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PDBsum entry 1ylk

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Top Page protein ligands metals Protein-protein interface(s) links
Unknown function PDB id
1ylk
Jmol
Contents
Protein chains
163 a.a.
Ligands
SCN ×5
Metals
_ZN ×4
Waters ×268
HEADER    UNKNOWN FUNCTION                        19-JAN-05   1YLK
TITLE     CRYSTAL STRUCTURE OF RV1284 FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX
TITLE    2 WITH THIOCYANATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HYPOTHETICAL PROTEIN RV1284/MT1322;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE   3 ORGANISM_TAXID: 83332;
SOURCE   4 STRAIN: H37RV;
SOURCE   5 GENE: RV1284;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-AI;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCRT7
KEYWDS    RV1284, HOMODIMER, ALPHA/BETA-FOLD, STRUCTURAL PROTEOMICS IN EUROPE,
KEYWDS   2 SPINE, STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.S.COVARRUBIAS,A.M.LARSSON,M.HOGBOM,J.LINDBERG,T.BERGFORS,
AUTHOR   2 C.BJORKELID,S.L.MOWBRAY,T.UNGE,T.A.JONES,STRUCTURAL PROTEOMICS IN
AUTHOR   3 EUROPE (SPINE)
REVDAT   4   13-JUL-11 1YLK    1       VERSN
REVDAT   3   24-FEB-09 1YLK    1       VERSN
REVDAT   2   24-MAY-05 1YLK    1       JRNL
REVDAT   1   08-MAR-05 1YLK    0
JRNL        AUTH   A.SUAREZ COVARRUBIAS,A.M.LARSSON,M.HOGBOM,J.LINDBERG,
JRNL        AUTH 2 T.BERGFORS,C.BJORKELID,S.L.MOWBRAY,T.UNGE,T.A.JONES
JRNL        TITL   STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES FROM
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS.
JRNL        REF    J.BIOL.CHEM.                  V. 280 18782 2005
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   15753099
JRNL        DOI    10.1074/JBC.M414348200
REMARK   2
REMARK   2 RESOLUTION.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.26
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2
REMARK   3   NUMBER OF REFLECTIONS             : 36658
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) : 0.183
REMARK   3   R VALUE            (WORKING SET) : 0.181
REMARK   3   FREE R VALUE                     : 0.226
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1946
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2607
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.35
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1960
REMARK   3   BIN FREE R VALUE SET COUNT          : 160
REMARK   3   BIN FREE R VALUE                    : 0.2670
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5084
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 19
REMARK   3   SOLVENT ATOMS            : 268
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.92
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.17
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.36000
REMARK   3    B22 (A**2) : -0.28000
REMARK   3    B33 (A**2) : -0.08000
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): 0.223
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.180
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.709
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5194 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7049 ; 1.305 ; 1.963
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   648 ; 5.982 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   236 ;33.244 ;23.220
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   868 ;13.279 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;14.634 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   816 ; 0.084 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3928 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2502 ; 0.223 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3587 ; 0.302 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   369 ; 0.130 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.030 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    62 ; 0.217 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    24 ; 0.097 ; 0.200
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):  3258 ; 0.523 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5297 ; 0.965 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1936 ; 1.788 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1752 ; 2.828 ; 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   : 1.20
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 1YLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-05.
REMARK 100 THE RCSB ID CODE IS RCSB031656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-03
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               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)
REMARK 200  OPTICS                         : SAGITALLY FOCUSING GE(220) AND A
REMARK 200                                   MULTILAYER
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38625
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6
REMARK 200  DATA REDUNDANCY                : 7.400
REMARK 200  R MERGE                    (I) : 0.08500
REMARK 200  R SYM                      (I) : 0.07900
REMARK 200   FOR THE DATA SET  : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.43400
REMARK 200  R SYM FOR SHELL            (I) : 0.39900
REMARK 200   FOR SHELL         : 6.300
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 1G5C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 37.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM THIOCYANATE, POLYETHYLENE
REMARK 280  GLYCOL 2000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
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,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X,Y+1/2,Z+1/2
REMARK 290       6555   -X,-Y+1/2,Z+1/2
REMARK 290       7555   -X,Y+1/2,-Z+1/2
REMARK 290       8555   X,-Y+1/2,-Z+1/2
REMARK 290       9555   X+1/2,Y,Z+1/2
REMARK 290      10555   -X+1/2,-Y,Z+1/2
REMARK 290      11555   -X+1/2,Y,-Z+1/2
REMARK 290      12555   X+1/2,-Y,-Z+1/2
REMARK 290      13555   X+1/2,Y+1/2,Z
REMARK 290      14555   -X+1/2,-Y+1/2,Z
REMARK 290      15555   -X+1/2,Y+1/2,-Z
REMARK 290      16555   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        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       77.03700
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       78.47150
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       77.03700
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       78.47150
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       77.03700
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       78.47150
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       77.03700
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       78.47150
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       78.47150
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       78.47150
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       78.47150
REMARK 290   SMTRY1  12  1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  12  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       78.47150
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.03700
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.03700
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       77.03700
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       50.08200
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       77.03700
REMARK 290   SMTRY3  16  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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.0 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 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 D 444  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     MET A    -8
REMARK 465     ALA A    -7
REMARK 465     HIS A    -6
REMARK 465     HIS A    -5
REMARK 465     HIS A    -4
REMARK 465     HIS A    -3
REMARK 465     HIS A    -2
REMARK 465     HIS A    -1
REMARK 465     SER A     0
REMARK 465     MET B    -8
REMARK 465     ALA B    -7
REMARK 465     HIS B    -6
REMARK 465     HIS B    -5
REMARK 465     HIS B    -4
REMARK 465     HIS B    -3
REMARK 465     HIS B    -2
REMARK 465     HIS B    -1
REMARK 465     SER B     0
REMARK 465     MET C    -8
REMARK 465     ALA C    -7
REMARK 465     HIS C    -6
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     SER C     0
REMARK 465     MET D    -8
REMARK 465     ALA D    -7
REMARK 465     HIS D    -6
REMARK 465     HIS D    -5
REMARK 465     HIS D    -4
REMARK 465     HIS D    -3
REMARK 465     HIS D    -2
REMARK 465     HIS D    -1
REMARK 465     SER D     0
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    ASP A  37      132.97    -38.57
REMARK 500    ASP B  37      131.12    -38.22
REMARK 500    ASP C  37      133.56    -38.90
REMARK 500    THR C 162      -80.30    -67.34
REMARK 500    ASP D  37      134.66    -39.34
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 401  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  88   NE2
REMARK 620 2 CYS A  91   SG  105.6
REMARK 620 3 HOH A 506   O    88.0 101.7
REMARK 620 4 CYS A  35   SG  111.5 125.3 118.0
REMARK 620 N                    1     2     3
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 HIS B  88   NE2
REMARK 620 2 CYS B  35   SG  115.4
REMARK 620 3 CYS B  91   SG  106.2 123.3
REMARK 620 4 HOH B 502   O    89.9 110.6 106.0
REMARK 620 N                    1     2     3
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 CYS C  91   SG
REMARK 620 2 CYS C  35   SG  128.5
REMARK 620 3 HIS C  88   NE2 107.4 111.6
REMARK 620 N                    1     2
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  88   NE2
REMARK 620 2 CYS D  91   SG  108.9
REMARK 620 3 HOH D 405   O    92.6 100.9
REMARK 620 4 CYS D  35   SG  110.0 126.8 112.1
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1284   RELATED DB: TARGETDB
DBREF  1YLK A    2   163  UNP    P64797   Y1284_MYCTU      2    163
DBREF  1YLK B    2   163  UNP    P64797   Y1284_MYCTU      2    163
DBREF  1YLK C    2   163  UNP    P64797   Y1284_MYCTU      2    163
DBREF  1YLK D    2   163  UNP    P64797   Y1284_MYCTU      2    163
SEQADV 1YLK MET A   -8  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK ALA A   -7  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS A   -6  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS A   -5  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS A   -4  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS A   -3  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS A   -2  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS A   -1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK SER A    0  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK GLY A    1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK MET B   -8  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK ALA B   -7  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS B   -6  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS B   -5  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS B   -4  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS B   -3  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS B   -2  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS B   -1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK SER B    0  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK GLY B    1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK MET C   -8  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK ALA C   -7  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS C   -6  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS C   -5  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS C   -4  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS C   -3  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS C   -2  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS C   -1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK SER C    0  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK GLY C    1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK MET D   -8  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK ALA D   -7  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS D   -6  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS D   -5  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS D   -4  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS D   -3  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS D   -2  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK HIS D   -1  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK SER D    0  UNP  P64797              CLONING ARTIFACT
SEQADV 1YLK GLY D    1  UNP  P64797              CLONING ARTIFACT
SEQRES   1 A  172  MET ALA HIS HIS HIS HIS HIS HIS SER GLY THR VAL THR
SEQRES   2 A  172  ASP ASP TYR LEU ALA ASN ASN VAL ASP TYR ALA SER GLY
SEQRES   3 A  172  PHE LYS GLY PRO LEU PRO MET PRO PRO SER LYS HIS ILE
SEQRES   4 A  172  ALA ILE VAL ALA CYS MET ASP ALA ARG LEU ASP VAL TYR
SEQRES   5 A  172  ARG MET LEU GLY ILE LYS GLU GLY GLU ALA HIS VAL ILE
SEQRES   6 A  172  ARG ASN ALA GLY CYS VAL VAL THR ASP ASP VAL ILE ARG
SEQRES   7 A  172  SER LEU ALA ILE SER GLN ARG LEU LEU GLY THR ARG GLU
SEQRES   8 A  172  ILE ILE LEU LEU HIS HIS THR ASP CYS GLY MET LEU THR
SEQRES   9 A  172  PHE THR ASP ASP ASP PHE LYS ARG ALA ILE GLN ASP GLU
SEQRES  10 A  172  THR GLY ILE ARG PRO THR TRP SER PRO GLU SER TYR PRO
SEQRES  11 A  172  ASP ALA VAL GLU ASP VAL ARG GLN SER LEU ARG ARG ILE
SEQRES  12 A  172  GLU VAL ASN PRO PHE VAL THR LYS HIS THR SER LEU ARG
SEQRES  13 A  172  GLY PHE VAL PHE ASP VAL ALA THR GLY LYS LEU ASN GLU
SEQRES  14 A  172  VAL THR PRO
SEQRES   1 B  172  MET ALA HIS HIS HIS HIS HIS HIS SER GLY THR VAL THR
SEQRES   2 B  172  ASP ASP TYR LEU ALA ASN ASN VAL ASP TYR ALA SER GLY
SEQRES   3 B  172  PHE LYS GLY PRO LEU PRO MET PRO PRO SER LYS HIS ILE
SEQRES   4 B  172  ALA ILE VAL ALA CYS MET ASP ALA ARG LEU ASP VAL TYR
SEQRES   5 B  172  ARG MET LEU GLY ILE LYS GLU GLY GLU ALA HIS VAL ILE
SEQRES   6 B  172  ARG ASN ALA GLY CYS VAL VAL THR ASP ASP VAL ILE ARG
SEQRES   7 B  172  SER LEU ALA ILE SER GLN ARG LEU LEU GLY THR ARG GLU
SEQRES   8 B  172  ILE ILE LEU LEU HIS HIS THR ASP CYS GLY MET LEU THR
SEQRES   9 B  172  PHE THR ASP ASP ASP PHE LYS ARG ALA ILE GLN ASP GLU
SEQRES  10 B  172  THR GLY ILE ARG PRO THR TRP SER PRO GLU SER TYR PRO
SEQRES  11 B  172  ASP ALA VAL GLU ASP VAL ARG GLN SER LEU ARG ARG ILE
SEQRES  12 B  172  GLU VAL ASN PRO PHE VAL THR LYS HIS THR SER LEU ARG
SEQRES  13 B  172  GLY PHE VAL PHE ASP VAL ALA THR GLY LYS LEU ASN GLU
SEQRES  14 B  172  VAL THR PRO
SEQRES   1 C  172  MET ALA HIS HIS HIS HIS HIS HIS SER GLY THR VAL THR
SEQRES   2 C  172  ASP ASP TYR LEU ALA ASN ASN VAL ASP TYR ALA SER GLY
SEQRES   3 C  172  PHE LYS GLY PRO LEU PRO MET PRO PRO SER LYS HIS ILE
SEQRES   4 C  172  ALA ILE VAL ALA CYS MET ASP ALA ARG LEU ASP VAL TYR
SEQRES   5 C  172  ARG MET LEU GLY ILE LYS GLU GLY GLU ALA HIS VAL ILE
SEQRES   6 C  172  ARG ASN ALA GLY CYS VAL VAL THR ASP ASP VAL ILE ARG
SEQRES   7 C  172  SER LEU ALA ILE SER GLN ARG LEU LEU GLY THR ARG GLU
SEQRES   8 C  172  ILE ILE LEU LEU HIS HIS THR ASP CYS GLY MET LEU THR
SEQRES   9 C  172  PHE THR ASP ASP ASP PHE LYS ARG ALA ILE GLN ASP GLU
SEQRES  10 C  172  THR GLY ILE ARG PRO THR TRP SER PRO GLU SER TYR PRO
SEQRES  11 C  172  ASP ALA VAL GLU ASP VAL ARG GLN SER LEU ARG ARG ILE
SEQRES  12 C  172  GLU VAL ASN PRO PHE VAL THR LYS HIS THR SER LEU ARG
SEQRES  13 C  172  GLY PHE VAL PHE ASP VAL ALA THR GLY LYS LEU ASN GLU
SEQRES  14 C  172  VAL THR PRO
SEQRES   1 D  172  MET ALA HIS HIS HIS HIS HIS HIS SER GLY THR VAL THR
SEQRES   2 D  172  ASP ASP TYR LEU ALA ASN ASN VAL ASP TYR ALA SER GLY
SEQRES   3 D  172  PHE LYS GLY PRO LEU PRO MET PRO PRO SER LYS HIS ILE
SEQRES   4 D  172  ALA ILE VAL ALA CYS MET ASP ALA ARG LEU ASP VAL TYR
SEQRES   5 D  172  ARG MET LEU GLY ILE LYS GLU GLY GLU ALA HIS VAL ILE
SEQRES   6 D  172  ARG ASN ALA GLY CYS VAL VAL THR ASP ASP VAL ILE ARG
SEQRES   7 D  172  SER LEU ALA ILE SER GLN ARG LEU LEU GLY THR ARG GLU
SEQRES   8 D  172  ILE ILE LEU LEU HIS HIS THR ASP CYS GLY MET LEU THR
SEQRES   9 D  172  PHE THR ASP ASP ASP PHE LYS ARG ALA ILE GLN ASP GLU
SEQRES  10 D  172  THR GLY ILE ARG PRO THR TRP SER PRO GLU SER TYR PRO
SEQRES  11 D  172  ASP ALA VAL GLU ASP VAL ARG GLN SER LEU ARG ARG ILE
SEQRES  12 D  172  GLU VAL ASN PRO PHE VAL THR LYS HIS THR SER LEU ARG
SEQRES  13 D  172  GLY PHE VAL PHE ASP VAL ALA THR GLY LYS LEU ASN GLU
SEQRES  14 D  172  VAL THR PRO
HET     ZN  A 401       1
HET     ZN  B 402       1
HET     ZN  C 403       1
HET     ZN  D 404       1
HET    SCN  B 501       3
HET    SCN  A 502       3
HET    SCN  C 503       3
HET    SCN  C 504       3
HET    SCN  A 505       3
HETNAM      ZN ZINC ION
HETNAM     SCN THIOCYANATE ION
FORMUL   5   ZN    4(ZN 2+)
FORMUL   9  SCN    5(C N S 1-)
FORMUL  14  HOH   *268(H2 O)
HELIX    1   1 THR A    2  GLY A   17  1                                  16
HELIX    2   2 ASP A   41  GLY A   47  1                                   7
HELIX    3   3 THR A   64  LEU A   77  1                                  14
HELIX    4   4 CYS A   91  THR A   95  5                                   5
HELIX    5   5 THR A   97  GLY A  110  1                                  14
HELIX    6   6 ASP A  122  VAL A  136  1                                  15
HELIX    7   7 THR B    2  PHE B   18  1                                  17
HELIX    8   8 ASP B   41  GLY B   47  1                                   7
HELIX    9   9 THR B   64  LEU B   77  1                                  14
HELIX   10  10 CYS B   91  THR B   95  5                                   5
HELIX   11  11 THR B   97  GLY B  110  1                                  14
HELIX   12  12 ASP B  122  ASN B  137  1                                  16
HELIX   13  13 THR C    2  GLY C   17  1                                  16
HELIX   14  14 ASP C   41  GLY C   47  1                                   7
HELIX   15  15 THR C   64  LEU C   77  1                                  14
HELIX   16  16 CYS C   91  THR C   95  5                                   5
HELIX   17  17 THR C   97  GLY C  110  1                                  14
HELIX   18  18 ASP C  122  VAL C  136  1                                  15
HELIX   19  19 THR D    2  GLY D   17  1                                  16
HELIX   20  20 ASP D   41  LEU D   46  1                                   6
HELIX   21  21 THR D   64  LEU D   77  1                                  14
HELIX   22  22 CYS D   91  THR D   95  5                                   5
HELIX   23  23 THR D   97  GLY D  110  1                                  14
HELIX   24  24 ASP D  122  ASN D  137  1                                  16
SHEET    1   A 5 ALA A  53  ASN A  58  0
SHEET    2   A 5 ILE A  30  CYS A  35  1  N  ILE A  32   O  ILE A  56
SHEET    3   A 5 GLU A  82  HIS A  88  1  O  ILE A  84   N  VAL A  33
SHEET    4   A 5 SER A 145  PHE A 151  1  O  PHE A 149   N  LEU A  85
SHEET    5   A 5 LEU A 158  VAL A 161 -1  O  VAL A 161   N  GLY A 148
SHEET    1   B 5 ALA B  53  ASN B  58  0
SHEET    2   B 5 ILE B  30  CYS B  35  1  N  ILE B  32   O  ILE B  56
SHEET    3   B 5 GLU B  82  HIS B  88  1  O  ILE B  84   N  VAL B  33
SHEET    4   B 5 SER B 145  PHE B 151  1  O  PHE B 149   N  HIS B  87
SHEET    5   B 5 LEU B 158  VAL B 161 -1  O  VAL B 161   N  GLY B 148
SHEET    1   C 5 ALA C  53  ASN C  58  0
SHEET    2   C 5 ILE C  30  CYS C  35  1  N  ILE C  32   O  ILE C  56
SHEET    3   C 5 GLU C  82  HIS C  88  1  O  LEU C  86   N  VAL C  33
SHEET    4   C 5 SER C 145  PHE C 151  1  O  SER C 145   N  ILE C  83
SHEET    5   C 5 LEU C 158  VAL C 161 -1  O  VAL C 161   N  GLY C 148
SHEET    1   D 5 ALA D  53  ASN D  58  0
SHEET    2   D 5 ILE D  30  CYS D  35  1  N  ILE D  32   O  ILE D  56
SHEET    3   D 5 GLU D  82  HIS D  88  1  O  LEU D  86   N  VAL D  33
SHEET    4   D 5 SER D 145  PHE D 151  1  O  PHE D 149   N  HIS D  87
SHEET    5   D 5 LEU D 158  VAL D 161 -1  O  VAL D 161   N  GLY D 148
LINK        ZN    ZN A 401                 NE2 HIS A  88     1555   1555  2.03
LINK        ZN    ZN A 401                 SG  CYS A  91     1555   1555  2.29
LINK        ZN    ZN A 401                 O   HOH A 506     1555   1555  2.24
LINK        ZN    ZN A 401                 SG  CYS A  35     1555   1555  2.33
LINK        ZN    ZN B 402                 NE2 HIS B  88     1555   1555  2.03
LINK        ZN    ZN B 402                 SG  CYS B  35     1555   1555  2.41
LINK        ZN    ZN B 402                 SG  CYS B  91     1555   1555  2.31
LINK        ZN    ZN B 402                 O   HOH B 502     1555   1555  2.22
LINK        ZN    ZN C 403                 SG  CYS C  91     1555   1555  2.32
LINK        ZN    ZN C 403                 SG  CYS C  35     1555   1555  2.31
LINK        ZN    ZN C 403                 NE2 HIS C  88     1555   1555  2.04
LINK        ZN    ZN D 404                 NE2 HIS D  88     1555   1555  2.10
LINK        ZN    ZN D 404                 SG  CYS D  91     1555   1555  2.33
LINK        ZN    ZN D 404                 O   HOH D 405     1555   1555  2.30
LINK        ZN    ZN D 404                 SG  CYS D  35     1555   1555  2.33
CISPEP   1 GLY A   20    PRO A   21          0         4.26
CISPEP   2 GLY B   20    PRO B   21          0         4.03
CISPEP   3 GLY C   20    PRO C   21          0         5.88
CISPEP   4 GLY D   20    PRO D   21          0         2.88
SITE     1 AC1  4 CYS A  35  HIS A  88  CYS A  91  HOH A 506
SITE     1 AC2  4 CYS B  35  HIS B  88  CYS B  91  HOH B 502
SITE     1 AC3  3 CYS C  35  HIS C  88  CYS C  91
SITE     1 AC4  4 CYS D  35  HIS D  88  CYS D  91  HOH D 405
SITE     1 AC5  4 ASP A  37  HOH A 506  HIS B  54  LEU B  78
SITE     1 AC6  4 HIS A  54  LEU A  78  ASP B  37  HOH B 502
SITE     1 AC7  3 ASP C  37  HIS D  54  LEU D  78
SITE     1 AC8  4 HIS C  54  LEU C  78  ASP D  37  HOH D 405
SITE     1 AC9  4 PRO A 121  ASP A 122  GLU A 125  ASP A 126
CRYST1  100.164  154.074  156.943  90.00  90.00  90.00 F 2 2 2      64
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      0.009984  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006490  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006372        0.00000
      
PROCHECK
Go to PROCHECK summary
 References