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PDBsum entry 3po6

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Lyase/lyase inhibitor PDB id
3po6
Jmol
Contents
Protein chain
258 a.a.
Ligands
DT9
RDT
GOL ×4
ACT
Metals
_ZN
Waters ×313
HEADER    LYASE/LYASE INHIBITOR                   22-NOV-10   3PO6
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II WITH 6,7-DIMETHOXY-1-
TITLE    2 METHYL-3,4-DIHYDROISOQUINOLINE-2(1H)-SULFONAMIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND   5 CARBONIC ANHYDRASE II, CA-II;
COMPND   6 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    CARBONIC ANHYDRASE, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.MADER,J.BRYNDA,R.GITTO,S.AGNELLO,S.FERRO,L.DE LUCA,D.VULLO,
AUTHOR   2 C.T.SUPURAN,A.CHIMIRRI
REVDAT   2   07-DEC-11 3PO6    1       JRNL   VERSN
REVDAT   1   06-APR-11 3PO6    0
JRNL        AUTH   P.MADER,J.BRYNDA,R.GITTO,S.AGNELLO,P.PACHL,C.T.SUPURAN,
JRNL        AUTH 2 A.CHIMIRRI,P.REZACOVA
JRNL        TITL   STRUCTURAL BASIS FOR THE INTERACTION BETWEEN CARBONIC
JRNL        TITL 2 ANHYDRASE AND
JRNL        TITL 3 1,2,3,4-TETRAHYDROISOQUINOLIN-2-YLSULFONAMIDES.
JRNL        REF    J.MED.CHEM.                   V.  54  2522 2011
JRNL        REFN                   ISSN 0022-2623
JRNL        PMID   21395315
JRNL        DOI    10.1021/JM2000213
REMARK   2
REMARK   2 RESOLUTION.    1.47 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0102
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.27
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 38750
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) : 0.145
REMARK   3   R VALUE            (WORKING SET) : 0.143
REMARK   3   FREE R VALUE                     : 0.175
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2045
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.47
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.51
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2850
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.37
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860
REMARK   3   BIN FREE R VALUE SET COUNT          : 132
REMARK   3   BIN FREE R VALUE                    : 0.2240
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2043
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 66
REMARK   3   SOLVENT ATOMS            : 313
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 13.74
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.02
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.04000
REMARK   3    B22 (A**2) : -0.05000
REMARK   3    B33 (A**2) : 0.05000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.10000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.063
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.039
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.227
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2264 ; 0.014 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  1528 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3084 ; 1.689 ; 1.973
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3749 ; 2.059 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   269 ; 6.352 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;34.916 ;25.000
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   375 ;12.605 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;20.569 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   321 ; 0.109 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2481 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   432 ; 0.002 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1314 ; 1.842 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   526 ; 0.515 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2139 ; 2.699 ; 3.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   950 ; 2.548 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   936 ; 3.726 ; 3.000
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  : 3
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     3        A    45
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.5500  -2.9160  23.6430
REMARK   3    T TENSOR
REMARK   3      T11:   0.0201 T22:   0.0703
REMARK   3      T33:   0.0701 T12:   0.0040
REMARK   3      T13:  -0.0143 T23:  -0.0103
REMARK   3    L TENSOR
REMARK   3      L11:   1.1037 L22:   0.5841
REMARK   3      L33:   0.9795 L12:  -0.0608
REMARK   3      L13:  -0.3537 L23:  -0.4762
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0750 S12:  -0.0791 S13:   0.0013
REMARK   3      S21:   0.0474 S22:   0.0290 S23:  -0.1399
REMARK   3      S31:   0.0335 S32:   0.0700 S33:   0.0460
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 :   A    46        A   255
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3080  -1.5610  13.9650
REMARK   3    T TENSOR
REMARK   3      T11:   0.0483 T22:   0.0396
REMARK   3      T33:   0.0567 T12:  -0.0068
REMARK   3      T13:  -0.0199 T23:   0.0089
REMARK   3    L TENSOR
REMARK   3      L11:   0.3116 L22:   0.7345
REMARK   3      L33:   0.4746 L12:  -0.0018
REMARK   3      L13:  -0.1464 L23:   0.1086
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0148 S12:  -0.0117 S13:   0.0148
REMARK   3      S21:  -0.1112 S22:   0.0362 S23:   0.0329
REMARK   3      S31:  -0.0176 S32:  -0.0187 S33:  -0.0214
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 :   A   256        A   260
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9480  -4.8640  34.0460
REMARK   3    T TENSOR
REMARK   3      T11:   0.0347 T22:   0.1656
REMARK   3      T33:   0.0542 T12:  -0.0095
REMARK   3      T13:   0.0246 T23:   0.0578
REMARK   3    L TENSOR
REMARK   3      L11:  24.2204 L22:   7.4787
REMARK   3      L33:   5.1416 L12:   3.7930
REMARK   3      L13:   8.5263 L23:   1.7072
REMARK   3    S TENSOR
REMARK   3      S11:   0.1790 S12:  -1.4465 S13:  -0.5039
REMARK   3      S21:   0.4296 S22:  -0.0403 S23:   0.2403
REMARK   3      S31:   0.0834 S32:  -0.4352 S33:  -0.1387
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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 3PO6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-DEC-10.
REMARK 100 THE RCSB ID CODE IS RCSB062613.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-MAY-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : X12
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95370
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39222
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.470
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.620
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.05300
REMARK 200  R SYM                      (I) : 0.05300
REMARK 200   FOR THE DATA SET  : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-CL, 2.5M AMMONIUM SULFATE,
REMARK 280  0.3M SODIUM CHLORIDE, PH 8.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
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       20.60500
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     SER A     2
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   4    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A   9    CE   NZ
REMARK 470     LYS A  45    CD   CE   NZ
REMARK 470     LYS A 133    CD   CE   NZ
REMARK 470     LYS A 261    CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HIS A     3     CAG  RDT A   263              2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NH2  ARG A    27     O    HOH A   510     2556     1.85
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    LYS A  76      -86.42   -117.13
REMARK 500    LYS A 111       -2.84     71.47
REMARK 500    PHE A 176       68.85   -150.29
REMARK 500    ASN A 244       47.91    -96.34
REMARK 500    LYS A 252     -135.07     53.60
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 451        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH A 543        DISTANCE =  5.05 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     ACT A  268
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   1  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT9 A 262   NAD
REMARK 620 2 HIS A  94   NE2 114.7
REMARK 620 3 HIS A  96   NE2 112.3 104.6
REMARK 620 4 HIS A 119   ND1 113.6 113.3  96.5
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DT9 A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RDT A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 268
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IGP   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER LIGAND
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE NUMBER 126 IS SIMPLY SKIPPED.
DBREF  3PO6 A    2   261  UNP    P00918   CAH2_HUMAN       2    260
SEQRES   1 A  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES   2 A  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES   8 A  259  PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES  10 A  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES  11 A  259  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A   1       1
HET    DT9  A 262      19
HET    RDT  A 263      19
HET    GOL  A 264       6
HET    GOL  A 265       6
HET    GOL  A 266       6
HET    GOL  A 267       6
HET    ACT  A 268       3
HETNAM      ZN ZINC ION
HETNAM     DT9 (1S)-6,7-DIMETHOXY-1-METHYL-3,4-DIHYDROISOQUINOLINE-
HETNAM   2 DT9  2(1H)-SULFONAMIDE
HETNAM     RDT (1R)-6,7-DIMETHOXY-1-METHYL-3,4-DIHYDROISOQUINOLINE-
HETNAM   2 RDT  2(1H)-SULFONAMIDE
HETNAM     GOL GLYCEROL
HETNAM     ACT ACETATE ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  DT9    C12 H18 N2 O4 S
FORMUL   4  RDT    C12 H18 N2 O4 S
FORMUL   5  GOL    4(C3 H8 O3)
FORMUL   9  ACT    C2 H3 O2 1-
FORMUL  10  HOH   *313(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  LYS A  80   N  SER A  48
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        ZN    ZN A   1                 NAD DT9 A 262     1555   1555  1.93
LINK         NE2 HIS A  94                ZN    ZN A   1     1555   1555  2.00
LINK         NE2 HIS A  96                ZN    ZN A   1     1555   1555  2.04
LINK         ND1 HIS A 119                ZN    ZN A   1     1555   1555  2.05
CISPEP   1 SER A   29    PRO A   30          0        -0.58
CISPEP   2 PRO A  201    PRO A  202          0         9.23
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  DT9 A 262
SITE     1 AC2 11  ZN A   1  ASN A  67  GLN A  92  HIS A  94
SITE     2 AC2 11 HIS A  96  HIS A 119  PHE A 131  LEU A 198
SITE     3 AC2 11 THR A 199  THR A 200  HOH A 513
SITE     1 AC3 16 HIS A   3  TRP A   5  HIS A  10  ASN A  11
SITE     2 AC3 16 HIS A  15  TRP A  16  ASP A  19  ASP A 180
SITE     3 AC3 16 ARG A 182  GLY A 183  ACT A 268  HOH A 300
SITE     4 AC3 16 HOH A 369  HOH A 408  HOH A 541  HOH A 555
SITE     1 AC4  5 TYR A   7  ASP A 243  TRP A 245  HOH A 269
SITE     2 AC4  5 HOH A 504
SITE     1 AC5  7 GLY A  63  LYS A 170  PHE A 231  ASN A 232
SITE     2 AC5  7 GLU A 239  HOH A 357  HOH A 558
SITE     1 AC6  4 TYR A 114  LYS A 149  PRO A 215  HOH A 355
SITE     1 AC7  5 GLU A  69  PHE A  70  ASP A  72  ILE A  91
SITE     2 AC7  5 HOH A 511
SITE     1 AC8  8 HIS A  10  HIS A  15  LYS A  18  LYS A 154
SITE     2 AC8  8 ARG A 182  LEU A 185  RDT A 263  HOH A 455
CRYST1   42.180   41.210   72.000  90.00 104.31  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      0.023708  0.000000  0.006047        0.00000
SCALE2      0.000000  0.024266  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014334        0.00000
      
PROCHECK
Go to PROCHECK summary
 References