D  213  GLU PHE GLU GLN ARG HIS VAL HIS GLU THR VAL ALA ILE
SEQRES  14 D  213  LEU MET ALA ARG SER SER ALA ILE SER GLU ARG ILE ALA
SEQRES  15 D  213  GLY GLY SER LEU ALA ILE VAL GLY VAL THR TYR GLN LEU
SEQRES  16 D  213  ASP ASP GLY ARG ALA VAL LEU ARG ASP HIS ILE GLY ASN
SEQRES  17 D  213  ILE GLY GLU GLU VAL
HET    SCN  A 501       3
HET     ZN  A 401       1
HET     ZN  A 405       1
HET     ZN  A 409       1
HET     ZN  A 400       1
HET    SCN  B 502       3
HET     ZN  B 402       1
HET     ZN  B 408       1
HET    SCN  C 503       3
HET    SCN  C 504       3
HET     ZN  C 403       1
HET     ZN  D 404       1
HET     ZN  D 406       1
HET     ZN  D 407       1
HET     ZN  D 410       1
HETNAM     SCN THIOCYANATE ION
HETNAM      ZN ZINC ION
FORMUL   5  SCN    4(C N S 1-)
FORMUL   6   ZN    11(ZN 2+)
FORMUL  20  HOH   *311(H2 O)
HELIX    1   1 ASN A    5  ALA A   22  1                                  18
HELIX    2   2 SER A   31  GLY A   37  1                                   7
HELIX    3   3 ALA A   57  PHE A   62  1                                   6
HELIX    4   4 ALA A   75  VAL A   78  5                                   4
HELIX    5   5 ASP A   80  VAL A   93  1                                  14
HELIX    6   6 CYS A  107  GLY A  120  1                                  14
HELIX    7   7 TYR A  126  ASP A  144  1                                  19
HELIX    8   8 ARG A  148  SER A  168  1                                  21
HELIX    9   9 SER A  168  GLY A  177  1                                  10
HELIX   10  10 ASN B    5  ALA B   22  1                                  18
HELIX   11  11 SER B   31  GLY B   37  1                                   7
HELIX   12  12 ALA B   57  PHE B   62  1                                   6
HELIX   13  13 ALA B   75  VAL B   78  5                                   4
HELIX   14  14 ASP B   80  VAL B   93  1                                  14
HELIX   15  15 CYS B  107  GLY B  120  1                                  14
HELIX   16  16 TYR B  126  ASP B  144  1                                  19
HELIX   17  17 ARG B  148  SER B  168  1                                  21
HELIX   18  18 SER B  168  GLY B  177  1                                  10
HELIX   19  19 ASN C    5  ALA C   22  1                                  18
HELIX   20  20 SER C   31  ALA C   39  1                                   9
HELIX   21  21 ALA C   57  PHE C   62  1                                   6
HELIX   22  22 ALA C   75  VAL C   78  5                                   4
HELIX   23  23 ASP C   80  VAL C   93  1                                  14
HELIX   24  24 CYS C  107  GLY C  120  1                                  14
HELIX   25  25 TYR C  126  ASP C  144  1                                  19
HELIX   26  26 ARG C  148  SER C  168  1                                  21
HELIX   27  27 SER C  168  GLY C  177  1                                  10
HELIX   28  28 ASN D    5  ALA D   22  1                                  18
HELIX   29  29 SER D   31  LEU D   38  1                                   8
HELIX   30  30 ALA D   57  PHE D   62  1                                   6
HELIX   31  31 ALA D   75  VAL D   78  5                                   4
HELIX   32  32 ASP D   80  VAL D   93  1                                  14
HELIX   33  33 CYS D  107  GLY D  120  1                                  14
HELIX   34  34 TYR D  126  ASP D  144  1                                  19
HELIX   35  35 ARG D  148  SER D  168  1                                  21
HELIX   36  36 SER D  168  GLY D  177  1                                  10
SHEET    1   A 5 MET A  69  THR A  74  0
SHEET    2   A 5 ALA A  46  CYS A  51  1  N  ILE A  48   O  VAL A  72
SHEET    3   A 5 LEU A  98  HIS A 104  1  O  VAL A 100   N  PHE A  49
SHEET    4   A 5 ALA A 181  TYR A 187  1  O  VAL A 183   N  ILE A  99
SHEET    5   A 5 ALA A 194  ILE A 200 -1  O  ASP A 198   N  GLY A 184
SHEET    1   B 5 MET B  69  THR B  74  0
SHEET    2   B 5 ALA B  46  CYS B  51  1  N  ILE B  48   O  VAL B  72
SHEET    3   B 5 LEU B  98  HIS B 104  1  O  VAL B 100   N  PHE B  49
SHEET    4   B 5 ALA B 181  TYR B 187  1  O  VAL B 183   N  VAL B 101
SHEET    5   B 5 ALA B 194  ILE B 200 -1  O  VAL B 195   N  THR B 186
SHEET    1   C 5 MET C  69  THR C  74  0
SHEET    2   C 5 ALA C  46  CYS C  51  1  N  ILE C  48   O  VAL C  72
SHEET    3   C 5 LEU C  98  HIS C 104  1  O  VAL C 100   N  PHE C  49
SHEET    4   C 5 ALA C 181  TYR C 187  1  O  TYR C 187   N  GLY C 103
SHEET    5   C 5 ALA C 194  ILE C 200 -1  O  ASP C 198   N  GLY C 184
SHEET    1   D 5 MET D  69  THR D  74  0
SHEET    2   D 5 ALA D  46  CYS D  51  1  N  ALA D  46   O  PHE D  70
SHEET    3   D 5 LEU D  98  HIS D 104  1  O  VAL D 100   N  VAL D  47
SHEET    4   D 5 ALA D 181  TYR D 187  1  O  VAL D 183   N  VAL D 101
SHEET    5   D 5 ALA D 194  ILE D 200 -1  O  ARG D 197   N  GLY D 184
LINK        ZN    ZN A 400                 ND1 HIS A  -4     1555   1555  1.99
LINK        ZN    ZN A 400                 NE2 HIS A  -2     1555   1555  1.99
LINK        ZN    ZN A 401                 SG  CYS A  51     1555   1555  2.39
LINK        ZN    ZN A 401                 SG  CYS A 107     1555   1555  2.32
LINK        ZN    ZN A 401                 NE2 HIS A 104     1555   1555  2.13
LINK        ZN    ZN A 401                 N   SCN A 501     1555   1555  1.87
LINK        ZN    ZN A 405                 ND1 HIS A  -3     1555   1555  2.07
LINK        ZN    ZN A 405                 NE2 HIS A   0     1555   1555  1.98
LINK        ZN    ZN A 409                 OD2 ASP A 198     1555   1555  2.11
LINK        ZN    ZN A 409                 ND1 HIS A 158     1555   1555  1.85
LINK        ZN    ZN B 402                 SG  CYS B  51     1555   1555  2.30
LINK        ZN    ZN B 402                 NE2 HIS B 104     1555   1555  2.18
LINK        ZN    ZN B 402                 SG  CYS B 107     1555   1555  2.31
LINK        ZN    ZN B 402                 N   SCN B 502     1555   1555  2.73
LINK        ZN    ZN B 408                 NE2 HIS B   0     1555   1555  2.26
LINK        ZN    ZN B 408                 ND1 HIS B  -2     1555   1555  2.47
LINK        ZN    ZN C 403                 NE2 HIS C 104     1555   1555  2.26
LINK        ZN    ZN C 403                 SG  CYS C 107     1555   1555  2.28
LINK        ZN    ZN C 403                 N   SCN C 503     1555   1555  2.02
LINK        ZN    ZN C 403                 SG  CYS C  51     1555   1555  2.32
LINK        ZN    ZN D 404                 NE2 HIS D 104     1555   1555  2.27
LINK        ZN    ZN D 404                 SG  CYS D 107     1555   1555  2.25
LINK        ZN    ZN D 404                 SG  CYS D  51     1555   1555  2.24
LINK        ZN    ZN D 406                 NE2 HIS D  -1     1555   1555  2.41
LINK        ZN    ZN D 406                 ND1 HIS D  -3     1555   1555  1.75
LINK        ZN    ZN D 407                 NE2 HIS D   0     1555   1555  2.27
LINK        ZN    ZN D 407                 ND1 HIS D  -2     1555   1555  2.42
LINK        ZN    ZN D 410                 ND1 HIS D 158     1555   1555  2.05
SITE     1 AC1  6 CYS A  51  ASP A  53  HIS A 104  CYS A 107
SITE     2 AC1  6 GLY A 108   ZN A 401
SITE     1 AC2  4 CYS A  51  HIS A 104  CYS A 107  SCN A 501
SITE     1 AC3  2 HIS A  -3  HIS A   0
SITE     1 AC4  2 HIS A 158  ASP A 198
SITE     1 AC5  2 HIS A  -4  HIS A  -2
SITE     1 AC6  6 TYR A  89  ASP B  53  HIS B 104  CYS B 107
SITE     2 AC6  6 GLY B 108   ZN B 402
SITE     1 AC7  4 CYS B  51  HIS B 104  CYS B 107  SCN B 502
SITE     1 AC8  2 HIS B  -2  HIS B   0
SITE     1 AC9  6 CYS C  51  ASP C  53  HIS C 104  CYS C 107
SITE     2 AC9  6 GLY C 108   ZN C 403
SITE     1 BC1  3 GLN C  42  ASP D  53  ALA D  75
SITE     1 BC2  4 CYS C  51  HIS C 104  CYS C 107  SCN C 503
SITE     1 BC3  3 CYS D  51  HIS D 104  CYS D 107
SITE     1 BC4  2 HIS D  -3  HIS D  -1
SITE     1 BC5  2 HIS D  -2  HIS D   0
SITE     1 BC6  2 HIS D 158  ASP D 198
CRYST1   67.884   70.302   84.361  90.00  93.41  90.00 P 1 21 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      0.014731  0.000000  0.000878        0.00000
SCALE2      0.000000  0.014224  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011875        0.00000
      
PROCHECK
Go to PROCHECK summary
 References