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PDBsum entry 3oik

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Lyase PDB id
3oik
Jmol
Contents
Protein chain
258 a.a.
Ligands
WZB
GOL
Metals
_ZN
Waters ×374
HEADER    LYASE                                   19-AUG-10   3OIK
TITLE     HUMAN CARBONIC ANHYDRASE II MUTANT A65S, N67Q (CA IX MIMIC) BOUND BY
TITLE    2 2-ETHYLESTRADIOL 3,17-O,O-BIS-SULFAMATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   5 CARBONIC ANHYDRASE C, CAC;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    2-ETHYLESTRONE, ESTRADIOL, SULFAMATE, MIXED ALPHA-BETA, CARBON
KEYWDS   2 DIOXIDE/BICARBONATE CONVERSION, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.H.SIPPEL,B.A.STANDER,A.H.ROBBINS,C.K.TU,M.AGBANDJE-MCKENNA,
AUTHOR   2 D.N.SILVERMAN,A.M.JOUBERT,R.MCKENNA
REVDAT   1   06-JUL-11 3OIK    0
JRNL        AUTH   K.H.SIPPEL,B.A.STANDER,A.H.ROBBINS,C.K.TU,
JRNL        AUTH 2 M.AGBANDJE-MCKENNA,D.N.SILVERMAN,A.M.JOUBERT,R.MCKENNA
JRNL        TITL   CHARACTERIZATION OF CARBONIC ANHYDRASE ISOZYME SPECIFIC
JRNL        TITL 2 INHIBITION BY SULFAMATED 2-ETHYLESTRA COMPOUNDS
JRNL        REF    LETT.DRUG DES.DISCOVERY       V.   8       2011
JRNL        REFN                   ISSN 1570-1808
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.E.COZIER,M.P.LEESE,M.D.LLOYD,M.D.BAKER,N.THIYAGARAJAN,
REMARK   1  AUTH 2 K.R.ACHARYA,B.V.POTTER
REMARK   1  TITL   STRUCTURES OF HUMAN CARBONIC ANHYDRASE II/INHIBITOR
REMARK   1  TITL 2 COMPLEXES REVEAL A SECOND BINDING SITE FOR STEROIDAL AND
REMARK   1  TITL 3 NONSTEROIDAL INHIBITORS.
REMARK   1  REF    BIOCHEMISTRY                  V.  49  3464 2010
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   20297840
REMARK   1  DOI    10.1021/BI902178W
REMARK   1 REFERENCE 2
REMARK   1  AUTH   C.GENIS,K.H.SIPPEL,N.CASE,W.CAO,B.S.AVVARU,L.J.TARTAGLIA,
REMARK   1  AUTH 2 L.GOVINDASAMY,C.TU,M.AGBANDJE-MCKENNA,D.N.SILVERMAN,
REMARK   1  AUTH 3 C.J.ROSSER,R.MCKENNA
REMARK   1  TITL   DESIGN OF A CARBONIC ANHYDRASE IX ACTIVE-SITE MIMIC TO
REMARK   1  TITL 2 SCREEN INHIBITORS FOR POSSIBLE ANTICANCER PROPERTIES.
REMARK   1  REF    BIOCHEMISTRY                  V.  48  1322 2009
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   19170619
REMARK   1  DOI    10.1021/BI802035F
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_467)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.32
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.2
REMARK   3   NUMBER OF REFLECTIONS             : 35886
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.137
REMARK   3   R VALUE            (WORKING SET) : 0.135
REMARK   3   FREE R VALUE                     : 0.163
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.530
REMARK   3   FREE R VALUE TEST SET COUNT      : 1985
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 25.3202 -  3.2289    0.99     3747   218  0.1260 0.1433
REMARK   3     2  3.2289 -  2.5637    0.98     3603   214  0.1253 0.1572
REMARK   3     3  2.5637 -  2.2398    0.97     3578   209  0.1176 0.1342
REMARK   3     4  2.2398 -  2.0351    0.95     3475   206  0.1264 0.1583
REMARK   3     5  2.0351 -  1.8893    0.94     3437   203  0.1293 0.1680
REMARK   3     6  1.8893 -  1.7779    0.91     3370   189  0.1210 0.1398
REMARK   3     7  1.7779 -  1.6889    0.89     3217   190  0.1323 0.1993
REMARK   3     8  1.6889 -  1.6154    0.87     3212   190  0.1606 0.2164
REMARK   3     9  1.6154 -  1.5532    0.87     3154   188  0.2053 0.2381
REMARK   3    10  1.5532 -  1.5000    0.85     3108   178  0.3070 0.3409
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.60
REMARK   3   SHRINKAGE RADIUS   : 0.41
REMARK   3   K_SOL              : 0.44
REMARK   3   B_SOL              : 54.45
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.950
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 12.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.61
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.96870
REMARK   3    B22 (A**2) : -0.72680
REMARK   3    B33 (A**2) : 1.69550
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.15210
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.014           2393
REMARK   3   ANGLE     :  1.603           3296
REMARK   3   CHIRALITY :  0.114            347
REMARK   3   PLANARITY :  0.010            426
REMARK   3   DIHEDRAL  : 14.424            945
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 5
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (CHAIN A AND RESID 3:9)
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6220  -4.7598  10.8168
REMARK   3    T TENSOR
REMARK   3      T11:   0.1133 T22:   0.1281
REMARK   3      T33:   0.1616 T12:  -0.0003
REMARK   3      T13:   0.0505 T23:   0.0154
REMARK   3    L TENSOR
REMARK   3      L11:   0.0654 L22:   0.0047
REMARK   3      L33:   0.0491 L12:  -0.0174
REMARK   3      L13:   0.0210 L23:  -0.0032
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0477 S12:   0.0624 S13:  -0.1221
REMARK   3      S21:  -0.0175 S22:  -0.0894 S23:  -0.1642
REMARK   3      S31:  -0.0376 S32:   0.1685 S33:  -0.0066
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (CHAIN A AND RESID 10:45)
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6615  -3.5654  27.4479
REMARK   3    T TENSOR
REMARK   3      T11:   0.0737 T22:   0.1063
REMARK   3      T33:   0.0641 T12:   0.0122
REMARK   3      T13:   0.0126 T23:  -0.0007
REMARK   3    L TENSOR
REMARK   3      L11:   0.2277 L22:   0.1741
REMARK   3      L33:   0.2889 L12:  -0.0168
REMARK   3      L13:   0.1195 L23:  -0.2114
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0860 S12:  -0.1585 S13:  -0.0830
REMARK   3      S21:   0.0949 S22:   0.0372 S23:  -0.1107
REMARK   3      S31:   0.0134 S32:   0.0635 S33:  -0.0041
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (CHAIN A AND RESID 46:87)
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8341   6.5292  13.2992
REMARK   3    T TENSOR
REMARK   3      T11:   0.0962 T22:   0.0894
REMARK   3      T33:   0.1216 T12:   0.0079
REMARK   3      T13:  -0.0091 T23:   0.0042
REMARK   3    L TENSOR
REMARK   3      L11:   0.1079 L22:   0.1447
REMARK   3      L33:   0.1198 L12:   0.0721
REMARK   3      L13:   0.1238 L23:   0.0254
REMARK   3    S TENSOR
REMARK   3      S11:   0.0107 S12:   0.0004 S13:   0.1085
REMARK   3      S21:  -0.0790 S22:  -0.0214 S23:   0.0572
REMARK   3      S31:  -0.0824 S32:  -0.0267 S33:   0.0000
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (CHAIN A AND RESID 88:251)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3368  -3.6881  13.5239
REMARK   3    T TENSOR
REMARK   3      T11:   0.0551 T22:   0.0387
REMARK   3      T33:   0.0465 T12:  -0.0024
REMARK   3      T13:  -0.0016 T23:   0.0018
REMARK   3    L TENSOR
REMARK   3      L11:   0.4907 L22:   0.2107
REMARK   3      L33:   0.3823 L12:  -0.0477
REMARK   3      L13:  -0.0291 L23:  -0.0222
REMARK   3    S TENSOR
REMARK   3      S11:   0.0017 S12:   0.0003 S13:  -0.0034
REMARK   3      S21:  -0.0406 S22:   0.0031 S23:   0.0059
REMARK   3      S31:   0.0067 S32:   0.0033 S33:  -0.0000
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (CHAIN A AND RESID 252:261)
REMARK   3    ORIGIN FOR THE GROUP (A): -12.0686  -3.5613  34.6073
REMARK   3    T TENSOR
REMARK   3      T11:   0.0991 T22:   0.1423
REMARK   3      T33:   0.0851 T12:   0.0054
REMARK   3      T13:   0.0123 T23:   0.0043
REMARK   3    L TENSOR
REMARK   3      L11:   0.1186 L22:   0.1679
REMARK   3      L33:   0.3126 L12:  -0.0294
REMARK   3      L13:  -0.0345 L23:   0.0734
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0274 S12:  -0.1875 S13:  -0.0036
REMARK   3      S21:   0.0911 S22:   0.1057 S23:  -0.0142
REMARK   3      S31:   0.1396 S32:   0.0074 S33:   0.1137
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: INDIVIDUAL COORDINATE, INDIVIDUAL
REMARK   3  ISOTROPIC ADP, TLS, OCCUPANCY, HYDROGEN WRITING
REMARK   4
REMARK   4 3OIK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061160.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-JUN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 9.0
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) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : OSMIC MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35886
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.2
REMARK 200  DATA REDUNDANCY                : 5.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05700
REMARK 200   FOR THE DATA SET  : 25.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.39000
REMARK 200   FOR SHELL         : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.6.3_467)
REMARK 200 STARTING MODEL: PDB ENTRY 2ILI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM CITRATE, 100 MM TRIS, 7.5
REMARK 280  MM 2-ETHYLESTRADIOL 3,17-O,O-BIS-SULFAMATE, PH 9.0, VAPOR
REMARK 280  DIFFUSION, HANGING 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       20.66100
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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     1
REMARK 465     SER A     2
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   O    PRO A    46     O    HOH A   457              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  11       16.61   -140.43
REMARK 500    ARG A  27       56.32   -141.62
REMARK 500    LYS A 111       -3.37     72.50
REMARK 500    ASN A 244       50.07    -98.58
REMARK 500    LYS A 252     -136.50     53.17
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 528        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH A 541        DISTANCE =  6.63 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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  94   NE2
REMARK 620 2 HIS A  96   NE2 104.9
REMARK 620 3 HIS A 119   ND1 111.1  98.1
REMARK 620 4 WZB A 300   NAD 111.2 117.5 113.1
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WZB A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OIL   RELATED DB: PDB
REMARK 900 RELATED ID: 3OIM   RELATED DB: PDB
REMARK 900 RELATED ID: 3OKU   RELATED DB: PDB
REMARK 900 RELATED ID: 3OKV   RELATED DB: PDB
DBREF  3OIK A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 3OIK SER A   65  UNP  P00918    ALA    65 ENGINEERED MUTATION
SEQADV 3OIK GLN A   67  UNP  P00918    ASN    67 ENGINEERED MUTATION
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS SER
SEQRES   6 A  260  PHE GLN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET    WZB  A 300      34
HET    GOL  A 301       7
HETNAM      ZN ZINC ION
HETNAM     WZB (9BETA,13ALPHA,14BETA,17ALPHA)-2-ETHYLESTRA-1(10),2,4-
HETNAM   2 WZB  TRIENE-3,17-DIYL DISULFAMATE
HETNAM     GOL GLYCEROL
HETSYN     WZB 2-ETHYLESTRADIOL 3,17-O,O-BIS-SULFAMATE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  WZB    C20 H30 N2 O6 S2
FORMUL   4  GOL    C3 H8 O3
FORMUL   5  HOH   *359(H2 O)
HELIX    1   1 GLY A   12  ASP A   19  5                                   8
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -1  O  VAL A  78   N  SER A  50
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  VAL A 121   N  GLN A  92
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.03
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.02
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.04
LINK        ZN    ZN A 262                 NAD WZB A 300     1555   1555  1.94
CISPEP   1 SER A   29    PRO A   30          0        -2.49
CISPEP   2 PRO A  201    PRO A  202          0         7.82
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  WZB A 300
SITE     1 AC2 12 HIS A  64  GLN A  92  HIS A  94  HIS A  96
SITE     2 AC2 12 HIS A 119  VAL A 143  LEU A 198  THR A 199
SITE     3 AC2 12 THR A 200   ZN A 262  GOL A 301  HOH A 409
SITE     1 AC3  4 GLN A  92  WZB A 300  HOH A 448  HOH A 599
CRYST1   42.238   41.322   72.201  90.00 104.34  90.00 P 1 21 1      2
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.023675  0.000000  0.006052        0.00000
SCALE2      0.000000  0.024200  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014296        0.00000
      
PROCHECK
Go to PROCHECK summary
 References