HEADER LYASE 11-MAY-11 3RYV
TITLE CARBONIC ANHYDRASE COMPLEXED WITH N-ETHYL-4-SULFAMOYLBENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: B;
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 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: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA BETA, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.W.SNYDER,S.BAI,A.HEROUX,G.W.WHITESIDES
REVDAT 3 28-FEB-24 3RYV 1 REMARK SEQADV LINK
REVDAT 2 16-NOV-11 3RYV 1 JRNL
REVDAT 1 10-AUG-11 3RYV 0
JRNL AUTH J.MECINOVIC,P.W.SNYDER,K.A.MIRICA,S.BAI,E.T.MACK,R.L.KWANT,
JRNL AUTH 2 D.T.MOUSTAKAS,A.HEROUX,G.M.WHITESIDES
JRNL TITL FLUOROALKYL AND ALKYL CHAINS HAVE SIMILAR HYDROPHOBICITIES
JRNL TITL 2 IN BINDING TO THE "HYDROPHOBIC WALL" OF CARBONIC ANHYDRASE.
JRNL REF J.AM.CHEM.SOC. V. 133 14017 2011
JRNL REFN ISSN 0002-7863
JRNL PMID 21790183
JRNL DOI 10.1021/JA2045293
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 76025
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) : 0.134
REMARK 3 R VALUE (WORKING SET) : 0.133
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3819
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5133
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 267
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.970
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2201 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3013 ; 2.274 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 283 ; 6.559 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 105 ;35.311 ;24.762
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 362 ;11.572 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;23.806 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.197 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1727 ; 0.014 ; 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): 1323 ; 2.592 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2149 ; 3.605 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 878 ; 4.822 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 851 ; 6.491 ; 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): 2201 ; 2.838 ; 3.000
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: U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3RYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76025
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 41.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-CL, 1.15 M SODIUM CITRATE,
REMARK 280 PH 7.8, VAPOR DIFFUSION, TEMPERATURE 277K
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 20.72000
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: 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 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 B 2
REMARK 465 HIS B 3
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 B 4 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 261 CG 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 NH2 ARG B 27 O HOH B 582 1.62
REMARK 500 O HOH B 488 O HOH B 581 1.69
REMARK 500 CA HIS B 4 O HOH B 565 1.79
REMARK 500 NZ LYS B 213 O HOH B 429 1.92
REMARK 500 NH2 ARG B 27 O HOH B 502 1.96
REMARK 500 OE2 GLU B 214 O HOH B 449 1.97
REMARK 500 CZ ARG B 27 O HOH B 582 2.10
REMARK 500 NH1 ARG B 27 O HOH B 582 2.12
REMARK 500 OD1 ASP B 34 O HOH B 353 2.16
REMARK 500 OD2 ASP B 165 O HOH B 441 2.16
REMARK 500 CD PRO B 46 O HOH B 588 2.17
REMARK 500 OD1 ASP B 165 O HOH B 569 2.17
REMARK 500 O HOH B 558 O HOH B 571 2.18
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 OE2 GLU B 14 O HOH B 473 1655 1.22
REMARK 500 CD GLU B 14 O HOH B 473 1655 1.96
REMARK 500 O HOH B 560 O HOH B 582 2646 2.03
REMARK 500 O HOH B 559 O HOH B 574 1655 2.10
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 B 14 CD GLU B 14 OE1 -0.074
REMARK 500 GLU B 14 CD GLU B 14 OE2 0.073
REMARK 500 VAL B 161 CB VAL B 161 CG2 -0.261
REMARK 500 GLU B 214 CD GLU B 214 OE1 -0.106
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 B 47 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG B 89 CG - CD - NE ANGL. DEV. = -20.3 DEGREES
REMARK 500 ARG B 89 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP B 130 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 LEU B 141 CB - CG - CD2 ANGL. DEV. = 16.0 DEGREES
REMARK 500 VAL B 161 CG1 - CB - CG2 ANGL. DEV. = -16.3 DEGREES
REMARK 500 ASP B 162 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 PHE B 226 CB - CG - CD1 ANGL. DEV. = 5.2 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 ARG B 27 56.29 -142.35
REMARK 500 LYS B 76 -75.27 -77.34
REMARK 500 GLU B 106 -60.55 -94.85
REMARK 500 LYS B 111 -2.53 72.62
REMARK 500 PHE B 176 69.54 -154.74
REMARK 500 ASN B 244 44.42 -89.85
REMARK 500 LYS B 252 -139.19 55.39
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 B 262 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 RYV B 1 N3S
REMARK 620 2 HIS B 94 NE2 110.1
REMARK 620 3 HIS B 96 NE2 111.0 104.5
REMARK 620 4 HIS B 119 ND1 115.5 114.6 100.0
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 B 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RYV B 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RYJ RELATED DB: PDB
REMARK 900 RELATED ID: 3RYX RELATED DB: PDB
REMARK 900 RELATED ID: 3RYY RELATED DB: PDB
REMARK 900 RELATED ID: 3RYZ RELATED DB: PDB
REMARK 900 RELATED ID: 3RZ0 RELATED DB: PDB
REMARK 900 RELATED ID: 3RZ1 RELATED DB: PDB
REMARK 900 RELATED ID: 3RZ5 RELATED DB: PDB
REMARK 900 RELATED ID: 3RZ7 RELATED DB: PDB
REMARK 900 RELATED ID: 3RZ8 RELATED DB: PDB
DBREF 3RYV B 2 261 UNP P00918 CAH2_HUMAN 2 260
SEQADV 3RYV GLY B 9 UNP P00918 LYS 9 CONFLICT
SEQRES 1 B 259 SER HIS HIS TRP GLY TYR GLY GLY HIS ASN GLY PRO GLU
SEQRES 2 B 259 HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES 3 B 259 GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES 4 B 259 ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES 5 B 259 ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES 6 B 259 ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES 7 B 259 LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES 8 B 259 PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES 9 B 259 GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES 10 B 259 HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES 11 B 259 LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES 12 B 259 ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES 13 B 259 LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES 14 B 259 LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES 15 B 259 LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES 16 B 259 LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES 17 B 259 VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES 18 B 259 LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES 19 B 259 PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES 20 B 259 PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN B 262 1
HET RYV B 1 15
HETNAM ZN ZINC ION
HETNAM RYV N-ETHYL-4-SULFAMOYLBENZAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 RYV C9 H12 N2 O3 S
FORMUL 4 HOH *326(H2 O)
HELIX 1 1 GLY B 12 ASP B 19 5 8
HELIX 2 2 PHE B 20 GLY B 25 5 6
HELIX 3 3 LYS B 127 GLY B 129 5 3
HELIX 4 4 ASP B 130 VAL B 135 1 6
HELIX 5 5 LYS B 154 GLY B 156 5 3
HELIX 6 6 LEU B 157 LEU B 164 1 8
HELIX 7 7 ASP B 165 LYS B 168 5 4
HELIX 8 8 ASP B 180 LEU B 185 5 6
HELIX 9 9 SER B 219 ARG B 227 1 9
SHEET 1 A 2 ASP B 32 ILE B 33 0
SHEET 2 A 2 THR B 108 VAL B 109 1 O THR B 108 N ILE B 33
SHEET 1 B10 LYS B 39 TYR B 40 0
SHEET 2 B10 LYS B 257 ALA B 258 1 O ALA B 258 N LYS B 39
SHEET 3 B10 TYR B 191 GLY B 196 -1 N THR B 193 O LYS B 257
SHEET 4 B10 VAL B 207 LEU B 212 -1 O VAL B 207 N GLY B 196
SHEET 5 B10 LEU B 141 VAL B 150 1 N GLY B 145 O ILE B 210
SHEET 6 B10 ALA B 116 ASN B 124 -1 N LEU B 118 O ILE B 146
SHEET 7 B10 TYR B 88 TRP B 97 -1 N HIS B 94 O HIS B 119
SHEET 8 B10 PHE B 66 PHE B 70 -1 N VAL B 68 O PHE B 93
SHEET 9 B10 SER B 56 ASN B 61 -1 N LEU B 57 O GLU B 69
SHEET 10 B10 SER B 173 ASP B 175 -1 O ALA B 174 N ILE B 59
SHEET 1 C 6 LEU B 47 SER B 50 0
SHEET 2 C 6 VAL B 78 GLY B 81 -1 O LYS B 80 N SER B 48
SHEET 3 C 6 TYR B 88 TRP B 97 -1 O TYR B 88 N LEU B 79
SHEET 4 C 6 ALA B 116 ASN B 124 -1 O HIS B 119 N HIS B 94
SHEET 5 C 6 LEU B 141 VAL B 150 -1 O ILE B 146 N LEU B 118
SHEET 6 C 6 ILE B 216 VAL B 218 1 O ILE B 216 N PHE B 147
LINK N3S RYV B 1 ZN ZN B 262 1555 1555 1.98
LINK NE2 HIS B 94 ZN ZN B 262 1555 1555 2.00
LINK NE2 HIS B 96 ZN ZN B 262 1555 1555 2.04
LINK ND1 HIS B 119 ZN ZN B 262 1555 1555 2.02
CISPEP 1 SER B 29 PRO B 30 0 -2.78
CISPEP 2 PRO B 201 PRO B 202 0 15.13
SITE 1 AC1 4 RYV B 1 HIS B 94 HIS B 96 HIS B 119
SITE 1 AC2 12 HIS B 94 HIS B 96 HIS B 119 PHE B 131
SITE 2 AC2 12 LEU B 198 THR B 199 THR B 200 TRP B 209
SITE 3 AC2 12 ZN B 262 HOH B 264 HOH B 281 HOH B 354
CRYST1 42.390 41.440 72.060 90.00 104.70 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 0.023590 0.000000 0.006189 0.00000
SCALE2 0.000000 0.024131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014347 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
