HEADER LYASE 28-DEC-17 6FE1
TITLE THREE DIMENSIONAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE IX IN COMPLEX
TITLE 2 WITH BENZENESULFONAMIDE.
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
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 6FE1 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. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 102100
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5404
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7470
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 338
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7667
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 736
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.88000
REMARK 3 B22 (A**2) : 0.88000
REMARK 3 B33 (A**2) : -2.85000
REMARK 3 B12 (A**2) : 0.44000
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): 0.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.042
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8077 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7329 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11028 ; 1.469 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17012 ; 0.942 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 995 ; 5.908 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 364 ;36.883 ;23.077
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1174 ;12.809 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;15.905 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1193 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8925 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1651 ; 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): 3983 ; 2.217 ; 3.794
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3982 ; 2.216 ; 3.793
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4944 ; 3.487 ; 5.658
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4945 ; 3.487 ; 5.659
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4094 ; 2.661 ; 4.093
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4095 ; 2.661 ; 4.094
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6074 ; 4.294 ; 6.057
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8902 ; 7.082 ;45.787
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8704 ; 6.993 ;45.214
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 6FE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200008155.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-16
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) : 0.91841
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 : 107506
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 25.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50100
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: 3IAI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
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 76.01000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.88439
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.40333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 76.01000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 43.88439
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 57.40333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 76.01000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 43.88439
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.40333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 87.76879
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 114.80667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 87.76879
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 114.80667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 87.76879
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 114.80667
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: 1640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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: 20410 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 -1
REMARK 465 PRO A 0
REMARK 465 ASP A 1
REMARK 465 GLN A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
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 -1
REMARK 465 PRO C 0
REMARK 465 ASP C 1
REMARK 465 GLN C 2
REMARK 465 SER C 3
REMARK 465 HIS C 4
REMARK 465 GLY D -1
REMARK 465 PRO D 0
REMARK 465 ASP D 1
REMARK 465 GLN D 2
REMARK 465 SER D 3
REMARK 465 HIS D 4
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 6 CG CD NE CZ NH1 NH2
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 ARG C 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 18 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 238 CG OD1 OD2
REMARK 470 ARG D 6 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 18 CG CD NE CZ NH1 NH2
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: 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 443 O HOH B 443 2555 0.71
REMARK 500 O HOH B 439 O HOH B 439 3555 2.01
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 PRO A 72 C GLY A 76 N 0.303
REMARK 500 GLY A 82 C PRO A 84 N 0.242
REMARK 500 THR A 125 C ALA A 127 N 0.269
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 PRO A 72 O - C - N ANGL. DEV. = -15.0 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 PHE A 27 69.04 -119.64
REMARK 500 ALA A 100 112.62 -27.62
REMARK 500 ASN A 244 53.80 -90.21
REMARK 500 ARG B 86 79.94 -109.98
REMARK 500 ALA B 99 129.68 -174.37
REMARK 500 ASN B 244 58.23 -91.89
REMARK 500 PHE C 27 70.47 -119.57
REMARK 500 ARG C 86 76.84 -118.95
REMARK 500 ASN C 244 54.08 -96.04
REMARK 500 ALA D 100 105.98 -41.74
REMARK 500 ASN D 244 50.18 -90.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO A 72 18.92
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 106.6
REMARK 620 3 HIS A 119 ND1 114.2 100.0
REMARK 620 4 V14 A 302 N10 114.0 115.2 106.2
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 102.4
REMARK 620 3 HIS B 119 ND1 115.3 97.3
REMARK 620 4 V14 B 302 N10 120.2 111.2 108.0
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 106.4
REMARK 620 3 HIS C 119 ND1 109.9 103.3
REMARK 620 4 V14 C 302 N10 115.3 112.1 109.2
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 108.2
REMARK 620 3 HIS D 119 ND1 116.1 95.7
REMARK 620 4 V14 D 302 S7 91.6 134.1 112.5
REMARK 620 5 V14 D 302 N10 120.1 108.9 105.0 30.8
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue V14 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 V14 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 V14 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 V14 D 302
DBREF 6FE1 A 1 261 UNP Q16790 CAH9_HUMAN 137 391
DBREF 6FE1 B 4 261 UNP Q16790 CAH9_HUMAN 137 391
DBREF 6FE1 C 1 261 UNP Q16790 CAH9_HUMAN 137 391
DBREF 6FE1 D 1 261 UNP Q16790 CAH9_HUMAN 137 391
SEQADV 6FE1 GLY A -1 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 PRO A 0 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 SER A 41 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 6FE1 GLY B 2 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 PRO B 3 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 SER B 41 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 6FE1 GLY C -1 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 PRO C 0 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 SER C 41 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 6FE1 GLY D -1 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 PRO D 0 UNP Q16790 EXPRESSION TAG
SEQADV 6FE1 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 V14 A 302 28
HET ZN B 301 1
HET V14 B 302 28
HET ZN C 301 1
HET V14 C 302 28
HET ZN D 301 1
HET V14 D 302 28
HETNAM ZN ZINC ION
HETNAM V14 3-(CYCLOOCTYLAMINO)-2,5,6-TRIFLUORO-4-[(2-
HETNAM 2 V14 HYDROXYETHYL)SULFONYL]BENZENESULFONAMIDE
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 V14 4(C16 H23 F3 N2 O5 S2)
FORMUL 13 HOH *736(H2 O)
HELIX 1 AA1 TRP A 16 SER A 20 1 5
HELIX 2 AA2 PRO A 21 GLY A 25 5 5
HELIX 3 AA3 ARG A 34 ALA A 38 5 5
HELIX 4 AA4 ARG A 130 LEU A 135 1 6
HELIX 5 AA5 ASN A 154 SER A 162 1 9
HELIX 6 AA6 ARG A 163 ALA A 168 5 6
HELIX 7 AA7 ASP A 180 LEU A 185 5 6
HELIX 8 AA8 SER A 219 THR A 228 1 11
HELIX 9 AA9 SER B 20 GLY B 25 5 6
HELIX 10 AB1 ARG B 34 ALA B 38 5 5
HELIX 11 AB2 ARG B 130 LEU B 135 1 6
HELIX 12 AB3 ASN B 154 SER B 162 1 9
HELIX 13 AB4 ARG B 163 ALA B 168 5 6
HELIX 14 AB5 ASP B 180 LEU B 185 5 6
HELIX 15 AB6 SER B 219 THR B 228 1 11
HELIX 16 AB7 TRP C 16 SER C 20 1 5
HELIX 17 AB8 PRO C 21 GLY C 25 5 5
HELIX 18 AB9 ARG C 34 ALA C 38 5 5
HELIX 19 AC1 ARG C 130 LEU C 135 1 6
HELIX 20 AC2 ASN C 154 SER C 162 1 9
HELIX 21 AC3 ARG C 163 ALA C 168 5 6
HELIX 22 AC4 ASP C 180 LEU C 185 5 6
HELIX 23 AC5 SER C 219 THR C 228 1 11
HELIX 24 AC6 TRP D 16 SER D 20 1 5
HELIX 25 AC7 PRO D 21 GLY D 25 5 5
HELIX 26 AC8 ARG D 130 LEU D 135 1 6
HELIX 27 AC9 ASN D 154 SER D 162 1 9
HELIX 28 AD1 ARG D 163 ALA D 168 5 6
HELIX 29 AD2 ASP D 180 LEU D 185 5 6
HELIX 30 AD3 SER D 219 LEU D 229 1 12
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 SER A 197 -1 N GLN A 193 O GLU A 257
SHEET 4 AA210 GLN A 205 PHE A 212 -1 O VAL A 207 N GLY A 196
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 SER B 197 -1 N GLN B 193 O GLU B 257
SHEET 4 AA510 GLN B 205 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 ARG B 86 N GLY B 82
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 ALA C 145 O THR C 210
SHEET 6 AA810 ALA C 116 SER C 124 -1 N ALA C 116 O LEU C 148
SHEET 7 AA810 ARG C 86 TRP C 97 -1 N LEU C 91 O VAL C 121
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 VAL C 121 N LEU C 91
SHEET 5 AA9 6 LEU C 141 GLU C 150 -1 O LEU C 148 N ALA C 116
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 211 N PHE D 192
SHEET 5 AB210 LEU D 141 GLU D 150 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 VAL D 176 N LEU D 57
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 GLU D 150 -1 O ALA D 142 N HIS D 122
SHEET 6 AB3 6 VAL D 216 LEU D 218 1 O VAL D 216 N GLU D 149
SSBOND 1 CYS A 23 CYS A 203 1555 1555 2.07
SSBOND 2 CYS B 23 CYS B 203 1555 1555 2.03
SSBOND 3 CYS C 23 CYS C 203 1555 1555 2.05
SSBOND 4 CYS D 23 CYS D 203 1555 1555 2.06
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.08
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.03
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.09
LINK NE2 HIS B 94 ZN ZN B 301 1555 1555 2.02
LINK NE2 HIS B 96 ZN ZN B 301 1555 1555 2.07
LINK ND1 HIS B 119 ZN ZN B 301 1555 1555 2.08
LINK NE2 HIS C 94 ZN ZN C 301 1555 1555 2.14
LINK NE2 HIS C 96 ZN ZN C 301 1555 1555 2.11
LINK ND1 HIS C 119 ZN ZN C 301 1555 1555 1.92
LINK NE2 HIS D 94 ZN ZN D 301 1555 1555 1.93
LINK NE2 HIS D 96 ZN ZN D 301 1555 1555 2.15
LINK ND1 HIS D 119 ZN ZN D 301 1555 1555 1.98
LINK ZN ZN A 301 N10 V14 A 302 1555 1555 1.98
LINK ZN ZN B 301 N10 V14 B 302 1555 1555 2.04
LINK ZN ZN C 301 N10 V14 C 302 1555 1555 1.98
LINK ZN ZN D 301 S7 V14 D 302 1555 1555 2.99
LINK ZN ZN D 301 N10 V14 D 302 1555 1555 2.08
CISPEP 1 ASP A 10 PRO A 11 0 -3.08
CISPEP 2 SER A 29 PRO A 30 0 -4.89
CISPEP 3 LEU A 54B PRO A 55 0 0.68
CISPEP 4 PRO A 201 PRO A 202 0 12.48
CISPEP 5 SER B 29 PRO B 30 0 -5.42
CISPEP 6 LEU B 54B PRO B 55 0 1.04
CISPEP 7 PRO B 201 PRO B 202 0 14.42
CISPEP 8 ASP C 10 PRO C 11 0 -4.50
CISPEP 9 SER C 29 PRO C 30 0 -4.81
CISPEP 10 LEU C 54B PRO C 55 0 -0.36
CISPEP 11 PRO C 201 PRO C 202 0 10.56
CISPEP 12 ASP D 10 PRO D 11 0 -8.35
CISPEP 13 SER D 29 PRO D 30 0 0.81
CISPEP 14 LEU D 54B PRO D 55 0 3.72
CISPEP 15 PRO D 201 PRO D 202 0 17.36
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 V14 A 302
SITE 1 AC2 12 ASN A 62 GLN A 67 GLN A 92 HIS A 94
SITE 2 AC2 12 HIS A 96 GLU A 106 HIS A 119 VAL A 121
SITE 3 AC2 12 LEU A 198 THR A 199 THR A 200 ZN A 301
SITE 1 AC3 4 HIS B 94 HIS B 96 HIS B 119 V14 B 302
SITE 1 AC4 11 ASN B 62 HIS B 64 GLN B 92 HIS B 94
SITE 2 AC4 11 HIS B 96 GLU B 106 HIS B 119 VAL B 131
SITE 3 AC4 11 LEU B 198 THR B 199 ZN B 301
SITE 1 AC5 4 HIS C 94 HIS C 96 HIS C 119 V14 C 302
SITE 1 AC6 13 ASN C 62 GLN C 67 GLN C 92 HIS C 94
SITE 2 AC6 13 HIS C 96 GLU C 106 HIS C 119 VAL C 121
SITE 3 AC6 13 VAL C 131 LEU C 198 THR C 199 THR C 200
SITE 4 AC6 13 ZN C 301
SITE 1 AC7 4 HIS D 94 HIS D 96 HIS D 119 V14 D 302
SITE 1 AC8 13 ASN D 62 HIS D 64 GLN D 67 HIS D 94
SITE 2 AC8 13 HIS D 96 GLU D 106 HIS D 119 VAL D 121
SITE 3 AC8 13 VAL D 131 LEU D 198 THR D 199 THR D 200
SITE 4 AC8 13 ZN D 301
CRYST1 152.020 152.020 172.210 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 0.006578 0.003798 0.000000 0.00000
SCALE2 0.000000 0.007596 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005807 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
