HEADER LYASE 07-NOV-08 3F7B
TITLE CRYSTAL STRUCTURE OF SOLUBLE DOMAIN OF CA4 IN COMPLEX WITH SMALL
TITLE 2 MOLECULE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN;
COMPND 5 SYNONYM: CARBONIC ANHYDRASE IV, CA-IV, CARBONATE DEHYDRATASE IV;
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 GENE: CA4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS STRUCTURE-BASED DRUG DESIGN. SMALL MOLECULE COMPLEX. CO-CRYSTAL.,
KEYWDS 2 CELL MEMBRANE, DISEASE MUTATION, GLYCOPROTEIN, GPI-ANCHOR,
KEYWDS 3 LIPOPROTEIN, LYASE, MEMBRANE, METAL-BINDING, RETINITIS PIGMENTOSA,
KEYWDS 4 SENSORY TRANSDUCTION, VISION, ZINC
EXPDTA X-RAY DIFFRACTION
AUTHOR S.E.GREASLEY,R.A.A.FERRE,T.A.PAULY,R.PAZ
REVDAT 3 06-SEP-23 3F7B 1 REMARK LINK
REVDAT 2 12-MAY-10 3F7B 1 JRNL
REVDAT 1 22-SEP-09 3F7B 0
JRNL AUTH W.VERNIER,W.CHONG,D.REWOLINSKI,S.GREASLEY,T.PAULY,M.SHAW,
JRNL AUTH 2 D.DINH,R.A.FERRE,S.NUKUI,M.ORNELAS,E.REYNER
JRNL TITL THIOETHER BENZENESULFONAMIDE INHIBITORS OF CARBONIC
JRNL TITL 2 ANHYDRASES II AND IV: STRUCTURE-BASED DRUG DESIGN,
JRNL TITL 3 SYNTHESIS, AND BIOLOGICAL EVALUATION.
JRNL REF BIOORG.MED.CHEM. V. 18 3307 2010
JRNL REFN ISSN 0968-0896
JRNL PMID 20363633
JRNL DOI 10.1016/J.BMC.2010.03.014
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0073
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 39564
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2094
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3045
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4002
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 263
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : -0.61000
REMARK 3 B33 (A**2) : 0.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.69000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.915
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4156 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5620 ; 2.072 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 493 ; 7.287 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;36.501 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 719 ;17.280 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;11.268 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 608 ; 0.171 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3109 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2510 ; 1.371 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4050 ; 2.372 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1646 ; 3.673 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1570 ; 5.741 ; 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): 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 : 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: NULL
REMARK 4
REMARK 4 3F7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 4.5
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) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41673
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 19.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : 2.560
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1ZNC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M NA ACETATE, 0.32M
REMARK 280 AMMONIUM SULFATE , PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 62.95500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.27800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 62.95500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 64.27800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 491 LIES ON A SPECIAL POSITION.
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 ALA A 1
REMARK 465 ARG A 129
REMARK 465 ASN A 130
REMARK 465 VAL A 131
REMARK 465 LYS A 132
REMARK 465 GLU A 133
REMARK 465 ALA A 134
REMARK 465 GLN A 135
REMARK 465 ASP A 136
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 465 SER B 3
REMARK 465 HIS B 4
REMARK 465 SER B 11C
REMARK 465 ASN B 11D
REMARK 465 TYR B 11E
REMARK 465 LYS B 125A
REMARK 465 GLY B 125B
REMARK 465 THR B 125C
REMARK 465 SER B 125D
REMARK 465 ARG B 125E
REMARK 465 ASN B 125F
REMARK 465 VAL B 125G
REMARK 465 LYS B 125H
REMARK 465 GLU B 125I
REMARK 465 ALA B 125J
REMARK 465 GLN B 125K
REMARK 465 ASP B 125L
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 ASN A 11D CG OD1 ND2
REMARK 470 TYR A 11E CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 42 CE NZ
REMARK 470 LYS A 43 CD CE NZ
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 SER A 128 OG
REMARK 470 LYS A 187 CD CE NZ
REMARK 470 GLU A 187B CD OE1 OE2
REMARK 470 ARG A 189A CD NE CZ NH1 NH2
REMARK 470 GLU A 221 CD OE1 OE2
REMARK 470 LYS B 42 CE NZ
REMARK 470 LYS B 43 CE NZ
REMARK 470 LYS B 53 CD CE NZ
REMARK 470 GLU B 138 CD OE1 OE2
REMARK 470 LYS B 187 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 OD2 ASP B 110 O HOH B 439 2.19
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 TRP A 16 C GLY A 20 N 0.195
REMARK 500 ASN A 72 C LYS A 76 N 0.196
REMARK 500 GLU A 171 CG GLU A 171 CD 0.091
REMARK 500 TYR A 191 CE2 TYR A 191 CD2 0.092
REMARK 500 LYS A 233 C GLU A 236 N 0.139
REMARK 500 TRP B 16 C GLY B 20 N 0.159
REMARK 500 ASN B 72 C LYS B 76 N 0.192
REMARK 500 LYS B 233 C GLU B 236 N 0.143
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 TRP A 16 CA - C - N ANGL. DEV. = 21.1 DEGREES
REMARK 500 TRP A 16 O - C - N ANGL. DEV. = -20.8 DEGREES
REMARK 500 GLY A 20 C - N - CA ANGL. DEV. = 22.5 DEGREES
REMARK 500 LEU A 218 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 LYS A 233 CA - C - N ANGL. DEV. = 24.9 DEGREES
REMARK 500 LYS A 233 O - C - N ANGL. DEV. = -26.8 DEGREES
REMARK 500 GLU A 236 C - N - CA ANGL. DEV. = 23.7 DEGREES
REMARK 500 GLY B 20 C - N - CA ANGL. DEV. = -20.7 DEGREES
REMARK 500 LYS B 233 O - C - N ANGL. DEV. = -12.9 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 SER A 98 -163.78 -124.36
REMARK 500 LYS B 25 -164.79 -78.22
REMARK 500 ARG B 27 50.71 -119.33
REMARK 500 SER B 65 -178.13 -171.74
REMARK 500 GLU B 171 -14.33 81.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 137 GLU A 138 -146.16
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 111.7
REMARK 620 3 HIS A 119 ND1 116.1 99.3
REMARK 620 4 AG5 A 302 N9 101.7 112.7 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 94 NE2
REMARK 620 2 HIS B 96 NE2 103.0
REMARK 620 3 HIS B 119 ND1 111.9 98.5
REMARK 620 4 AG5 B 303 N9 109.5 110.7 121.2
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 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AG5 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AG5 B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F7U RELATED DB: PDB
REMARK 900 SMALL MOLECULE FROM SAME CHEMICAL SERIES.
REMARK 900 RELATED ID: 3FW3 RELATED DB: PDB
DBREF 3F7B A 1 259 UNP P22748 CAH4_HUMAN 19 284
DBREF 3F7B B 1 259 UNP P22748 CAH4_HUMAN 19 284
SEQRES 1 A 266 ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER
SEQRES 2 A 266 SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY
SEQRES 3 A 266 ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL
SEQRES 4 A 266 THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE
SEQRES 5 A 266 PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL
SEQRES 6 A 266 GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN
SEQRES 7 A 266 LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR
SEQRES 8 A 266 GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO
SEQRES 9 A 266 TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE
SEQRES 10 A 266 ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY
SEQRES 11 A 266 THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP
SEQRES 12 A 266 GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR
SEQRES 13 A 266 GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU
SEQRES 14 A 266 SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA
SEQRES 15 A 266 GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS
SEQRES 16 A 266 LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR
SEQRES 17 A 266 PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG
SEQRES 18 A 266 GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE
SEQRES 19 A 266 SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER
SEQRES 20 A 266 MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN
SEQRES 21 A 266 ARG THR VAL ILE LYS SER
SEQRES 1 B 266 ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER
SEQRES 2 B 266 SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY
SEQRES 3 B 266 ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL
SEQRES 4 B 266 THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE
SEQRES 5 B 266 PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL
SEQRES 6 B 266 GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN
SEQRES 7 B 266 LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR
SEQRES 8 B 266 GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO
SEQRES 9 B 266 TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE
SEQRES 10 B 266 ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY
SEQRES 11 B 266 THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP
SEQRES 12 B 266 GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR
SEQRES 13 B 266 GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU
SEQRES 14 B 266 SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA
SEQRES 15 B 266 GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS
SEQRES 16 B 266 LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR
SEQRES 17 B 266 PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG
SEQRES 18 B 266 GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE
SEQRES 19 B 266 SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER
SEQRES 20 B 266 MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN
SEQRES 21 B 266 ARG THR VAL ILE LYS SER
HET ZN A 300 1
HET AG5 A 302 28
HET ZN B 301 1
HET AG5 B 303 28
HETNAM ZN ZINC ION
HETNAM AG5 N-(2-PHENYLETHYL)-2-(PHENYLSULFANYL)-5-
HETNAM 2 AG5 SULFAMOYLPYRIDINE-3-CARBOXAMIDE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 AG5 2(C20 H19 N3 O3 S2)
FORMUL 7 HOH *263(H2 O)
HELIX 1 1 TYR A 7 SER A 11B 1 7
HELIX 2 2 VAL A 12 TRP A 16 5 5
HELIX 3 3 VAL A 34 ALA A 38 5 5
HELIX 4 4 ASN A 154 GLY A 156 5 3
HELIX 5 5 PHE A 157 SER A 165 1 9
HELIX 6 6 LEU A 181 LEU A 185 5 5
HELIX 7 7 LYS A 187 ARG A 189A 5 6
HELIX 8 8 ARG A 220 LEU A 229 1 11
HELIX 9 9 TYR B 7 SER B 11B 1 7
HELIX 10 10 VAL B 12 TRP B 16 5 5
HELIX 11 11 VAL B 34 ALA B 38 5 5
HELIX 12 12 ASN B 154 GLY B 156 5 3
HELIX 13 13 PHE B 157 LEU B 164 1 8
HELIX 14 14 SER B 165 ILE B 167 5 3
HELIX 15 15 SER B 180 LEU B 184 5 5
HELIX 16 16 LYS B 187 ARG B 189A 5 6
HELIX 17 17 ARG B 220 LEU B 229 1 11
SHEET 1 A 2 HIS A 4 TRP A 5 0
SHEET 2 A 2 CYS A 11G LEU A 11H 1 O LEU A 11H N HIS A 4
SHEET 1 B 2 ASN A 32 ILE A 33 0
SHEET 2 B 2 SER A 108 LEU A 109 1 O SER A 108 N ILE A 33
SHEET 1 C10 LYS A 39 VAL A 40 0
SHEET 2 C10 ILE A 257 LYS A 258 1 O LYS A 258 N LYS A 39
SHEET 3 C10 TYR A 191 GLY A 196 -1 N ARG A 193 O ILE A 257
SHEET 4 C10 VAL A 207 PHE A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 C10 ILE A 141 GLY A 151 1 N ILE A 141 O VAL A 208
SHEET 6 C10 MET A 116 LYS A 124 -1 N MET A 118 O PHE A 146
SHEET 7 C10 TYR A 88 TRP A 97 -1 N LYS A 91 O VAL A 121
SHEET 8 C10 VAL A 66 LEU A 69 -1 N MET A 68 O LEU A 93
SHEET 9 C10 THR A 58 ASN A 61 -1 N GLN A 60 O MET A 67
SHEET 10 C10 SER A 173 THR A 175 -1 O THR A 174 N VAL A 59
SHEET 1 D 6 PHE A 47 SER A 50 0
SHEET 2 D 6 SER A 78 GLY A 81 -1 O SER A 80 N PHE A 48
SHEET 3 D 6 TYR A 88 TRP A 97 -1 O TYR A 88 N ILE A 79
SHEET 4 D 6 MET A 116 LYS A 124 -1 O VAL A 121 N LYS A 91
SHEET 5 D 6 ILE A 141 GLY A 151 -1 O PHE A 146 N MET A 118
SHEET 6 D 6 ILE A 216 HIS A 219 1 O ILE A 216 N LEU A 147
SHEET 1 E 2 ASN B 32 ILE B 33 0
SHEET 2 E 2 SER B 108 LEU B 109 1 O SER B 108 N ILE B 33
SHEET 1 F10 LYS B 39 VAL B 40 0
SHEET 2 F10 ILE B 257 LYS B 258 1 O LYS B 258 N LYS B 39
SHEET 3 F10 TYR B 191 GLY B 196 -1 N ARG B 193 O ILE B 257
SHEET 4 F10 VAL B 207 PHE B 212 -1 O VAL B 207 N GLY B 196
SHEET 5 F10 ILE B 141 GLY B 151 1 N ALA B 145 O THR B 210
SHEET 6 F10 MET B 116 LYS B 124 -1 N MET B 118 O PHE B 146
SHEET 7 F10 TYR B 88 TRP B 97 -1 N LYS B 91 O VAL B 121
SHEET 8 F10 VAL B 66 LEU B 69 -1 N MET B 68 O LEU B 93
SHEET 9 F10 THR B 58 ASN B 61 -1 N GLN B 60 O MET B 67
SHEET 10 F10 SER B 173 THR B 175 -1 O THR B 174 N VAL B 59
SHEET 1 G 6 PHE B 47 SER B 50 0
SHEET 2 G 6 SER B 78 GLY B 81 -1 O SER B 80 N PHE B 48
SHEET 3 G 6 TYR B 88 TRP B 97 -1 O TYR B 88 N ILE B 79
SHEET 4 G 6 MET B 116 LYS B 124 -1 O VAL B 121 N LYS B 91
SHEET 5 G 6 ILE B 141 GLY B 151 -1 O PHE B 146 N MET B 118
SHEET 6 G 6 ILE B 216 HIS B 219 1 O ILE B 216 N LEU B 147
SSBOND 1 CYS A 6 CYS A 11G 1555 1555 2.07
SSBOND 2 CYS A 23 CYS A 203 1555 1555 2.08
SSBOND 3 CYS B 6 CYS B 11G 1555 1555 2.09
SSBOND 4 CYS B 23 CYS B 203 1555 1555 2.06
LINK NE2 HIS A 94 ZN ZN A 300 1555 1555 2.03
LINK NE2 HIS A 96 ZN ZN A 300 1555 1555 2.08
LINK ND1 HIS A 119 ZN ZN A 300 1555 1555 2.09
LINK ZN ZN A 300 N9 AG5 A 302 1555 1555 2.03
LINK NE2 HIS B 94 ZN ZN B 301 1555 1555 2.12
LINK NE2 HIS B 96 ZN ZN B 301 1555 1555 2.18
LINK ND1 HIS B 119 ZN ZN B 301 1555 1555 1.97
LINK ZN ZN B 301 N9 AG5 B 303 1555 1555 1.97
CISPEP 1 SER A 29 PRO A 30 0 2.94
CISPEP 2 PRO A 201 THR A 202 0 9.32
CISPEP 3 SER B 29 PRO B 30 0 0.70
CISPEP 4 PRO B 201 THR B 202 0 5.85
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 AG5 A 302
SITE 1 AC2 16 TYR A 7 ASN A 62 HIS A 64 SER A 65
SITE 2 AC2 16 MET A 67 GLN A 92 HIS A 94 HIS A 96
SITE 3 AC2 16 HIS A 119 VAL A 121 ILE A 141 LEU A 198
SITE 4 AC2 16 THR A 199 THR A 200 ZN A 300 HOH A 564
SITE 1 AC3 4 HIS B 94 HIS B 96 HIS B 119 AG5 B 303
SITE 1 AC4 17 SER A 128 HOH A 470 TYR B 7 ASN B 62
SITE 2 AC4 17 HIS B 64 SER B 65 GLN B 92 HIS B 94
SITE 3 AC4 17 HIS B 96 HIS B 119 VAL B 121 ILE B 141
SITE 4 AC4 17 LEU B 198 THR B 199 THR B 200 TRP B 209
SITE 5 AC4 17 ZN B 301
CRYST1 125.910 128.556 46.365 90.00 99.88 90.00 C 1 2 1 8
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 0.007942 0.000000 0.001384 0.00000
SCALE2 0.000000 0.007779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021893 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
