HEADER LYASE 10-APR-18 6G98
TITLE THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN COMPLEX
TITLE 2 WITH SULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 9;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE IX,CARBONIC ANHYDRASE IX,CAIX,MEMBRANE
COMPND 5 ANTIGEN MN,P54/58N,RENAL CELL CARCINOMA-ASSOCIATED ANTIGEN G250,RCC-
COMPND 6 ASSOCIATED ANTIGEN G250,PMW1;
COMPND 7 EC: 4.2.1.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 OTHER_DETAILS: A, B, C, D CHAINS ARE IDENTICAL.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CA9, G250, MN;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LEITANS,K.TARS
REVDAT 1 04-JUL-18 6G98 0
JRNL AUTH J.KAZOKAITE,R.NIEMANS,V.DUDUTIENE,H.M.BECKER,J.LEITANS,
JRNL AUTH 2 A.ZUBRIENE,L.BARANAUSKIENE,G.GONDI,R.ZEIDLER,J.MATULIENE,
JRNL AUTH 3 K.TARS,A.YAROMINA,P.LAMBIN,L.J.DUBOIS,D.MATULIS
JRNL TITL NOVEL FLUORINATED CARBONIC ANHYDRASE IX INHIBITORS REDUCE
JRNL TITL 2 HYPOXIA-INDUCED ACIDIFICATION AND CLONOGENIC SURVIVAL OF
JRNL TITL 3 CANCER CELLS.
JRNL REF ONCOTARGET V. 9 26800 2018
JRNL REFN ESSN 1949-2553
JRNL PMID 29928486
JRNL DOI 10.18632/ONCOTARGET.25508
REMARK 2
REMARK 2 RESOLUTION. 2.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 50547
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2703
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) : 2.47
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.53
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3768
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 190
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7397
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 422
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -1.38000
REMARK 3 B12 (A**2) : 0.21000
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): 0.278
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.172
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.097
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7748 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7079 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10545 ; 1.453 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16423 ; 0.943 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 942 ; 6.091 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 345 ;36.979 ;23.246
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1139 ;14.143 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;17.309 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1144 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8553 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1563 ; 0.003 ; 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): 3828 ; 2.233 ; 3.896
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3827 ; 2.227 ; 3.895
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4750 ; 3.681 ; 5.828
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4751 ; 3.682 ; 5.829
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3920 ; 2.734 ; 4.244
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3921 ; 2.734 ; 4.244
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5796 ; 4.548 ; 6.251
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8067 ; 6.839 ;45.423
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7999 ; 6.817 ;45.310
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 : NULL
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
REMARK 4
REMARK 4 6G98 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1200009602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-18
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 : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91840
REMARK 200 MONOCHROMATOR : KMC-1
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53252
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.470
REMARK 200 RESOLUTION RANGE LOW (A) : 76.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.16600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.81100
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: NULL
REMARK 200 STARTING MODEL: 5FL4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
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 76.19500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.99120
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.27667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 76.19500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 43.99120
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.27667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 76.19500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 43.99120
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.27667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 87.98241
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 114.55333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 87.98241
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 114.55333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 87.98241
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 114.55333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 2
REMARK 465 PRO A 3
REMARK 465 ASP A 4
REMARK 465 GLN A 5
REMARK 465 SER A 6
REMARK 465 HIS A 7
REMARK 465 TRP A 8
REMARK 465 ARG A 9
REMARK 465 TYR A 10
REMARK 465 GLY A 11
REMARK 465 GLY A 12
REMARK 465 ASP A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 TRP A 16
REMARK 465 PRO A 17
REMARK 465 GLY B 2
REMARK 465 PRO B 3
REMARK 465 ASP B 4
REMARK 465 GLN B 5
REMARK 465 SER B 6
REMARK 465 HIS B 7
REMARK 465 TRP B 8
REMARK 465 ARG B 9
REMARK 465 TYR B 10
REMARK 465 GLY B 11
REMARK 465 GLY B 12
REMARK 465 ASP B 13
REMARK 465 PRO B 14
REMARK 465 PRO B 15
REMARK 465 GLY C 2
REMARK 465 PRO C 3
REMARK 465 ASP C 4
REMARK 465 GLN C 5
REMARK 465 SER C 6
REMARK 465 HIS C 7
REMARK 465 TRP C 8
REMARK 465 ARG C 9
REMARK 465 TYR C 10
REMARK 465 GLY C 11
REMARK 465 GLY C 12
REMARK 465 ASP C 13
REMARK 465 PRO C 14
REMARK 465 PRO C 15
REMARK 465 TRP C 16
REMARK 465 PRO C 17
REMARK 465 ARG C 18
REMARK 465 VAL C 19
REMARK 465 GLY D 2
REMARK 465 PRO D 3
REMARK 465 ASP D 4
REMARK 465 GLN D 5
REMARK 465 SER D 6
REMARK 465 HIS D 7
REMARK 465 TRP D 8
REMARK 465 ARG D 9
REMARK 465 TYR D 10
REMARK 465 GLY D 11
REMARK 465 GLY D 12
REMARK 465 ASP D 13
REMARK 465 PRO D 14
REMARK 465 PRO D 15
REMARK 465 TRP D 16
REMARK 465 PRO D 17
REMARK 465 ARG D 18
REMARK 465 VAL D 19
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 ARG A 18 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 238 CG OD1 OD2
REMARK 470 ARG B 18 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 238 CG OD1 OD2
REMARK 470 ASP C 238 CG OD1 OD2
REMARK 470 LYS D 221 CG CD CE NZ
REMARK 470 ASP D 238 CG OD1 OD2
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 20 83.53 70.38
REMARK 500 ARG A 86 75.48 -108.72
REMARK 500 ASP A 238 58.81 -104.82
REMARK 500 ASN A 244 57.90 -92.02
REMARK 500 ARG B 86 78.58 -114.43
REMARK 500 ASP B 238 67.88 -112.06
REMARK 500 ASN B 244 56.52 -96.57
REMARK 500 PHE C 27 72.81 -116.45
REMARK 500 ASP C 180 99.79 -63.06
REMARK 500 ASN C 244 49.94 -105.94
REMARK 500 ARG D 86 73.07 -106.04
REMARK 500 ASP D 238 44.86 31.43
REMARK 500 ASN D 244 47.08 -89.95
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 103.1
REMARK 620 3 HIS A 119 ND1 112.2 98.7
REMARK 620 4 ER5 A 302 N40 106.8 123.7 112.1
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 104.3
REMARK 620 3 HIS B 119 ND1 114.7 94.2
REMARK 620 4 ER5 B 302 N40 113.9 116.8 111.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 94 NE2
REMARK 620 2 HIS C 96 NE2 99.7
REMARK 620 3 HIS C 119 ND1 114.0 96.6
REMARK 620 4 ER5 C 302 N40 112.2 120.9 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 94 NE2
REMARK 620 2 HIS D 96 NE2 98.7
REMARK 620 3 HIS D 119 ND1 115.5 96.3
REMARK 620 4 ER5 D 302 N40 113.6 117.9 113.1
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER5 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 ER5 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER5 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ER5 D 302
DBREF 6G98 A 2 261 UNP Q16790 CAH9_HUMAN 135 391
DBREF 6G98 B 2 261 UNP Q16790 CAH9_HUMAN 135 391
DBREF 6G98 C 2 261 UNP Q16790 CAH9_HUMAN 135 391
DBREF 6G98 D 2 261 UNP Q16790 CAH9_HUMAN 135 391
SEQADV 6G98 PRO A 3 UNP Q16790 ASP 136 CONFLICT
SEQADV 6G98 SER A 41 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 6G98 PRO B 3 UNP Q16790 ASP 136 CONFLICT
SEQADV 6G98 SER B 41 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 6G98 PRO C 3 UNP Q16790 ASP 136 CONFLICT
SEQADV 6G98 SER C 41 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 6G98 PRO D 3 UNP Q16790 ASP 136 CONFLICT
SEQADV 6G98 SER D 41 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 301 1
HET ER5 A 302 38
HET ZN B 301 1
HET ER5 B 302 38
HET ZN C 301 1
HET ER5 C 302 38
HET ZN D 301 1
HET ER5 D 302 38
HETNAM ZN ZINC ION
HETNAM ER5 4-[2-[3-(CYCLODODECYLAMINO)-2,5,6-TRIS(FLUORANYL)-4-
HETNAM 2 ER5 SULFAMOYL-PHENYL]SULFANYLETHYL]BENZOIC ACID
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 ER5 4(C27 H35 F3 N2 O4 S2)
FORMUL 13 HOH *422(H2 O)
HELIX 1 AA1 SER A 20 GLY A 25 5 6
HELIX 2 AA2 ARG A 34 ALA A 38 5 5
HELIX 3 AA3 ARG A 130 LEU A 135 1 6
HELIX 4 AA4 ASN A 154 SER A 162 1 9
HELIX 5 AA5 ARG A 163 ALA A 168 5 6
HELIX 6 AA6 ASP A 180 LEU A 185 5 6
HELIX 7 AA7 SER A 219 THR A 228 1 11
HELIX 8 AA8 SER B 20 GLY B 25 5 6
HELIX 9 AA9 ARG B 34 ALA B 38 5 5
HELIX 10 AB1 ARG B 130 LEU B 135 1 6
HELIX 11 AB2 ASN B 154 SER B 162 1 9
HELIX 12 AB3 ARG B 163 ALA B 168 5 6
HELIX 13 AB4 ASP B 180 LEU B 185 5 6
HELIX 14 AB5 SER B 219 THR B 228 1 11
HELIX 15 AB6 SER C 20 GLY C 25 5 6
HELIX 16 AB7 ARG C 34 ALA C 38 5 5
HELIX 17 AB8 ARG C 130 LEU C 135 1 6
HELIX 18 AB9 ASN C 154 SER C 162 1 9
HELIX 19 AC1 ARG C 163 ALA C 168 5 6
HELIX 20 AC2 ASP C 180 LEU C 185 5 6
HELIX 21 AC3 SER C 219 THR C 228 1 11
HELIX 22 AC4 SER D 20 GLY D 25 5 6
HELIX 23 AC5 ARG D 130 LEU D 135 1 6
HELIX 24 AC6 ASN D 154 SER D 162 1 9
HELIX 25 AC7 ARG D 163 ALA D 168 5 6
HELIX 26 AC8 ASP D 180 LEU D 185 5 6
HELIX 27 AC9 ALA D 220 THR D 228 1 10
SHEET 1 AA1 2 ASP A 32 ILE A 33 0
SHEET 2 AA1 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 AA210 ALA A 39 PHE A 40 0
SHEET 2 AA210 GLU A 257 ALA A 258 1 O ALA A 258 N ALA A 39
SHEET 3 AA210 TYR A 191 GLY A 196 -1 N GLN A 193 O GLU A 257
SHEET 4 AA210 VAL A 207 PHE A 212 -1 O VAL A 211 N PHE A 192
SHEET 5 AA210 LEU A 141 GLU A 150 1 N ALA A 145 O THR A 210
SHEET 6 AA210 ALA A 116 SER A 124 -1 N ALA A 116 O LEU A 148
SHEET 7 AA210 ARG A 86 TRP A 97 -1 N LEU A 91 O VAL A 121
SHEET 8 AA210 VAL A 66 THR A 69 -1 N LEU A 68 O LEU A 93
SHEET 9 AA210 LEU A 57 ASN A 61 -1 N ARG A 60 O GLN A 67
SHEET 10 AA210 GLU A 173 VAL A 176 -1 O VAL A 176 N LEU A 57
SHEET 1 AA3 6 GLU A 48 LEU A 50 0
SHEET 2 AA3 6 GLU A 78 GLY A 82 -1 O GLU A 78 N LEU A 50
SHEET 3 AA3 6 ARG A 86 TRP A 97 -1 O TYR A 88 N MET A 79
SHEET 4 AA3 6 ALA A 116 SER A 124 -1 O VAL A 121 N LEU A 91
SHEET 5 AA3 6 LEU A 141 GLU A 150 -1 O LEU A 148 N ALA A 116
SHEET 6 AA3 6 VAL A 216 LEU A 218 1 O LEU A 218 N GLU A 149
SHEET 1 AA4 2 ASP B 32 ILE B 33 0
SHEET 2 AA4 2 THR B 108 VAL B 109 1 O THR B 108 N ILE B 33
SHEET 1 AA510 ALA B 39 PHE B 40 0
SHEET 2 AA510 GLU B 257 ALA B 258 1 O ALA B 258 N ALA B 39
SHEET 3 AA510 TYR B 191 GLY B 196 -1 N GLN B 193 O GLU B 257
SHEET 4 AA510 VAL B 207 PHE B 212 -1 O VAL B 211 N PHE B 192
SHEET 5 AA510 LEU B 141 GLU B 150 1 N ALA B 145 O THR B 210
SHEET 6 AA510 ALA B 116 SER B 124 -1 N ALA B 116 O LEU B 148
SHEET 7 AA510 ARG B 86 TRP B 97 -1 N LEU B 91 O VAL B 121
SHEET 8 AA510 VAL B 66 THR B 69 -1 N LEU B 68 O LEU B 93
SHEET 9 AA510 LEU B 57 ASN B 61 -1 N ARG B 60 O GLN B 67
SHEET 10 AA510 GLU B 173 VAL B 176 -1 O VAL B 176 N LEU B 57
SHEET 1 AA6 6 GLU B 48 LEU B 50 0
SHEET 2 AA6 6 GLU B 78 GLY B 82 -1 O GLU B 78 N LEU B 50
SHEET 3 AA6 6 ARG B 86 TRP B 97 -1 O TYR B 88 N MET B 79
SHEET 4 AA6 6 ALA B 116 SER B 124 -1 O VAL B 121 N LEU B 91
SHEET 5 AA6 6 LEU B 141 GLU B 150 -1 O LEU B 148 N ALA B 116
SHEET 6 AA6 6 VAL B 216 LEU B 218 1 O VAL B 216 N GLU B 149
SHEET 1 AA7 2 ASP C 32 ILE C 33 0
SHEET 2 AA7 2 THR C 108 VAL C 109 1 O THR C 108 N ILE C 33
SHEET 1 AA810 ALA C 39 PHE C 40 0
SHEET 2 AA810 GLU C 257 ALA C 258 1 O ALA C 258 N ALA C 39
SHEET 3 AA810 TYR C 191 SER C 197 -1 N GLN C 193 O GLU C 257
SHEET 4 AA810 GLN C 205 PHE C 212 -1 O VAL C 207 N GLY C 196
SHEET 5 AA810 LEU C 141 GLU C 150 1 N VAL C 143 O ILE C 208
SHEET 6 AA810 ALA C 116 SER C 124 -1 N HIS C 122 O ALA C 142
SHEET 7 AA810 ARG C 86 TRP C 97 -1 N ARG C 89 O LEU C 123
SHEET 8 AA810 VAL C 66 THR C 69 -1 N LEU C 68 O LEU C 93
SHEET 9 AA810 LEU C 57 ASN C 61 -1 N ARG C 60 O GLN C 67
SHEET 10 AA810 GLU C 173 VAL C 176 -1 O VAL C 176 N LEU C 57
SHEET 1 AA9 6 GLU C 48 LEU C 50 0
SHEET 2 AA9 6 GLU C 78 GLY C 82 -1 O GLU C 78 N LEU C 50
SHEET 3 AA9 6 ARG C 86 TRP C 97 -1 O TYR C 88 N MET C 79
SHEET 4 AA9 6 ALA C 116 SER C 124 -1 O LEU C 123 N ARG C 89
SHEET 5 AA9 6 LEU C 141 GLU C 150 -1 O ALA C 142 N HIS C 122
SHEET 6 AA9 6 VAL C 216 LEU C 218 1 O LEU C 218 N GLU C 149
SHEET 1 AB1 2 ASP D 32 ILE D 33 0
SHEET 2 AB1 2 THR D 108 VAL D 109 1 O THR D 108 N ILE D 33
SHEET 1 AB210 ALA D 39 PHE D 40 0
SHEET 2 AB210 GLU D 257 ALA D 258 1 O ALA D 258 N ALA D 39
SHEET 3 AB210 TYR D 191 SER D 197 -1 N GLN D 193 O GLU D 257
SHEET 4 AB210 GLN D 205 PHE D 212 -1 O VAL D 207 N GLY D 196
SHEET 5 AB210 LEU D 141 GLY D 151 1 N ALA D 145 O THR D 210
SHEET 6 AB210 ALA D 116 SER D 124 -1 N HIS D 122 O ALA D 142
SHEET 7 AB210 ARG D 86 TRP D 97 -1 N LEU D 91 O VAL D 121
SHEET 8 AB210 VAL D 66 THR D 69 -1 N LEU D 68 O LEU D 93
SHEET 9 AB210 LEU D 57 ASN D 61 -1 N ARG D 60 O GLN D 67
SHEET 10 AB210 GLU D 173 VAL D 176 -1 O THR D 174 N LEU D 59
SHEET 1 AB3 6 GLU D 48 LEU D 50 0
SHEET 2 AB3 6 GLU D 78 GLY D 82 -1 O GLU D 78 N LEU D 50
SHEET 3 AB3 6 ARG D 86 TRP D 97 -1 O TYR D 88 N MET D 79
SHEET 4 AB3 6 ALA D 116 SER D 124 -1 O VAL D 121 N LEU D 91
SHEET 5 AB3 6 LEU D 141 GLY D 151 -1 O ALA D 142 N HIS D 122
SHEET 6 AB3 6 VAL D 216 SER D 219 1 O LEU D 218 N GLU D 149
SSBOND 1 CYS A 23 CYS A 203 1555 1555 2.11
SSBOND 2 CYS B 23 CYS B 203 1555 1555 2.10
SSBOND 3 CYS C 23 CYS C 203 1555 1555 2.10
SSBOND 4 CYS D 23 CYS D 203 1555 1555 2.10
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.10
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.07
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.12
LINK NE2 HIS B 94 ZN ZN B 301 1555 1555 1.99
LINK NE2 HIS B 96 ZN ZN B 301 1555 1555 2.10
LINK ND1 HIS B 119 ZN ZN B 301 1555 1555 2.09
LINK NE2 HIS C 94 ZN ZN C 301 1555 1555 2.05
LINK NE2 HIS C 96 ZN ZN C 301 1555 1555 2.07
LINK ND1 HIS C 119 ZN ZN C 301 1555 1555 2.06
LINK NE2 HIS D 94 ZN ZN D 301 1555 1555 1.96
LINK NE2 HIS D 96 ZN ZN D 301 1555 1555 2.13
LINK ND1 HIS D 119 ZN ZN D 301 1555 1555 1.97
LINK ZN ZN A 301 N40 ER5 A 302 1555 1555 2.01
LINK ZN ZN B 301 N40 ER5 B 302 1555 1555 2.09
LINK ZN ZN C 301 N40 ER5 C 302 1555 1555 1.95
LINK ZN ZN D 301 N40 ER5 D 302 1555 1555 2.19
CISPEP 1 SER A 29 PRO A 30 0 -2.61
CISPEP 2 LEU A 54B PRO A 55 0 -2.56
CISPEP 3 PRO A 201 PRO A 202 0 16.31
CISPEP 4 SER B 29 PRO B 30 0 -2.20
CISPEP 5 LEU B 54B PRO B 55 0 0.66
CISPEP 6 PRO B 201 PRO B 202 0 11.77
CISPEP 7 SER C 29 PRO C 30 0 -3.18
CISPEP 8 LEU C 54B PRO C 55 0 2.77
CISPEP 9 PRO C 201 PRO C 202 0 11.23
CISPEP 10 SER D 29 PRO D 30 0 1.84
CISPEP 11 LEU D 54B PRO D 55 0 6.54
CISPEP 12 PRO D 201 PRO D 202 0 17.10
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 ER5 A 302
SITE 1 AC2 14 ARG A 60 ASN A 62 GLN A 67 GLN A 92
SITE 2 AC2 14 HIS A 94 HIS A 96 HIS A 119 VAL A 121
SITE 3 AC2 14 VAL A 131 LEU A 198 THR A 199 THR A 200
SITE 4 AC2 14 ZN A 301 HOH A 405
SITE 1 AC3 5 HIS B 94 HIS B 96 GLU B 106 HIS B 119
SITE 2 AC3 5 ER5 B 302
SITE 1 AC4 15 ARG B 60 ASN B 62 HIS B 64 GLN B 67
SITE 2 AC4 15 GLN B 92 HIS B 94 HIS B 96 GLU B 106
SITE 3 AC4 15 HIS B 119 VAL B 121 VAL B 131 LEU B 198
SITE 4 AC4 15 THR B 199 THR B 200 ZN B 301
SITE 1 AC5 4 HIS C 94 HIS C 96 HIS C 119 ER5 C 302
SITE 1 AC6 14 ARG C 60 ASN C 62 GLN C 67 GLN C 92
SITE 2 AC6 14 HIS C 94 HIS C 96 HIS C 119 VAL C 121
SITE 3 AC6 14 VAL C 131 LEU C 198 THR C 199 THR C 200
SITE 4 AC6 14 PRO C 202 ZN C 301
SITE 1 AC7 4 HIS D 94 HIS D 96 HIS D 119 ER5 D 302
SITE 1 AC8 12 ARG D 60 ASN D 62 HIS D 64 GLN D 67
SITE 2 AC8 12 GLN D 92 HIS D 94 HIS D 96 HIS D 119
SITE 3 AC8 12 LEU D 198 THR D 199 THR D 200 ZN D 301
CRYST1 152.390 152.390 171.830 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 0.006562 0.003789 0.000000 0.00000
SCALE2 0.000000 0.007577 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005820 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
