HEADER LYASE/LYASE INHIBITOR 10-MAR-10 3M40
TITLE CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE ISOZYME II WITH 4-[N-(6-
TITLE 2 CHLORO-5-NITROPYRIMIDIN-4-YL)AMINO]BENZENESULFONAMIDE
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
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS DRUG DESIGN, CARBONIC ANHYDRASE, SULFONAMIDE, METAL-BINDING, LYASE-
KEYWDS 2 LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GRAZULIS,E.MANAKOVA,D.GOLOVENKO
REVDAT 5 01-NOV-23 3M40 1 REMARK
REVDAT 4 04-OCT-17 3M40 1 REMARK
REVDAT 3 17-NOV-10 3M40 1 HEADER KEYWDS
REVDAT 2 27-OCT-10 3M40 1 JRNL
REVDAT 1 20-OCT-10 3M40 0
JRNL AUTH J.SUDZIUS,L.BARANAUSKIENE,D.GOLOVENKO,J.MATULIENE,
JRNL AUTH 2 V.MICHAILOVIENE,J.TORRESAN,J.JACHNO,R.SUKACKAITE,E.MANAKOVA,
JRNL AUTH 3 S.GRAZULIS,S.TUMKEVICIUS,D.MATULIS
JRNL TITL 4-[N-(SUBSTITUTED 4-PYRIMIDINYL)AMINO]BENZENESULFONAMIDES AS
JRNL TITL 2 INHIBITORS OF CARBONIC ANHYDRASE ISOZYMES I, II, VII, AND
JRNL TITL 3 XIII
JRNL REF BIOORG.MED.CHEM. V. 18 7413 2010
JRNL REFN ISSN 0968-0896
JRNL PMID 20889345
JRNL DOI 10.1016/J.BMC.2010.09.011
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 30126
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3047
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1738
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.1470
REMARK 3 BIN FREE R VALUE SET COUNT : 206
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2059
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.48000
REMARK 3 B33 (A**2) : 0.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.471
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2248 ; 0.026 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3069 ; 1.947 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 279 ; 6.745 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;32.695 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 369 ;13.955 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;21.894 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1775 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1092 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1502 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 191 ; 0.148 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.041 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 71 ; 0.221 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.163 ; 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): 1402 ; 2.366 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2203 ; 3.265 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1014 ; 4.919 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 866 ; 6.057 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2416 ; 3.027 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 230 ;14.807 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2176 ; 8.866 ; 3.000
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 : 1.40
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 3M40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
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 : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8150
REMARK 200 MONOCHROMATOR : SI (111), HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : BENT, VERTICALLY FOCUSSING
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR555 FLAT PANEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.19
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30141
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 16.295
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : 0.16100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.20200
REMARK 200 R SYM FOR SHELL (I) : 0.20200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2NNO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA-BICINE PH 9.0, 2M NA-MALONATE
REMARK 280 PH7.55, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 8
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 20.58250
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 HOH A 472 O HOH A 496 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 14 CD GLU A 14 OE2 0.074
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 LEU A 47 CA - CB - CG ANGL. DEV. = 14.6 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 LYS A 76 -90.26 -115.30
REMARK 500 LYS A 76 -90.26 -85.67
REMARK 500 LYS A 111 -4.23 77.71
REMARK 500 PHE A 176 75.61 -155.76
REMARK 500 PHE A 176 75.61 -151.19
REMARK 500 ASN A 244 49.41 -95.15
REMARK 500 LYS A 252 -136.21 54.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 METAL ION NATURALLY OCCURS IN CARBONIC ANHYDRASES.
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 J45 A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 264
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3M2N RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 900 RELATED ID: 3M3X RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 900 RELATED ID: 3M5E RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 900 RELATED ID: 3MHI RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 900 RELATED ID: 3MHL RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 900 RELATED ID: 3MHM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 900 RELATED ID: 3MHO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH OTHER LIGAND
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 126 IS SKIPPED IN THE NUMBERING.
DBREF 3M40 A 1 261 UNP P00918 CAH2_HUMAN 1 260
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 ALA
SEQRES 6 A 260 PHE ASN 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 J45 A 263 21
HET DMS A 264 4
HETNAM ZN ZINC ION
HETNAM J45 4-[(6-CHLORO-5-NITROPYRIMIDIN-4-YL)
HETNAM 2 J45 AMINO]BENZENESULFONAMIDE
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 J45 C10 H8 CL N5 O4 S
FORMUL 4 DMS C2 H6 O S
FORMUL 5 HOH *229(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 ILE A 167 5 3
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 PHE A 70 O ILE A 91
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
CISPEP 1 SER A 29 PRO A 30 0 2.26
CISPEP 2 PRO A 201 PRO A 202 0 6.33
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 J45 A 263
SITE 1 AC2 11 GLN A 92 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC2 11 PHE A 131 LEU A 198 THR A 199 THR A 200
SITE 3 AC2 11 TRP A 209 ZN A 262 HOH A 293
SITE 1 AC3 5 TYR A 7 ASP A 243 TRP A 245 PRO A 247
SITE 2 AC3 5 HOH A 489
CRYST1 42.184 41.165 72.477 90.00 104.54 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 0.023706 0.000000 0.006148 0.00000
SCALE2 0.000000 0.024292 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
