HEADER LYASE/LYASE INHIBITOR 15-APR-11 3RJ7
TITLE HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH ITS INHIBITOR RHENIUM(I)
TITLE 2 TRISCARBONYL-CYCLOPENTADIENYL-CARBOXY-4-AMINOMETHYLBENZENE-
TITLE 3 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;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS INHIBITOR, TRANSITION METAL COMPLEX, ANHYDRASE, CARBON DIOXIDE,
KEYWDS 2 LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SPINGLER,D.CAN,R.ALBERTO
REVDAT 5 13-SEP-23 3RJ7 1 REMARK LINK
REVDAT 4 08-NOV-17 3RJ7 1 REMARK
REVDAT 3 17-OCT-12 3RJ7 1 JRNL
REVDAT 2 07-MAR-12 3RJ7 1 JRNL
REVDAT 1 29-FEB-12 3RJ7 0
JRNL AUTH D.CAN,B.SPINGLER,P.SCHMUTZ,F.MENDES,P.RAPOSINHO,C.FERNANDES,
JRNL AUTH 2 F.CARTA,A.INNOCENTI,I.SANTOS,C.T.SUPURAN,R.ALBERTO
JRNL TITL [(CP-R)M(CO)(3) ] (M=RE OR (99M) TC) ARYLSULFONAMIDE,
JRNL TITL 2 ARYLSULFAMIDE, AND ARYLSULFAMATE CONJUGATES FOR SELECTIVE
JRNL TITL 3 TARGETING OF HUMAN CARBONIC ANHYDRASE IX.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 51 3354 2012
JRNL REFN ISSN 1433-7851
JRNL PMID 22344779
JRNL DOI 10.1002/ANIE.201107333
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.166
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.166
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 7121
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 142060
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.153
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.153
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 6109
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 121548
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2053
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2429.8
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 15
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 10049
REMARK 3 NUMBER OF RESTRAINTS : 9185
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.018
REMARK 3 ANGLE DISTANCES (A) : 0.033
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.032
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.091
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.093
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.020
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.050
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RJ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064997.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : BARTELS MONOCHROMATOR
REMARK 200 OPTICS : MIRROR, BARTELS MONOCHROMATOR,
REMARK 200 DUAL CHANNEL CUT CRYSTALS,
REMARK 200 TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121548
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 2.020
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03080
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.27
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.710
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3IQK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULFATE, 0.1 M TRIS
REMARK 280 -HCL, PH 8.0, 1 MM 4-HYDROXYMERCURIBENZOIC ACID, 5% V/V DMSO, 4
REMARK 280 WEEKS AT 298K, 2 WEEKS AT 277K, 4 WEEKS AGAIN AT 298K, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
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 20.81950
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 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 3 N CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 206 CB CYS A 206 SG -0.121
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TYR A 88 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ASP A 130 OD1 - CG - OD2 ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASP A 130 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP A 139 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 162 CB - CG - OD2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 ASP A 175 OD1 - CG - OD2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 ASP A 175 CB - CG - OD1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 CYS A 206 CA - CB - SG ANGL. DEV. = 20.9 DEGREES
REMARK 500 GLU A 221 OE1 - CD - OE2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 PHE A 226 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 PHE A 226 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASN A 253 O - C - N ANGL. DEV. = 11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 11 17.91 -143.27
REMARK 500 ARG A 27 57.14 -142.26
REMARK 500 LYS A 76 -98.95 -105.14
REMARK 500 GLU A 106 -61.92 -96.28
REMARK 500 LYS A 111 -2.42 69.42
REMARK 500 PHE A 176 60.74 -152.89
REMARK 500 ASN A 244 52.51 -98.67
REMARK 500 LYS A 252 -136.90 52.61
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 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 105.0
REMARK 620 3 HIS A 119 ND1 113.7 98.4
REMARK 620 4 RCS A 302 N2 107.4 114.5 117.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MBO A 301 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 135 O
REMARK 620 2 MBO A 301 CE1 131.2
REMARK 620 3 GLN A 137 O 112.5 76.3
REMARK 620 4 CYS A 206 SG 76.4 152.3 93.4
REMARK 620 5 HOH A 392 O 63.7 80.9 142.9 119.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MBO A 301 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 137 O
REMARK 620 2 MBO A 301 CE1 100.8
REMARK 620 3 GLU A 205 O 94.0 86.2
REMARK 620 4 CYS A 206 SG 82.3 176.8 93.6
REMARK 620 5 HOH A 392 O 130.7 100.2 131.5 77.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RCS A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RCS A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 314
DBREF 3RJ7 A 3 261 UNP P00918 CAH2_HUMAN 3 260
SEQRES 1 A 258 HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS
SEQRES 2 A 258 TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN
SEQRES 3 A 258 SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP
SEQRES 4 A 258 PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA
SEQRES 5 A 258 THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN
SEQRES 6 A 258 VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS
SEQRES 7 A 258 GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE
SEQRES 8 A 258 HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU
SEQRES 9 A 258 HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS
SEQRES 10 A 258 LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS
SEQRES 11 A 258 ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE
SEQRES 12 A 258 PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS
SEQRES 13 A 258 VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS
SEQRES 14 A 258 SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU
SEQRES 15 A 258 PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU
SEQRES 16 A 258 THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL
SEQRES 17 A 258 LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU
SEQRES 18 A 258 LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO
SEQRES 19 A 258 GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO
SEQRES 20 A 258 LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 300 1
HET MBO A 301 11
HET RCS A 302 28
HET RCS A 303 26
HET DMS A 314 4
HETNAM ZN ZINC ION
HETNAM MBO MERCURIBENZOIC ACID
HETNAM RCS TRISCARBONYL-CYCLOPENTADIENYL-CARBOXY-4-
HETNAM 2 RCS AMINOMETHYLBENZENE-SULFONAMIDE RHENIUM(I)
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 MBO C7 H5 HG O2
FORMUL 4 RCS 2(C16 H13 N2 O6 RE S)
FORMUL 6 DMS C2 H6 O S
FORMUL 7 HOH *333(H2 O)
HELIX 1 1 HIS A 15 ASP A 19 5 5
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 LEU A 212
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 HIS A 94 O HIS A 119
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 LYS A 45 SER A 50 0
SHEET 2 C 6 VAL A 78 GLY A 82 -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 HIS A 119 N HIS A 94
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 300 1555 1555 2.00
LINK NE2 HIS A 96 ZN ZN A 300 1555 1555 2.04
LINK ND1 HIS A 119 ZN ZN A 300 1555 1555 2.03
LINK O VAL A 135 HG BMBO A 301 1555 1555 3.15
LINK O GLN A 137 HG AMBO A 301 1555 1555 3.01
LINK O GLN A 137 HG BMBO A 301 1555 1555 3.18
LINK O GLU A 205 HG AMBO A 301 1555 1555 3.00
LINK SG ACYS A 206 HG AMBO A 301 1555 1555 2.35
LINK SG BCYS A 206 HG BMBO A 301 1555 1555 2.35
LINK ZN ZN A 300 N2 RCS A 302 1555 1555 1.97
LINK HG BMBO A 301 O HOH A 392 1555 1555 2.26
LINK HG AMBO A 301 O HOH A 392 1555 1555 2.66
CISPEP 1 HIS A 3 HIS A 4 0 -0.39
CISPEP 2 SER A 29 PRO A 30 0 -3.78
CISPEP 3 PRO A 201 PRO A 202 0 9.56
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 RCS A 302
SITE 1 AC2 8 VAL A 135 GLN A 136 GLN A 137 PRO A 138
SITE 2 AC2 8 GLU A 205 CYS A 206 HOH A 392 HOH A 640
SITE 1 AC3 12 HIS A 94 HIS A 96 HIS A 119 PHE A 131
SITE 2 AC3 12 GLY A 132 LEU A 198 THR A 199 THR A 200
SITE 3 AC3 12 PRO A 202 TRP A 209 ZN A 300 HOH A 432
SITE 1 AC4 15 HIS A 4 TRP A 5 HIS A 10 ASN A 11
SITE 2 AC4 15 HIS A 15 TRP A 16 ASP A 19 PHE A 20
SITE 3 AC4 15 PRO A 155 GLY A 156 GLY A 183 HOH A 538
SITE 4 AC4 15 HOH A 607 HOH A 693 HOH A 696
SITE 1 AC5 4 TYR A 7 ASP A 243 TRP A 245 HOH A 623
CRYST1 42.243 41.639 72.107 90.00 104.55 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 0.023673 0.000000 0.006144 0.00000
SCALE2 0.000000 0.024016 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014328 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
