HEADER LYASE 21-OCT-15 5FL4
TITLE THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN COMPLEX
TITLE 2 WITH 5-(1-NAPHTHALEN-1-YL-1,2,3-TRIAZOL-4-YL)THIOPHENE-2-SULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 9;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 137-391;
COMPND 5 SYNONYM: CARBONATE DEHYDRATASE IX, CARBONIC ANHYDRASE IX, CA-IX,
COMPND 6 CAIX, MEMBRANE ANTIGEN MN, P54/58N, RENAL CELL CARCINOMA-ASSOCIATED
COMPND 7 ANTIGEN G250, RCC-ASSOCIATED ANTIGEN G250, PMW1;
COMPND 8 EC: 4.2.1.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: 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: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LEITANS,K.TARS,R.ZALUBOVSKIS
REVDAT 5 06-FEB-19 5FL4 1 REMARK
REVDAT 4 30-JAN-19 5FL4 1 REMARK
REVDAT 3 17-JAN-18 5FL4 1 REMARK
REVDAT 2 09-DEC-15 5FL4 1 JRNL
REVDAT 1 11-NOV-15 5FL4 0
JRNL AUTH J.LEITANS,A.KAZAKS,A.BALODE,J.IVANOVA,R.ZALUBOVSKIS,
JRNL AUTH 2 C.T.SUPURAN,K.TARS
JRNL TITL AN EFFICIENT EXPRESSION AND CRYSTALLIZATION SYSTEM OF THE
JRNL TITL 2 CANCER ASOCIATED CARBONIC ANHYDRASE ISOFORM IX.
JRNL REF J.MED.CHEM. V. 58 9004 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26522624
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01343
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 126519
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 6944
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9382
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 496
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7738
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 1050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.55000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -1.77000
REMARK 3 B12 (A**2) : 0.27000
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): 0.111
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.349
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8156 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7566 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11146 ; 1.725 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17386 ; 0.911 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1012 ; 5.838 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 364 ;36.842 ;22.967
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1170 ;12.359 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 70 ;17.197 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1186 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9298 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1932 ; 0.002 ; 0.020
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): 4030 ; 1.762 ; 3.005
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4023 ; 1.758 ; 3.001
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5026 ; 2.744 ; 4.495
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4126 ; 2.162 ; 3.262
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5FL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1290065346.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91922
REMARK 200 MONOCHROMATOR : SI CRYSTAL
REMARK 200 OPTICS : MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133470
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 61.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 3IAI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M DI-AMMONIUM HYDROGEN PHOSPHATE,
REMARK 280 0.1 M SODIUM ACETATE PH 4.5, PROTEIN 10 MG/ML 5-10 MM INHIBITOR
REMARK 280 (STOCK SOLUTION WAS 100 MM INHIBITOR DISSOLVED IN 100% DIMETHYL
REMARK 280 SULFOXIDE) VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.14500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.96234
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.37667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 76.14500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 43.96234
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.37667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 76.14500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 43.96234
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.37667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 87.92467
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 114.75333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 87.92467
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 114.75333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 87.92467
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 114.75333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
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: C
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: 4
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: D
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 3
REMARK 465 PRO A 4
REMARK 465 ASP A 5
REMARK 465 GLN A 6
REMARK 465 SER A 7
REMARK 465 HIS A 8
REMARK 465 GLY B 3
REMARK 465 PRO B 4
REMARK 465 ASP B 5
REMARK 465 GLN B 6
REMARK 465 SER B 7
REMARK 465 HIS B 8
REMARK 465 GLY C 3
REMARK 465 PRO C 4
REMARK 465 ASP C 5
REMARK 465 GLN C 6
REMARK 465 SER C 7
REMARK 465 HIS C 8
REMARK 465 GLY D 3
REMARK 465 PRO D 4
REMARK 465 ASP D 5
REMARK 465 GLN D 6
REMARK 465 SER D 7
REMARK 465 HIS D 8
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 GLU A 165 CG CD OE1 OE2
REMARK 470 ASP A 236 CG OD1 OD2
REMARK 470 ARG B 10 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 LYS B 222 CG CD CE NZ
REMARK 470 ASP B 236 CG OD1 OD2
REMARK 470 GLN C 37 CG CD OE1 NE2
REMARK 470 GLU C 152 CG CD OE1 OE2
REMARK 470 ASP C 236 CG OD1 OD2
REMARK 470 ARG D 10 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 19 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 169 CG CD OE1 OE2
REMARK 470 ASP D 236 CG OD1 OD2
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 B 2206 O HOH B 2207 1.41
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 O HOH B 2061 O HOH B 2061 3555 0.75
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 ALA B 100 92.86 -35.71
REMARK 500 GLU B 110 42.42 39.23
REMARK 500 ALA D 100 110.11 -39.32
REMARK 500 GLU D 110 41.37 38.40
REMARK 500 ASP D 236 57.99 -102.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2123 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A2138 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH C2017 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH D2013 DISTANCE = 5.91 ANGSTROMS
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 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 103.3
REMARK 620 3 HIS A 119 ND1 110.8 99.2
REMARK 620 4 9FK A 269 N24 112.2 113.0 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 94 NE2
REMARK 620 2 9FK B 268 N24 108.7
REMARK 620 3 HIS B 96 NE2 103.3 106.2
REMARK 620 4 HIS B 119 ND1 117.0 117.6 102.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 94 NE2
REMARK 620 2 HIS C 96 NE2 108.6
REMARK 620 3 HIS C 119 ND1 108.9 101.3
REMARK 620 4 9FK C 267 N24 106.6 111.4 119.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 264 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 96 NE2
REMARK 620 2 9FK D 266 N24 104.7
REMARK 620 3 9FK D 266 S21 135.8 31.1
REMARK 620 4 HIS D 119 ND1 101.1 120.2 104.1
REMARK 620 5 HIS D 94 NE2 108.8 107.5 93.7 113.5
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 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9FK A 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9FK B 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9FK C 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9FK D 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 1260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 1260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 1261
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1261
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 1262
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FL5 RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN
REMARK 900 COMPLEX WITH 5-(1-(4-METHOXYPHENYL)-1H-1,2, 3-TRIAZOL-4-YL)
REMARK 900 THIOPHENE-2-SULFONAMIDE
REMARK 900 RELATED ID: 5FL6 RELATED DB: PDB
REMARK 900 THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN
REMARK 900 COMPLEX WITH 5-(1-(4-METHYLPHENYL)-1H-1,2, 3-TRIAZOL-4-YL)THIOPHENE-
REMARK 900 2-SULFONAMIDE
DBREF 5FL4 A 5 259 UNP Q16790 CAH9_HUMAN 137 391
DBREF 5FL4 B 5 259 UNP Q16790 CAH9_HUMAN 137 391
DBREF 5FL4 C 5 259 UNP Q16790 CAH9_HUMAN 137 391
DBREF 5FL4 D 5 259 UNP Q16790 CAH9_HUMAN 137 391
SEQADV 5FL4 GLY A 3 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 PRO A 4 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 SER A 42 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 5FL4 GLY B 3 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 PRO B 4 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 SER B 42 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 5FL4 GLY C 3 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 PRO C 4 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 SER C 42 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 5FL4 GLY D 3 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 PRO D 4 UNP Q16790 EXPRESSION TAG
SEQADV 5FL4 SER D 42 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQRES 1 A 257 GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO
SEQRES 2 A 257 PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE
SEQRES 3 A 257 GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE
SEQRES 4 A 257 SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN
SEQRES 5 A 257 LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY
SEQRES 6 A 257 HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET
SEQRES 7 A 257 ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU
SEQRES 8 A 257 HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU
SEQRES 9 A 257 HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS
SEQRES 10 A 257 VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU
SEQRES 11 A 257 ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA
SEQRES 12 A 257 PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU
SEQRES 13 A 257 GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY
SEQRES 14 A 257 SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU
SEQRES 15 A 257 LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY
SEQRES 16 A 257 SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP
SEQRES 17 A 257 THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN
SEQRES 18 A 257 LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP
SEQRES 19 A 257 SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU
SEQRES 20 A 257 ASN GLY ARG VAL ILE GLU ALA SER PHE PRO
SEQRES 1 B 257 GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO
SEQRES 2 B 257 PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE
SEQRES 3 B 257 GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE
SEQRES 4 B 257 SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN
SEQRES 5 B 257 LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY
SEQRES 6 B 257 HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET
SEQRES 7 B 257 ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU
SEQRES 8 B 257 HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU
SEQRES 9 B 257 HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS
SEQRES 10 B 257 VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU
SEQRES 11 B 257 ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA
SEQRES 12 B 257 PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU
SEQRES 13 B 257 GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY
SEQRES 14 B 257 SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU
SEQRES 15 B 257 LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY
SEQRES 16 B 257 SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP
SEQRES 17 B 257 THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN
SEQRES 18 B 257 LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP
SEQRES 19 B 257 SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU
SEQRES 20 B 257 ASN GLY ARG VAL ILE GLU ALA SER PHE PRO
SEQRES 1 C 257 GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO
SEQRES 2 C 257 PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE
SEQRES 3 C 257 GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE
SEQRES 4 C 257 SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN
SEQRES 5 C 257 LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY
SEQRES 6 C 257 HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET
SEQRES 7 C 257 ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU
SEQRES 8 C 257 HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU
SEQRES 9 C 257 HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS
SEQRES 10 C 257 VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU
SEQRES 11 C 257 ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA
SEQRES 12 C 257 PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU
SEQRES 13 C 257 GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY
SEQRES 14 C 257 SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU
SEQRES 15 C 257 LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY
SEQRES 16 C 257 SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP
SEQRES 17 C 257 THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN
SEQRES 18 C 257 LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP
SEQRES 19 C 257 SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU
SEQRES 20 C 257 ASN GLY ARG VAL ILE GLU ALA SER PHE PRO
SEQRES 1 D 257 GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO
SEQRES 2 D 257 PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE
SEQRES 3 D 257 GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE
SEQRES 4 D 257 SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN
SEQRES 5 D 257 LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY
SEQRES 6 D 257 HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET
SEQRES 7 D 257 ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU
SEQRES 8 D 257 HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU
SEQRES 9 D 257 HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS
SEQRES 10 D 257 VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU
SEQRES 11 D 257 ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA
SEQRES 12 D 257 PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU
SEQRES 13 D 257 GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY
SEQRES 14 D 257 SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU
SEQRES 15 D 257 LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY
SEQRES 16 D 257 SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP
SEQRES 17 D 257 THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN
SEQRES 18 D 257 LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP
SEQRES 19 D 257 SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU
SEQRES 20 D 257 ASN GLY ARG VAL ILE GLU ALA SER PHE PRO
HET ZN A 264 1
HET 9FK A 269 24
HET GOL A 273 6
HET ACY A1260 4
HET ACY A1261 4
HET ZN B 264 1
HET 9FK B 268 24
HET GOL B 272 6
HET ACY B1260 4
HET ZN C 264 1
HET 9FK C 267 24
HET GOL C 271 6
HET ACY C1260 4
HET ACY C1261 4
HET ACY C1262 4
HET ZN D 264 1
HET 9FK D 266 24
HET GOL D 271 6
HETNAM ZN ZINC ION
HETNAM 9FK 5-(1-NAPHTHALEN-1-YL-1,2,3-TRIAZOL-4-YL)THIOPHENE-2-
HETNAM 2 9FK SULFONAMIDE
HETNAM GOL GLYCEROL
HETNAM ACY ACETIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 9FK 4(C16 H12 N4 O2 S2)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 8 ACY 6(C2 H4 O2)
FORMUL 23 HOH *1050(H2 O)
HELIX 1 1 PRO A 16 SER A 21 1 6
HELIX 2 2 PRO A 22 GLY A 26 5 5
HELIX 3 3 ARG A 129 LEU A 134 1 6
HELIX 4 4 ASN A 154 SER A 162 1 9
HELIX 5 5 ARG A 163 ALA A 168 5 6
HELIX 6 6 ILE A 181 LEU A 185 5 5
HELIX 7 7 SER A 220 THR A 230 1 11
HELIX 8 8 PRO B 16 VAL B 20 5 5
HELIX 9 9 SER B 21 GLY B 26 5 6
HELIX 10 10 ARG B 35 ALA B 39 5 5
HELIX 11 11 ARG B 129 LEU B 134 1 6
HELIX 12 12 ASN B 154 SER B 162 1 9
HELIX 13 13 ARG B 163 ALA B 168 5 6
HELIX 14 14 ILE B 181 LEU B 185 5 5
HELIX 15 15 SER B 220 THR B 230 1 11
HELIX 16 16 PRO C 16 SER C 21 1 6
HELIX 17 17 PRO C 22 GLY C 26 5 5
HELIX 18 18 ARG C 35 ALA C 39 5 5
HELIX 19 19 ARG C 129 LEU C 134 1 6
HELIX 20 20 ASN C 154 SER C 162 1 9
HELIX 21 21 ARG C 163 ALA C 168 5 6
HELIX 22 22 ILE C 181 LEU C 185 5 5
HELIX 23 23 ALA C 221 LEU C 231 1 11
HELIX 24 24 PRO D 16 SER D 21 1 6
HELIX 25 25 PRO D 22 GLY D 26 5 5
HELIX 26 26 ARG D 129 LEU D 134 1 6
HELIX 27 27 ASN D 154 SER D 162 1 9
HELIX 28 28 ARG D 163 ALA D 168 5 6
HELIX 29 29 ILE D 181 LEU D 185 5 5
HELIX 30 30 SER D 220 THR D 230 1 11
SHEET 1 AA 2 ASP A 33 ILE A 34 0
SHEET 2 AA 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 34
SHEET 1 AB 6 ALA A 40 PHE A 41 0
SHEET 2 AB 6 GLU A 255 ALA A 256 1 N ALA A 256 O ALA A 40
SHEET 3 AB 6 TYR A 192 SER A 198 -1 O GLN A 194 N GLU A 255
SHEET 4 AB 6 GLN A 206 PHE A 213 -1 N GLY A 207 O GLY A 197
SHEET 5 AB 6 LEU A 140 GLU A 149 1 O LEU A 140 N ILE A 209
SHEET 6 AB 6 VAL A 217 LEU A 219 1 O VAL A 217 N GLU A 148
SHEET 1 AC 9 ALA A 40 PHE A 41 0
SHEET 2 AC 9 GLU A 255 ALA A 256 1 N ALA A 256 O ALA A 40
SHEET 3 AC 9 TYR A 192 SER A 198 -1 O GLN A 194 N GLU A 255
SHEET 4 AC 9 GLN A 206 PHE A 213 -1 N GLY A 207 O GLY A 197
SHEET 5 AC 9 LEU A 140 GLU A 149 1 O LEU A 140 N ILE A 209
SHEET 6 AC 9 ALA A 116 SER A 124 -1 O ALA A 116 N LEU A 147
SHEET 7 AC 9 GLU A 87 TRP A 97 -1 O ARG A 89 N LEU A 123
SHEET 8 AC 9 GLU A 79 ALA A 81 -1 O MET A 80 N TYR A 88
SHEET 9 AC 9 GLU A 49 LEU A 51 1 O GLU A 49 N ALA A 81
SHEET 1 AD10 ALA A 40 PHE A 41 0
SHEET 2 AD10 GLU A 255 ALA A 256 1 N ALA A 256 O ALA A 40
SHEET 3 AD10 TYR A 192 SER A 198 -1 O GLN A 194 N GLU A 255
SHEET 4 AD10 GLN A 206 PHE A 213 -1 N GLY A 207 O GLY A 197
SHEET 5 AD10 LEU A 140 GLU A 149 1 O LEU A 140 N ILE A 209
SHEET 6 AD10 ALA A 116 SER A 124 -1 O ALA A 116 N LEU A 147
SHEET 7 AD10 GLU A 87 TRP A 97 -1 O ARG A 89 N LEU A 123
SHEET 8 AD10 VAL A 70 THR A 73 -1 O VAL A 70 N LEU A 95
SHEET 9 AD10 LEU A 61 ASN A 65 -1 O ARG A 62 N THR A 73
SHEET 10 AD10 GLU A 173 VAL A 176 -1 O THR A 174 N LEU A 63
SHEET 1 AE 2 VAL A 217 LEU A 219 0
SHEET 2 AE 2 LEU A 140 GLU A 149 1 O PHE A 146 N VAL A 217
SHEET 1 BA 2 ASP B 33 ILE B 34 0
SHEET 2 BA 2 THR B 108 VAL B 109 1 O THR B 108 N ILE B 34
SHEET 1 BB 6 ALA B 40 PHE B 41 0
SHEET 2 BB 6 GLU B 255 ALA B 256 1 N ALA B 256 O ALA B 40
SHEET 3 BB 6 TYR B 192 SER B 198 -1 O GLN B 194 N GLU B 255
SHEET 4 BB 6 GLN B 206 PHE B 213 -1 N GLY B 207 O GLY B 197
SHEET 5 BB 6 LEU B 140 GLU B 149 1 O LEU B 140 N ILE B 209
SHEET 6 BB 6 VAL B 217 LEU B 219 1 O VAL B 217 N GLU B 148
SHEET 1 BC 9 ALA B 40 PHE B 41 0
SHEET 2 BC 9 GLU B 255 ALA B 256 1 N ALA B 256 O ALA B 40
SHEET 3 BC 9 TYR B 192 SER B 198 -1 O GLN B 194 N GLU B 255
SHEET 4 BC 9 GLN B 206 PHE B 213 -1 N GLY B 207 O GLY B 197
SHEET 5 BC 9 LEU B 140 GLU B 149 1 O LEU B 140 N ILE B 209
SHEET 6 BC 9 ALA B 116 SER B 124 -1 O ALA B 116 N LEU B 147
SHEET 7 BC 9 ARG B 86 TRP B 97 -1 O ARG B 89 N LEU B 123
SHEET 8 BC 9 GLU B 79 GLY B 83 -1 O MET B 80 N TYR B 88
SHEET 9 BC 9 GLU B 49 LEU B 51 1 O GLU B 49 N ALA B 81
SHEET 1 BD10 ALA B 40 PHE B 41 0
SHEET 2 BD10 GLU B 255 ALA B 256 1 N ALA B 256 O ALA B 40
SHEET 3 BD10 TYR B 192 SER B 198 -1 O GLN B 194 N GLU B 255
SHEET 4 BD10 GLN B 206 PHE B 213 -1 N GLY B 207 O GLY B 197
SHEET 5 BD10 LEU B 140 GLU B 149 1 O LEU B 140 N ILE B 209
SHEET 6 BD10 ALA B 116 SER B 124 -1 O ALA B 116 N LEU B 147
SHEET 7 BD10 ARG B 86 TRP B 97 -1 O ARG B 89 N LEU B 123
SHEET 8 BD10 VAL B 70 THR B 73 -1 O VAL B 70 N LEU B 95
SHEET 9 BD10 LEU B 61 ASN B 65 -1 O ARG B 62 N THR B 73
SHEET 10 BD10 GLU B 173 VAL B 176 -1 O THR B 174 N LEU B 63
SHEET 1 BE 2 VAL B 217 LEU B 219 0
SHEET 2 BE 2 LEU B 140 GLU B 149 1 O PHE B 146 N VAL B 217
SHEET 1 CA 2 ASP C 33 ILE C 34 0
SHEET 2 CA 2 THR C 108 VAL C 109 1 O THR C 108 N ILE C 34
SHEET 1 CB 6 ALA C 40 PHE C 41 0
SHEET 2 CB 6 GLU C 255 ALA C 256 1 N ALA C 256 O ALA C 40
SHEET 3 CB 6 TYR C 192 SER C 198 -1 O GLN C 194 N GLU C 255
SHEET 4 CB 6 GLN C 206 PHE C 213 -1 N GLY C 207 O GLY C 197
SHEET 5 CB 6 LEU C 140 GLY C 150 1 O LEU C 140 N ILE C 209
SHEET 6 CB 6 VAL C 217 SER C 220 1 O VAL C 217 N GLU C 148
SHEET 1 CC 9 ALA C 40 PHE C 41 0
SHEET 2 CC 9 GLU C 255 ALA C 256 1 N ALA C 256 O ALA C 40
SHEET 3 CC 9 TYR C 192 SER C 198 -1 O GLN C 194 N GLU C 255
SHEET 4 CC 9 GLN C 206 PHE C 213 -1 N GLY C 207 O GLY C 197
SHEET 5 CC 9 LEU C 140 GLY C 150 1 O LEU C 140 N ILE C 209
SHEET 6 CC 9 ALA C 116 SER C 124 -1 O ALA C 116 N LEU C 147
SHEET 7 CC 9 ARG C 86 TRP C 97 -1 O ARG C 89 N LEU C 123
SHEET 8 CC 9 GLU C 79 GLY C 83 -1 O MET C 80 N TYR C 88
SHEET 9 CC 9 GLU C 49 LEU C 51 1 O GLU C 49 N ALA C 81
SHEET 1 CD10 ALA C 40 PHE C 41 0
SHEET 2 CD10 GLU C 255 ALA C 256 1 N ALA C 256 O ALA C 40
SHEET 3 CD10 TYR C 192 SER C 198 -1 O GLN C 194 N GLU C 255
SHEET 4 CD10 GLN C 206 PHE C 213 -1 N GLY C 207 O GLY C 197
SHEET 5 CD10 LEU C 140 GLY C 150 1 O LEU C 140 N ILE C 209
SHEET 6 CD10 ALA C 116 SER C 124 -1 O ALA C 116 N LEU C 147
SHEET 7 CD10 ARG C 86 TRP C 97 -1 O ARG C 89 N LEU C 123
SHEET 8 CD10 VAL C 70 THR C 73 -1 O VAL C 70 N LEU C 95
SHEET 9 CD10 LEU C 61 ASN C 65 -1 O ARG C 62 N THR C 73
SHEET 10 CD10 GLU C 173 VAL C 176 -1 O THR C 174 N LEU C 63
SHEET 1 CE 2 VAL C 217 SER C 220 0
SHEET 2 CE 2 LEU C 140 GLY C 150 1 O PHE C 146 N VAL C 217
SHEET 1 CF 2 TRP C 232 GLY C 233 0
SHEET 2 CF 2 SER C 237 ARG C 238 -1 O SER C 237 N GLY C 233
SHEET 1 DA 2 ASP D 33 ILE D 34 0
SHEET 2 DA 2 THR D 108 VAL D 109 1 O THR D 108 N ILE D 34
SHEET 1 DB 6 ALA D 40 PHE D 41 0
SHEET 2 DB 6 GLU D 255 ALA D 256 1 N ALA D 256 O ALA D 40
SHEET 3 DB 6 TYR D 192 SER D 198 -1 O GLN D 194 N GLU D 255
SHEET 4 DB 6 GLN D 206 PHE D 213 -1 N GLY D 207 O GLY D 197
SHEET 5 DB 6 LEU D 140 GLU D 149 1 O LEU D 140 N ILE D 209
SHEET 6 DB 6 VAL D 217 LEU D 219 1 O VAL D 217 N GLU D 148
SHEET 1 DC 9 ALA D 40 PHE D 41 0
SHEET 2 DC 9 GLU D 255 ALA D 256 1 N ALA D 256 O ALA D 40
SHEET 3 DC 9 TYR D 192 SER D 198 -1 O GLN D 194 N GLU D 255
SHEET 4 DC 9 GLN D 206 PHE D 213 -1 N GLY D 207 O GLY D 197
SHEET 5 DC 9 LEU D 140 GLU D 149 1 O LEU D 140 N ILE D 209
SHEET 6 DC 9 ALA D 116 SER D 124 -1 O ALA D 116 N LEU D 147
SHEET 7 DC 9 ARG D 86 TRP D 97 -1 O ARG D 89 N LEU D 123
SHEET 8 DC 9 GLU D 79 GLY D 83 -1 O MET D 80 N TYR D 88
SHEET 9 DC 9 GLU D 49 LEU D 51 1 O GLU D 49 N ALA D 81
SHEET 1 DD10 ALA D 40 PHE D 41 0
SHEET 2 DD10 GLU D 255 ALA D 256 1 N ALA D 256 O ALA D 40
SHEET 3 DD10 TYR D 192 SER D 198 -1 O GLN D 194 N GLU D 255
SHEET 4 DD10 GLN D 206 PHE D 213 -1 N GLY D 207 O GLY D 197
SHEET 5 DD10 LEU D 140 GLU D 149 1 O LEU D 140 N ILE D 209
SHEET 6 DD10 ALA D 116 SER D 124 -1 O ALA D 116 N LEU D 147
SHEET 7 DD10 ARG D 86 TRP D 97 -1 O ARG D 89 N LEU D 123
SHEET 8 DD10 VAL D 70 THR D 73 -1 O VAL D 70 N LEU D 95
SHEET 9 DD10 LEU D 61 ASN D 65 -1 O ARG D 62 N THR D 73
SHEET 10 DD10 GLU D 173 VAL D 176 -1 O THR D 174 N LEU D 63
SHEET 1 DE 2 VAL D 217 LEU D 219 0
SHEET 2 DE 2 LEU D 140 GLU D 149 1 O PHE D 146 N VAL D 217
SSBOND 1 CYS A 24 CYS A 204 1555 1555 2.09
SSBOND 2 CYS B 24 CYS B 204 1555 1555 2.07
SSBOND 3 CYS C 24 CYS C 204 1555 1555 2.09
SSBOND 4 CYS D 24 CYS D 204 1555 1555 2.08
LINK ZN ZN A 264 NE2 HIS A 94 1555 1555 2.10
LINK ZN ZN A 264 NE2 HIS A 96 1555 1555 2.10
LINK ZN ZN A 264 ND1 HIS A 119 1555 1555 2.10
LINK ZN ZN A 264 N24 9FK A 269 1555 1555 2.07
LINK ZN ZN B 264 NE2 HIS B 94 1555 1555 2.13
LINK ZN ZN B 264 N24 9FK B 268 1555 1555 2.13
LINK ZN ZN B 264 NE2 HIS B 96 1555 1555 2.21
LINK ZN ZN B 264 ND1 HIS B 119 1555 1555 2.08
LINK ZN ZN C 264 NE2 HIS C 94 1555 1555 2.19
LINK ZN ZN C 264 NE2 HIS C 96 1555 1555 2.14
LINK ZN ZN C 264 ND1 HIS C 119 1555 1555 2.10
LINK ZN ZN C 264 N24 9FK C 267 1555 1555 2.10
LINK ZN ZN D 264 NE2 HIS D 96 1555 1555 2.24
LINK ZN ZN D 264 N24 9FK D 266 1555 1555 2.10
LINK ZN ZN D 264 S21 9FK D 266 1555 1555 2.97
LINK ZN ZN D 264 ND1 HIS D 119 1555 1555 2.05
LINK ZN ZN D 264 NE2 HIS D 94 1555 1555 2.14
CISPEP 1 ASP A 14 PRO A 15 0 0.90
CISPEP 2 SER A 30 PRO A 31 0 -0.07
CISPEP 3 LEU A 58 PRO A 59 0 8.97
CISPEP 4 PRO A 202 PRO A 203 0 10.05
CISPEP 5 ASP B 14 PRO B 15 0 15.40
CISPEP 6 SER B 30 PRO B 31 0 -1.26
CISPEP 7 LEU B 58 PRO B 59 0 4.17
CISPEP 8 PRO B 202 PRO B 203 0 9.37
CISPEP 9 ASP C 14 PRO C 15 0 -1.91
CISPEP 10 SER C 30 PRO C 31 0 -0.39
CISPEP 11 LEU C 58 PRO C 59 0 7.97
CISPEP 12 PRO C 202 PRO C 203 0 8.75
CISPEP 13 ASP D 14 PRO D 15 0 3.55
CISPEP 14 SER D 30 PRO D 31 0 3.54
CISPEP 15 LEU D 58 PRO D 59 0 2.73
CISPEP 16 PRO D 202 PRO D 203 0 14.56
SITE 1 AC1 5 HIS A 94 HIS A 96 HIS A 119 9FK A 269
SITE 2 AC1 5 GOL A 273
SITE 1 AC2 14 GLN A 92 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC2 14 VAL A 130 LEU A 134 LEU A 199 THR A 200
SITE 3 AC2 14 THR A 201 TRP A 210 ZN A 264 GOL A 273
SITE 4 AC2 14 HOH A2348 ARG C 129
SITE 1 AC3 11 ASN A 66 HIS A 68 SER A 69 GLN A 71
SITE 2 AC3 11 GLN A 92 HIS A 94 THR A 201 ZN A 264
SITE 3 AC3 11 9FK A 269 HOH A2005 HOH A2134
SITE 1 AC4 4 HIS B 94 HIS B 96 HIS B 119 9FK B 268
SITE 1 AC5 11 HIS B 94 HIS B 96 HIS B 119 LEU B 134
SITE 2 AC5 11 LEU B 199 THR B 200 THR B 201 TRP B 210
SITE 3 AC5 11 ZN B 264 GOL B 272 HOH B2143
SITE 1 AC6 9 ASN B 66 HIS B 68 SER B 69 GLN B 71
SITE 2 AC6 9 GLN B 92 HIS B 94 9FK B 268 HOH B2005
SITE 3 AC6 9 HOH B2244
SITE 1 AC7 4 HIS C 94 HIS C 96 HIS C 119 9FK C 267
SITE 1 AC8 15 ARG A 129 GLN C 92 HIS C 94 HIS C 96
SITE 2 AC8 15 HIS C 119 VAL C 121 VAL C 130 ASP C 131
SITE 3 AC8 15 LEU C 134 LEU C 199 THR C 200 THR C 201
SITE 4 AC8 15 TRP C 210 ZN C 264 GOL C 271
SITE 1 AC9 9 ASN C 66 HIS C 68 GLN C 71 GLN C 92
SITE 2 AC9 9 HIS C 94 THR C 201 9FK C 267 HOH C2005
SITE 3 AC9 9 HOH C2224
SITE 1 BC1 4 HIS D 94 HIS D 96 HIS D 119 9FK D 266
SITE 1 BC2 11 HIS D 94 HIS D 96 HIS D 119 LEU D 134
SITE 2 BC2 11 LEU D 199 THR D 200 THR D 201 TRP D 210
SITE 3 BC2 11 ZN D 264 GOL D 271 HOH D2102
SITE 1 BC3 8 ASN D 66 HIS D 68 SER D 69 GLN D 71
SITE 2 BC3 8 GLN D 92 HIS D 94 9FK D 266 HOH D2003
SITE 1 BC4 7 GLY A 98 ALA A 99 ARG A 102 PRO A 115
SITE 2 BC4 7 LEU A 224 SER A 228 HOH A2350
SITE 1 BC5 2 HIS B 112 HOH B2161
SITE 1 BC6 5 SER B 187 HOH B2253 PRO C 248 LEU C 249
SITE 2 BC6 5 ASN C 250
SITE 1 BC7 5 HOH B2225 ARG C 27 PHE C 28 ASN C 250
SITE 2 BC7 5 HOH C2225
SITE 1 BC8 6 LEU A 249 ASN A 250 HOH A2340 HOH A2351
SITE 2 BC8 6 HOH A2352 SER D 187
SITE 1 BC9 8 PHE C 28 GLU C 196 GLY C 197 GLN C 206
SITE 2 BC9 8 GLY C 207 HOH C2202 HOH C2226 PRO D 84
CRYST1 152.290 152.290 172.130 90.00 90.00 120.00 H 3 36
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 0.006566 0.003791 0.000000 0.00000
SCALE2 0.000000 0.007582 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005810 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
