HEADER LYASE/LYASE INHIBITOR 08-MAR-10 3M2Y
TITLE CARBONIC ANHYDRASE II IN COMPLEX WITH NOVEL SULFONAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CARBONIC ANHYDRASE II;
COMPND 5 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND 6 CARBONIC ANHYDRASE C, CAC;
COMPND 7 EC: 4.2.1.1;
COMPND 8 ENGINEERED: 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 CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1
KEYWDS 10 STRANDED TWISTED BETA-SHEETS, LYASE, DISEASE MUTATION, METAL-
KEYWDS 2 BINDING, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SCHULZE WISCHELER,A.HEINE,G.KLEBE
REVDAT 5 28-FEB-24 3M2Y 1 HETSYN
REVDAT 4 06-SEP-23 3M2Y 1 REMARK SEQADV LINK
REVDAT 3 17-JUL-19 3M2Y 1 REMARK
REVDAT 2 08-NOV-17 3M2Y 1 REMARK
REVDAT 1 25-MAY-11 3M2Y 0
JRNL AUTH J.SCHULZE WISCHELER,N.U.SANDNER,M.HAAKE,C.SUPURAN,A.HEINE,
JRNL AUTH 2 G.KLEBE
JRNL TITL STRUCTURAL INVESTIGATION AND INHIBITOR STUIES ON CARBONIC
JRNL TITL 2 ANHYDRASE II
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.17 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) : 1.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
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) : 0.128
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.127
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.161
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3947
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 77967
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.124
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 70416
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 : 32
REMARK 3 SOLVENT ATOMS : 266
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2339.4
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1975.8
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 7
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 21322
REMARK 3 NUMBER OF RESTRAINTS : 26593
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.021
REMARK 3 ANGLE DISTANCES (A) : 0.030
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.031
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.077
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.081
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.068
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.041
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.080
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 3 ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
REMARK 4
REMARK 4 3M2Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : SILICON
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79675
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.170
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OQ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM SULFATE 50 MM TRIS 0.1
REMARK 280 MM P-CHLOROMERCURIBENZOIC ACID 1 MM SULFONAMIDE, PH 7.8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, 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 20.70000
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 GLY A -4
REMARK 465 SER A -3
REMARK 465 PRO A -2
REMARK 465 GLU A -1
REMARK 465 PHE A 0
REMARK 465 MET A 1
REMARK 465 LYS A 261
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 LYS A 9 CG CD CE NZ
REMARK 470 LYS A 45 CG CD CE NZ
REMARK 470 LYS A 76 CG CD CE NZ
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 HIS A 96 CG HIS A 96 CD2 0.058
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 HIS A 15 CG - ND1 - CE1 ANGL. DEV. = 10.6 DEGREES
REMARK 500 HIS A 15 ND1 - CE1 - NE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG A 27 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 TYR A 51 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 130 OD1 - CG - OD2 ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP A 130 CB - CG - OD1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ASP A 175 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH1 ANGL. DEV. = 3.9 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 17.63 -142.24
REMARK 500 ARG A 27 53.02 -141.42
REMARK 500 GLU A 106 -62.43 -91.53
REMARK 500 LYS A 111 -3.04 74.73
REMARK 500 PHE A 176 61.28 -150.40
REMARK 500 ASN A 244 47.88 -94.42
REMARK 500 LYS A 252 -138.67 54.50
REMARK 500
REMARK 500 REMARK: NULL
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 BE7 A 505
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 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 104.0
REMARK 620 3 HIS A 119 ND1 114.9 98.4
REMARK 620 4 BE0 A 504 N2 107.3 116.1 115.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 501 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 137 O
REMARK 620 2 GLU A 205 O 93.0
REMARK 620 3 HOH A1171 O 133.1 132.6
REMARK 620 N 1 2
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE0 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE0 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BE7 A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KIG RELATED DB: PDB
REMARK 900 RELATED ID: 3KNE RELATED DB: PDB
REMARK 900 RELATED ID: 2Q38 RELATED DB: PDB
REMARK 900 RELATED ID: 3M04 RELATED DB: PDB
REMARK 900 RELATED ID: 3M14 RELATED DB: PDB
REMARK 900 RELATED ID: 3M1K RELATED DB: PDB
REMARK 900 RELATED ID: 3M1Q RELATED DB: PDB
REMARK 900 RELATED ID: 3M1W RELATED DB: PDB
REMARK 900 RELATED ID: 3M2X RELATED DB: PDB
REMARK 900 RELATED ID: 3M2Z RELATED DB: PDB
DBREF 3M2Y A 1 261 UNP P00918 CAH2_HUMAN 1 260
SEQADV 3M2Y GLY A -4 UNP P00918 EXPRESSION TAG
SEQADV 3M2Y SER A -3 UNP P00918 EXPRESSION TAG
SEQADV 3M2Y PRO A -2 UNP P00918 EXPRESSION TAG
SEQADV 3M2Y GLU A -1 UNP P00918 EXPRESSION TAG
SEQADV 3M2Y PHE A 0 UNP P00918 EXPRESSION TAG
SEQRES 1 A 265 GLY SER PRO GLU PHE MET SER HIS HIS TRP GLY TYR GLY
SEQRES 2 A 265 LYS HIS ASN GLY PRO GLU HIS TRP HIS LYS ASP PHE PRO
SEQRES 3 A 265 ILE ALA LYS GLY GLU ARG GLN SER PRO VAL ASP ILE ASP
SEQRES 4 A 265 THR HIS THR ALA LYS TYR ASP PRO SER LEU LYS PRO LEU
SEQRES 5 A 265 SER VAL SER TYR ASP GLN ALA THR SER LEU ARG ILE LEU
SEQRES 6 A 265 ASN ASN GLY HIS ALA PHE ASN VAL GLU PHE ASP ASP SER
SEQRES 7 A 265 GLN ASP LYS ALA VAL LEU LYS GLY GLY PRO LEU ASP GLY
SEQRES 8 A 265 THR TYR ARG LEU ILE GLN PHE HIS PHE HIS TRP GLY SER
SEQRES 9 A 265 LEU ASP GLY GLN GLY SER GLU HIS THR VAL ASP LYS LYS
SEQRES 10 A 265 LYS TYR ALA ALA GLU LEU HIS LEU VAL HIS TRP ASN THR
SEQRES 11 A 265 LYS TYR GLY ASP PHE GLY LYS ALA VAL GLN GLN PRO ASP
SEQRES 12 A 265 GLY LEU ALA VAL LEU GLY ILE PHE LEU LYS VAL GLY SER
SEQRES 13 A 265 ALA LYS PRO GLY LEU GLN LYS VAL VAL ASP VAL LEU ASP
SEQRES 14 A 265 SER ILE LYS THR LYS GLY LYS SER ALA ASP PHE THR ASN
SEQRES 15 A 265 PHE ASP PRO ARG GLY LEU LEU PRO GLU SER LEU ASP TYR
SEQRES 16 A 265 TRP THR TYR PRO GLY SER LEU THR THR PRO PRO LEU LEU
SEQRES 17 A 265 GLU CYS VAL THR TRP ILE VAL LEU LYS GLU PRO ILE SER
SEQRES 18 A 265 VAL SER SER GLU GLN VAL LEU LYS PHE ARG LYS LEU ASN
SEQRES 19 A 265 PHE ASN GLY GLU GLY GLU PRO GLU GLU LEU MET VAL ASP
SEQRES 20 A 265 ASN TRP ARG PRO ALA GLN PRO LEU LYS ASN ARG GLN ILE
SEQRES 21 A 265 LYS ALA SER PHE LYS
HET ZN A 500 1
HET HG A 501 1
HET ZN A 502 1
HET BE0 A 503 10
HET BE0 A 504 10
HET BE7 A 505 9
HETNAM ZN ZINC ION
HETNAM HG MERCURY (II) ION
HETNAM BE0 PIPERIDINE-1-SULFONAMIDE
HETNAM BE7 (4-CARBOXYPHENYL)(CHLORO)MERCURY
HETSYN BE7 P-CHLOROMERCURIBENZOIC ACID;(4-CARBOXYPHENYL)-
HETSYN 2 BE7 CHLORANYL-MERCURY
FORMUL 2 ZN 2(ZN 2+)
FORMUL 3 HG HG 2+
FORMUL 5 BE0 2(C5 H12 N2 O2 S)
FORMUL 7 BE7 C7 H5 CL HG O2
FORMUL 8 HOH *266(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 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 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 ND1 HIS A 64 ZN ZN A 502 1555 1555 2.49
LINK NE2 HIS A 94 ZN ZN A 500 1555 1555 1.99
LINK NE2 HIS A 96 ZN ZN A 500 1555 1555 2.01
LINK ND1 HIS A 119 ZN ZN A 500 1555 1555 2.04
LINK O GLN A 137 HG HG A 501 1555 1555 2.96
LINK O GLU A 205 HG HG A 501 1555 1555 3.02
LINK ZN ZN A 500 N2 BE0 A 504 1555 1555 1.96
LINK HG HG A 501 O HOH A1171 1555 1555 2.96
CISPEP 1 SER A 29 PRO A 30 0 -1.44
CISPEP 2 PRO A 201 PRO A 202 0 12.61
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 BE0 A 504
SITE 1 AC2 5 GLN A 137 GLU A 205 CYS A 206 BE7 A 505
SITE 2 AC2 5 HOH A1171
SITE 1 AC3 3 ASN A 62 GLY A 63 HIS A 64
SITE 1 AC4 8 HIS A 3 TRP A 5 HIS A 10 HIS A 15
SITE 2 AC4 8 TRP A 16 ASP A 19 PHE A 20 HOH A1200
SITE 1 AC5 9 HIS A 94 HIS A 96 HIS A 119 VAL A 121
SITE 2 AC5 9 LEU A 198 THR A 199 THR A 200 TRP A 209
SITE 3 AC5 9 ZN A 500
SITE 1 AC6 4 GLN A 136 PRO A 138 GLU A 205 HG A 501
CRYST1 42.400 41.400 72.200 90.00 104.60 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 0.023585 0.000000 0.006143 0.00000
SCALE2 0.000000 0.024155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014313 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
