HEADER LYASE/INHIBITOR 10-JUN-16 5L9E
TITLE CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A
TITLE 2 QUINOLINE OLIGOAMIDE FOLDAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II,CARBONIC ANHYDRASE C,CAC,CARBONIC
COMPND 5 ANHYDRASE II,CA-II;
COMPND 6 EC: 4.2.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS PROTEIN-FOLDAMER COMPLEX, PROTEIN FOLDAMER INTERACTIONS, MODIFIED
KEYWDS 2 INHIBITOR, ANCHORED FOLDAMER, HCAII DIMERISATION, QUINOLINE
KEYWDS 3 OLIGOAMIDE FOLDAMER, BENZENE SULFONAMIDE MODIFIED INHIBITOR, LYASE-
KEYWDS 4 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.VALLADE,B.LANGLOIS D'ESTAINTOT,T.GRANIER,I.HUC
REVDAT 4 10-JAN-24 5L9E 1 REMARK
REVDAT 3 15-NOV-23 5L9E 1 LINK ATOM
REVDAT 2 12-JUN-19 5L9E 1 AUTHOR JRNL
REVDAT 1 21-JUN-17 5L9E 0
JRNL AUTH M.VALLADE,L.FISCHER,B.LANGLOIS D'ESTAINTOT,T.GRANIER,I.HUC
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX
JRNL TITL 2 WITH A QUINOLINE OLIGOAMIDE FOLDAMER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 27248
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1397
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1834
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.3270
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.4250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7909
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 432
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.89000
REMARK 3 B22 (A**2) : -1.47000
REMARK 3 B33 (A**2) : -0.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.585
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.452
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.895
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.872
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8659 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7556 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11783 ; 1.456 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17300 ; 3.975 ; 3.006
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1027 ; 6.169 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 359 ;36.538 ;24.345
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1190 ;13.793 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;17.691 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1195 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9871 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2022 ; 0.013 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 260 B 2 260 29858 0.050 0.050
REMARK 3 2 A 4 259 C 4 259 29210 0.050 0.050
REMARK 3 3 A 4 258 D 4 258 27934 0.060 0.050
REMARK 3 4 B 4 259 C 4 259 29122 0.050 0.050
REMARK 3 5 B 4 258 D 4 258 27820 0.060 0.050
REMARK 3 6 C 4 258 D 4 258 28408 0.050 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 315
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0640 22.4560 51.5300
REMARK 3 T TENSOR
REMARK 3 T11: 0.3532 T22: 0.3937
REMARK 3 T33: 0.0126 T12: -0.0161
REMARK 3 T13: 0.0201 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 2.8288 L22: 3.4597
REMARK 3 L33: 3.3767 L12: -0.0995
REMARK 3 L13: -0.4575 L23: -0.0499
REMARK 3 S TENSOR
REMARK 3 S11: -0.0383 S12: 0.0838 S13: -0.0440
REMARK 3 S21: 0.0078 S22: -0.1516 S23: 0.0533
REMARK 3 S31: 0.0786 S32: -0.0665 S33: 0.1899
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 312
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0230 15.2470 13.4200
REMARK 3 T TENSOR
REMARK 3 T11: 0.3479 T22: 0.3575
REMARK 3 T33: 0.0574 T12: -0.0022
REMARK 3 T13: 0.1229 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 3.2647 L22: 2.6026
REMARK 3 L33: 4.1093 L12: 0.0321
REMARK 3 L13: -0.0416 L23: -0.0467
REMARK 3 S TENSOR
REMARK 3 S11: -0.0565 S12: -0.0748 S13: -0.0991
REMARK 3 S21: 0.0380 S22: -0.1299 S23: 0.0453
REMARK 3 S31: -0.0853 S32: -0.0642 S33: 0.1863
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 311
REMARK 3 ORIGIN FOR THE GROUP (A): 67.1780 -16.9640 58.4460
REMARK 3 T TENSOR
REMARK 3 T11: 0.4116 T22: 0.3963
REMARK 3 T33: 0.0378 T12: 0.0163
REMARK 3 T13: 0.1120 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 2.8435 L22: 4.7130
REMARK 3 L33: 3.4437 L12: -0.9797
REMARK 3 L13: -0.1624 L23: 0.2340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.0106 S13: -0.1103
REMARK 3 S21: -0.2764 S22: -0.0505 S23: -0.0316
REMARK 3 S31: -0.1041 S32: 0.0727 S33: 0.0487
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 311
REMARK 3 ORIGIN FOR THE GROUP (A): 74.8510 -20.5170 15.7880
REMARK 3 T TENSOR
REMARK 3 T11: 0.5664 T22: 0.4092
REMARK 3 T33: 0.0344 T12: -0.0060
REMARK 3 T13: 0.0515 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 3.0099 L22: 5.6980
REMARK 3 L33: 3.9393 L12: 1.2095
REMARK 3 L13: 0.1071 L23: 0.8463
REMARK 3 S TENSOR
REMARK 3 S11: -0.0854 S12: -0.0600 S13: 0.0569
REMARK 3 S21: 0.5384 S22: -0.0616 S23: -0.0165
REMARK 3 S31: -0.0865 S32: 0.0740 S33: 0.1470
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5L9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000375.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : KIRKPATRICK-BAEZ PAIR OF BI
REMARK 200 -MORPH MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28671
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 85.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55800
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: PHASER 2.5.7
REMARK 200 STARTING MODEL: 3KS3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ZNOAC, NACAC, PEG 8000, NAN3, PH 7.1,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.63830
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.57000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.46003
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.63830
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.57000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 69.46003
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 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 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 MET A 1
REMARK 465 MET B 1
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 HIS C 3
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 HIS D 3
REMARK 465 LYS D 260
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 LYS A 9 CG CD CE NZ
REMARK 470 HIS A 10 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 14 CD OE1 OE2
REMARK 470 LYS A 18 CE NZ
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 LYS A 80 CE NZ
REMARK 470 ASP A 85 CG OD1 OD2
REMARK 470 LYS A 111 CE NZ
REMARK 470 LYS A 132 CG CD CE NZ
REMARK 470 GLN A 135 CG CD OE1 NE2
REMARK 470 LYS A 148 CE NZ
REMARK 470 LYS A 158 CG CD CE NZ
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 LYS A 169 NZ
REMARK 470 LYS A 212 CD CE NZ
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 LEU A 223 CD1 CD2
REMARK 470 GLN A 254 CG CD OE1 NE2
REMARK 470 SER B 2 OG
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 LYS B 45 CE NZ
REMARK 470 LYS B 80 CE NZ
REMARK 470 ASP B 85 OD1 OD2
REMARK 470 LYS B 111 NZ
REMARK 470 LYS B 112 NZ
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 470 GLN B 135 CG CD OE1 NE2
REMARK 470 LYS B 148 CE NZ
REMARK 470 LYS B 158 CG CD CE NZ
REMARK 470 LYS B 167 CG CD CE NZ
REMARK 470 LYS B 212 CG CD CE NZ
REMARK 470 GLU B 220 CG CD OE1 OE2
REMARK 470 LEU B 223 CD1 CD2
REMARK 470 LYS B 251 CE NZ
REMARK 470 ASN B 252 CG OD1 ND2
REMARK 470 LYS B 260 O CG CD CE NZ
REMARK 470 LYS C 9 CG CD CE NZ
REMARK 470 HIS C 10 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 14 OE1 OE2
REMARK 470 LYS C 18 CG CD CE NZ
REMARK 470 THR C 37 OG1 CG2
REMARK 470 LYS C 39 CE NZ
REMARK 470 LYS C 45 CE NZ
REMARK 470 SER C 50 OG
REMARK 470 ARG C 58 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 74 CG CD OE1 NE2
REMARK 470 LYS C 76 CE NZ
REMARK 470 LYS C 80 CE NZ
REMARK 470 ASP C 85 OD1 OD2
REMARK 470 LYS C 111 CD CE NZ
REMARK 470 LYS C 112 CE NZ
REMARK 470 LYS C 132 CE NZ
REMARK 470 GLN C 135 CG CD OE1 NE2
REMARK 470 GLN C 136 CG CD OE1 NE2
REMARK 470 LYS C 169 NZ
REMARK 470 GLU C 186 CG CD OE1 OE2
REMARK 470 LYS C 212 CG CD CE NZ
REMARK 470 GLU C 220 CG CD OE1 OE2
REMARK 470 LEU C 223 CD1 CD2
REMARK 470 ASN C 252 CG OD1 ND2
REMARK 470 GLN C 254 CG CD OE1 NE2
REMARK 470 LYS C 260 O CG CD CE NZ
REMARK 470 HIS D 10 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 14 CG CD OE1 OE2
REMARK 470 LYS D 18 CG CD CE NZ
REMARK 470 LYS D 24 CE NZ
REMARK 470 LYS D 39 CG CD CE NZ
REMARK 470 LYS D 45 CE NZ
REMARK 470 LEU D 47 CG CD1 CD2
REMARK 470 ASP D 52 CG OD1 OD2
REMARK 470 GLN D 53 CG CD OE1 NE2
REMARK 470 ARG D 58 CG CD NE CZ NH1 NH2
REMARK 470 SER D 73 OG
REMARK 470 GLN D 74 CG CD OE1 NE2
REMARK 470 LYS D 76 CE NZ
REMARK 470 LYS D 80 CE NZ
REMARK 470 ASP D 85 CG OD1 OD2
REMARK 470 LYS D 111 CG CD CE NZ
REMARK 470 LYS D 112 CD CE NZ
REMARK 470 LYS D 126 CD CE NZ
REMARK 470 LYS D 132 CD CE NZ
REMARK 470 GLN D 135 CG CD OE1 NE2
REMARK 470 GLN D 136 CG CD OE1 NE2
REMARK 470 VAL D 149 CG1 CG2
REMARK 470 SER D 151 OG
REMARK 470 LYS D 169 CE NZ
REMARK 470 LYS D 171 NZ
REMARK 470 GLU D 186 CG CD OE1 OE2
REMARK 470 LYS D 212 CG CD CE NZ
REMARK 470 GLU D 213 CG CD OE1 OE2
REMARK 470 GLU D 220 CG CD OE1 OE2
REMARK 470 LEU D 223 CG CD1 CD2
REMARK 470 LEU D 250 CG CD1 CD2
REMARK 470 ASN D 252 CG OD1 ND2
REMARK 470 GLN D 254 CG CD OE1 NE2
REMARK 470 LYS D 256 NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 404 O HOH A 433 1.79
REMARK 500 O HOH A 425 O HOH B 418 2.10
REMARK 500 OD1 ASP A 34 O HOH A 401 2.16
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 HIS B 4 N - CA - CB ANGL. DEV. = 14.4 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 HIS A 3 -52.13 -26.82
REMARK 500 LEU A 57 -56.81 -121.89
REMARK 500 ALA A 65 -165.73 -161.19
REMARK 500 LYS A 111 -2.44 69.91
REMARK 500 LYS A 251 -137.38 62.13
REMARK 500 ASN A 252 37.53 -87.92
REMARK 500 HIS B 3 -72.92 -28.62
REMARK 500 LEU B 57 -56.85 -121.84
REMARK 500 ALA B 65 -165.88 -160.51
REMARK 500 LYS B 111 -2.54 69.90
REMARK 500 LYS B 251 -137.54 62.59
REMARK 500 ASN B 252 36.60 -87.21
REMARK 500 LEU C 57 -57.26 -122.32
REMARK 500 ALA C 65 -165.90 -160.36
REMARK 500 LYS C 111 -2.57 70.09
REMARK 500 LYS C 251 -137.88 62.71
REMARK 500 ASN C 252 36.36 -86.78
REMARK 500 LEU D 57 -57.44 -122.22
REMARK 500 ALA D 65 -165.27 -160.69
REMARK 500 LYS D 111 -3.24 70.64
REMARK 500 LYS D 251 -137.95 62.35
REMARK 500 ASN D 252 36.76 -86.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 QUJ A 303
REMARK 610 QUJ A 305
REMARK 610 QUJ B 303
REMARK 610 QUJ B 305
REMARK 610 QUJ B 312
REMARK 610 QUJ C 303
REMARK 610 QUJ C 305
REMARK 610 QUJ D 303
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 307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 4 NE2
REMARK 620 2 HIS A 64 NE2 101.2
REMARK 620 3 QVE A 306 O 97.8 160.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 17 NE2
REMARK 620 2 GLU C 26 OE2 73.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 26 OE2
REMARK 620 2 HOH A 413 O 17.6
REMARK 620 3 HOH A 417 O 16.2 1.4
REMARK 620 4 HIS C 17 NE2 16.3 2.0 1.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 310 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 34 OD1
REMARK 620 2 HIS A 36 ND1 114.3
REMARK 620 3 HOH A 401 O 65.1 80.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 312 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 ASP A 52 OD2 62.3
REMARK 620 3 HOH A 425 O 105.0 162.1
REMARK 620 4 ASP B 52 OD1 145.8 90.4 105.7
REMARK 620 5 ASP B 52 OD2 90.4 82.5 111.3 64.4
REMARK 620 6 HOH B 418 O 97.8 104.1 63.6 109.2 171.3
REMARK 620 N 1 2 3 4 5
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 106.9
REMARK 620 3 HIS A 119 ND1 110.9 94.0
REMARK 620 4 6H0 A 302 S24 102.4 142.1 97.5
REMARK 620 5 6H0 A 302 O25 89.7 162.8 75.5 31.2
REMARK 620 6 6H0 A 302 N26 117.4 110.0 114.8 33.1 64.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 174 OD1
REMARK 620 2 ASP A 174 OD2 65.9
REMARK 620 3 HOH C 428 O 124.1 89.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 311 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 186 OE1
REMARK 620 2 GLU A 186 OE2 65.3
REMARK 620 3 HOH A 404 O 81.6 107.3
REMARK 620 4 HOH A 433 O 130.3 105.7 53.3
REMARK 620 5 ASP B 189 OD1 110.2 108.7 143.7 118.5
REMARK 620 6 ASP B 189 OD2 79.5 139.8 84.8 111.9 65.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 315 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 189 OD1
REMARK 620 2 ASP A 189 OD2 63.2
REMARK 620 3 GLU B 186 OE1 105.3 79.0
REMARK 620 4 GLU B 186 OE2 102.7 135.9 64.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 316 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 233 OE2
REMARK 620 2 GLU A 233 OE2 0.0
REMARK 620 3 GLU C 233 OE1 131.9 131.9
REMARK 620 4 GLU C 233 OE2 95.2 95.2 58.7
REMARK 620 5 GLU C 233 OE1 131.9 131.9 0.0 58.7
REMARK 620 6 GLU C 233 OE2 95.2 95.2 58.7 0.0 58.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 4 NE2
REMARK 620 2 HIS B 64 NE2 98.7
REMARK 620 3 QVE B 306 O 93.5 167.7
REMARK 620 4 QVE B 306 OXT 95.6 165.3 4.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 310 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 14 OE1
REMARK 620 2 ASP C 34 OD1 4.6
REMARK 620 3 HIS C 36 ND1 2.2 2.4
REMARK 620 4 HOH C 413 O 3.8 1.8 1.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 17 NE2
REMARK 620 2 GLU D 26 OE2 51.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 26 OE1
REMARK 620 2 HOH B 415 O 81.8
REMARK 620 3 HIS D 17 NE2 78.7 4.2
REMARK 620 4 HOH D 402 O 77.8 4.3 1.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 310 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 34 OD1
REMARK 620 2 HIS B 36 ND1 123.8
REMARK 620 3 HOH B 401 O 71.2 86.6
REMARK 620 4 HOH B 424 O 111.6 122.9 125.9
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 106.5
REMARK 620 3 HIS B 119 ND1 113.9 94.6
REMARK 620 4 6H0 B 302 S24 104.2 137.3 99.4
REMARK 620 5 6H0 B 302 N26 117.6 105.8 115.0 32.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 174 OD1
REMARK 620 2 ASP B 174 OD2 65.4
REMARK 620 3 HOH B 427 O 122.0 143.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 311 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 233 OE2
REMARK 620 2 GLU D 233 OE1 75.7
REMARK 620 3 GLU D 233 OE2 74.8 1.3
REMARK 620 4 GLU D 233 OE1 75.7 0.0 1.3
REMARK 620 5 GLU D 233 OE2 74.8 1.3 0.0 1.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 308 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 428 O
REMARK 620 2 ASP D 174 OD2 154.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 4 NE2
REMARK 620 2 HIS C 64 NE2 99.6
REMARK 620 3 QVE C 306 OXT 103.6 155.6
REMARK 620 4 HOH C 401 O 111.7 67.8 96.2
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 108.6
REMARK 620 3 HIS C 119 ND1 115.0 98.5
REMARK 620 4 6H0 C 302 N26 110.3 107.0 116.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 174 OD1
REMARK 620 2 ASP C 174 OD2 65.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 306 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 4 NE2
REMARK 620 2 HIS D 64 NE2 98.8
REMARK 620 3 QVE D 305 O 102.6 158.4
REMARK 620 4 QVE D 305 OXT 108.3 152.8 7.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 309 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 34 OD1
REMARK 620 2 HOH D 425 O 110.1
REMARK 620 N 1
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 105.9
REMARK 620 3 HIS D 119 ND1 113.7 96.1
REMARK 620 4 6H0 D 302 N26 112.0 108.8 118.2
REMARK 620 5 6H0 D 302 S24 102.1 138.1 100.4 30.3
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 ZN A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 6H0 A 302 and QUJ A
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ A 303 and QVE A
REMARK 800 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QVE A 304 and QUJ A
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ A 305 and QVE A
REMARK 800 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 6H0 B 302 and QUJ B
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ B 303 and QVE B
REMARK 800 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QVE B 304 and QUJ B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ B 305 and QVE B
REMARK 800 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ B 312 and QVE D
REMARK 800 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ B 312 and QVE D
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 6H0 C 302 and QUJ C
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ C 303 and QVE C
REMARK 800 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QVE C 304 and QUJ C
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ C 305 and QVE C
REMARK 800 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 6H0 D 302 and QUJ D
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues QUJ D 303 and QVE D
REMARK 800 304
DBREF 5L9E A 1 260 UNP P00918 CAH2_HUMAN 1 260
DBREF 5L9E B 1 260 UNP P00918 CAH2_HUMAN 1 260
DBREF 5L9E C 1 260 UNP P00918 CAH2_HUMAN 1 260
DBREF 5L9E D 1 260 UNP P00918 CAH2_HUMAN 1 260
SEQRES 1 A 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 A 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 A 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 A 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 A 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 A 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 A 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 A 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 A 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 A 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 A 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 A 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 A 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 A 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 A 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 A 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 A 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 A 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 A 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
SEQRES 1 B 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 B 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 B 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 B 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 B 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 B 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 B 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 B 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 B 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 B 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 B 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 B 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 B 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 B 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 B 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 B 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 B 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 B 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 B 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 B 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
SEQRES 1 C 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 C 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 C 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 C 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 C 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 C 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 C 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 C 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 C 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 C 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 C 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 C 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 C 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 C 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 C 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 C 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 C 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 C 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 C 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 C 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
SEQRES 1 D 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 D 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 D 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 D 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 D 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 D 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 D 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 D 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 D 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 D 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 D 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 D 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 D 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 D 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 D 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 D 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 D 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 D 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 D 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 D 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET 6H0 A 302 28
HET QUJ A 303 14
HET QVE A 304 18
HET QUJ A 305 16
HET QVE A 306 19
HET ZN A 307 1
HET ZN A 308 1
HET ZN A 309 1
HET ZN A 310 1
HET ZN A 311 1
HET ZN A 312 1
HET ZN A 313 1
HET GOL A 314 6
HET ZN A 315 1
HET ZN A 316 1
HET ZN B 301 1
HET 6H0 B 302 28
HET QUJ B 303 14
HET QVE B 304 18
HET QUJ B 305 16
HET QVE B 306 19
HET ZN B 307 1
HET ZN B 308 1
HET ZN B 309 1
HET ZN B 310 1
HET GOL B 311 6
HET QUJ B 312 16
HET ZN C 301 1
HET 6H0 C 302 28
HET QUJ C 303 14
HET QVE C 304 18
HET QUJ C 305 17
HET QVE C 306 19
HET ZN C 307 1
HET ZN C 308 1
HET ZN C 309 1
HET ZN C 310 1
HET GOL C 311 6
HET ZN C 312 1
HET ZN D 301 1
HET 6H0 D 302 28
HET QUJ D 303 14
HET QVE D 304 18
HET QVE D 305 19
HET ZN D 306 1
HET ZN D 307 1
HET ZN D 308 1
HET ZN D 309 1
HET GOL D 310 6
HET ZN D 311 1
HETNAM ZN ZINC ION
HETNAM 6H0 ~{N}-[[3-(4-FORMAMIDOBUTOXY)PHENYL]METHYL]-4-SULFAMOYL-
HETNAM 2 6H0 BENZAMIDE
HETNAM QUJ 8-AZANYL-4-(2-METHYLPROPOXY)QUINOLINE-2-CARBOXYLIC ACID
HETNAM QVE 8-AZANYL-4-(2-HYDROXY-2-OXOETHYLOXY)QUINOLINE-2-
HETNAM 2 QVE CARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 ZN 27(ZN 2+)
FORMUL 6 6H0 4(C19 H23 N3 O5 S)
FORMUL 7 QUJ 8(C14 H16 N2 O3)
FORMUL 8 QVE 8(C12 H10 N2 O5)
FORMUL 18 GOL 4(C3 H8 O3)
FORMUL 56 HOH *160(H2 O)
HELIX 1 AA1 GLY A 12 ASP A 19 5 8
HELIX 2 AA2 PHE A 20 GLY A 25 5 6
HELIX 3 AA3 LYS A 126 GLY A 128 5 3
HELIX 4 AA4 ASP A 129 VAL A 134 1 6
HELIX 5 AA5 LYS A 153 GLY A 155 5 3
HELIX 6 AA6 LEU A 156 LEU A 163 1 8
HELIX 7 AA7 ASP A 164 LYS A 167 5 4
HELIX 8 AA8 ASP A 179 LEU A 184 5 6
HELIX 9 AA9 SER A 218 ARG A 226 1 9
HELIX 10 AB1 GLY B 12 ASP B 19 5 8
HELIX 11 AB2 PHE B 20 GLY B 25 5 6
HELIX 12 AB3 LYS B 126 GLY B 128 5 3
HELIX 13 AB4 ASP B 129 VAL B 134 1 6
HELIX 14 AB5 LYS B 153 GLY B 155 5 3
HELIX 15 AB6 LEU B 156 LEU B 163 1 8
HELIX 16 AB7 ASP B 164 LYS B 167 5 4
HELIX 17 AB8 ASP B 179 LEU B 184 5 6
HELIX 18 AB9 SER B 218 ARG B 226 1 9
HELIX 19 AC1 GLY C 12 ASP C 19 5 8
HELIX 20 AC2 PHE C 20 GLY C 25 5 6
HELIX 21 AC3 LYS C 126 GLY C 128 5 3
HELIX 22 AC4 ASP C 129 VAL C 134 1 6
HELIX 23 AC5 LYS C 153 GLY C 155 5 3
HELIX 24 AC6 LEU C 156 LEU C 163 1 8
HELIX 25 AC7 ASP C 164 LYS C 167 5 4
HELIX 26 AC8 ASP C 179 LEU C 184 5 6
HELIX 27 AC9 SER C 218 ARG C 226 1 9
HELIX 28 AD1 GLY D 12 ASP D 19 5 8
HELIX 29 AD2 PHE D 20 GLY D 25 5 6
HELIX 30 AD3 LYS D 126 GLY D 128 5 3
HELIX 31 AD4 ASP D 129 VAL D 134 1 6
HELIX 32 AD5 LYS D 153 GLY D 155 5 3
HELIX 33 AD6 LEU D 156 LEU D 163 1 8
HELIX 34 AD7 ASP D 164 LYS D 167 5 4
HELIX 35 AD8 ASP D 179 LEU D 184 5 6
HELIX 36 AD9 SER D 218 ARG D 226 1 9
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 AA2 6 LEU A 47 SER A 50 0
SHEET 2 AA2 6 VAL A 78 GLY A 81 -1 O LYS A 80 N SER A 48
SHEET 3 AA2 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AA2 6 ALA A 116 ASN A 124 -1 O VAL A 121 N GLN A 92
SHEET 5 AA2 6 LEU A 140 VAL A 149 -1 O ILE A 145 N LEU A 118
SHEET 6 AA2 6 ILE A 215 VAL A 217 1 O ILE A 215 N PHE A 146
SHEET 1 AA3 9 SER A 172 ASP A 174 0
SHEET 2 AA3 9 SER A 56 ASN A 61 -1 N ILE A 59 O ALA A 173
SHEET 3 AA3 9 PHE A 66 PHE A 70 -1 O GLU A 69 N LEU A 57
SHEET 4 AA3 9 TYR A 88 TRP A 97 -1 O ILE A 91 N PHE A 70
SHEET 5 AA3 9 ALA A 116 ASN A 124 -1 O VAL A 121 N GLN A 92
SHEET 6 AA3 9 LEU A 140 VAL A 149 -1 O ILE A 145 N LEU A 118
SHEET 7 AA3 9 VAL A 206 LEU A 211 1 O ILE A 209 N GLY A 144
SHEET 8 AA3 9 TYR A 190 GLY A 195 -1 N GLY A 195 O VAL A 206
SHEET 9 AA3 9 LYS A 256 ALA A 257 -1 O LYS A 256 N THR A 192
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 AA5 6 LEU B 47 SER B 50 0
SHEET 2 AA5 6 VAL B 78 GLY B 81 -1 O LYS B 80 N SER B 48
SHEET 3 AA5 6 TYR B 88 TRP B 97 -1 O TYR B 88 N LEU B 79
SHEET 4 AA5 6 ALA B 116 ASN B 124 -1 O VAL B 121 N GLN B 92
SHEET 5 AA5 6 LEU B 140 VAL B 149 -1 O ILE B 145 N LEU B 118
SHEET 6 AA5 6 ILE B 215 VAL B 217 1 O ILE B 215 N PHE B 146
SHEET 1 AA6 9 SER B 172 ASP B 174 0
SHEET 2 AA6 9 SER B 56 ASN B 61 -1 N ILE B 59 O ALA B 173
SHEET 3 AA6 9 PHE B 66 PHE B 70 -1 O GLU B 69 N LEU B 57
SHEET 4 AA6 9 TYR B 88 TRP B 97 -1 O ILE B 91 N PHE B 70
SHEET 5 AA6 9 ALA B 116 ASN B 124 -1 O VAL B 121 N GLN B 92
SHEET 6 AA6 9 LEU B 140 VAL B 149 -1 O ILE B 145 N LEU B 118
SHEET 7 AA6 9 VAL B 206 LEU B 211 1 O ILE B 209 N GLY B 144
SHEET 8 AA6 9 TYR B 190 GLY B 195 -1 N GLY B 195 O VAL B 206
SHEET 9 AA6 9 LYS B 256 ALA B 257 -1 O LYS B 256 N THR B 192
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 AA8 6 LEU C 47 SER C 50 0
SHEET 2 AA8 6 VAL C 78 GLY C 81 -1 O LYS C 80 N SER C 48
SHEET 3 AA8 6 TYR C 88 TRP C 97 -1 O TYR C 88 N LEU C 79
SHEET 4 AA8 6 ALA C 116 ASN C 124 -1 O VAL C 121 N GLN C 92
SHEET 5 AA8 6 LEU C 140 VAL C 149 -1 O ILE C 145 N LEU C 118
SHEET 6 AA8 6 ILE C 215 VAL C 217 1 O ILE C 215 N PHE C 146
SHEET 1 AA9 9 SER C 172 ASP C 174 0
SHEET 2 AA9 9 SER C 56 ASN C 61 -1 N ILE C 59 O ALA C 173
SHEET 3 AA9 9 PHE C 66 PHE C 70 -1 O GLU C 69 N LEU C 57
SHEET 4 AA9 9 TYR C 88 TRP C 97 -1 O ILE C 91 N PHE C 70
SHEET 5 AA9 9 ALA C 116 ASN C 124 -1 O VAL C 121 N GLN C 92
SHEET 6 AA9 9 LEU C 140 VAL C 149 -1 O ILE C 145 N LEU C 118
SHEET 7 AA9 9 VAL C 206 LEU C 211 1 O ILE C 209 N GLY C 144
SHEET 8 AA9 9 TYR C 190 GLY C 195 -1 N GLY C 195 O VAL C 206
SHEET 9 AA9 9 LYS C 256 ALA C 257 -1 O LYS C 256 N THR C 192
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 AB2 6 LEU D 47 SER D 50 0
SHEET 2 AB2 6 VAL D 78 GLY D 81 -1 O LYS D 80 N SER D 48
SHEET 3 AB2 6 TYR D 88 TRP D 97 -1 O TYR D 88 N LEU D 79
SHEET 4 AB2 6 ALA D 116 ASN D 124 -1 O VAL D 121 N GLN D 92
SHEET 5 AB2 6 LEU D 140 VAL D 149 -1 O ILE D 145 N LEU D 118
SHEET 6 AB2 6 ILE D 215 VAL D 217 1 O ILE D 215 N PHE D 146
SHEET 1 AB3 9 SER D 172 ASP D 174 0
SHEET 2 AB3 9 SER D 56 ASN D 61 -1 N ILE D 59 O ALA D 173
SHEET 3 AB3 9 PHE D 66 PHE D 70 -1 O GLU D 69 N LEU D 57
SHEET 4 AB3 9 TYR D 88 TRP D 97 -1 O ILE D 91 N PHE D 70
SHEET 5 AB3 9 ALA D 116 ASN D 124 -1 O VAL D 121 N GLN D 92
SHEET 6 AB3 9 LEU D 140 VAL D 149 -1 O ILE D 145 N LEU D 118
SHEET 7 AB3 9 VAL D 206 LEU D 211 1 O ILE D 209 N GLY D 144
SHEET 8 AB3 9 TYR D 190 GLY D 195 -1 N GLY D 195 O VAL D 206
SHEET 9 AB3 9 LYS D 256 ALA D 257 -1 O LYS D 256 N THR D 192
LINK C2 6H0 A 302 N QUJ A 303 1555 1555 1.34
LINK C QUJ A 303 N QVE A 304 1555 1555 1.35
LINK C QVE A 304 N QUJ A 305 1555 1555 1.35
LINK C QUJ A 305 N QVE A 306 1555 1555 1.35
LINK C2 6H0 B 302 N QUJ B 303 1555 1555 1.35
LINK C QUJ B 303 N QVE B 304 1555 1555 1.35
LINK C QVE B 304 N QUJ B 305 1555 1555 1.34
LINK C QUJ B 305 N QVE B 306 1555 1555 1.34
LINK N QUJ B 312 C QVE D 304 1555 1555 1.34
LINK C QUJ B 312 N QVE D 305 1555 1555 1.35
LINK C2 6H0 C 302 N QUJ C 303 1555 1555 1.34
LINK C QUJ C 303 N QVE C 304 1555 1555 1.35
LINK C QVE C 304 N QUJ C 305 1555 1555 1.35
LINK C QUJ C 305 N QVE C 306 1555 1555 1.35
LINK C2 6H0 D 302 N QUJ D 303 1555 1555 1.35
LINK C QUJ D 303 N QVE D 304 1555 1555 1.36
LINK NE2 HIS A 4 ZN ZN A 307 1555 1555 2.13
LINK NE2 HIS A 17 ZN ZN A 308 1555 1555 1.98
LINK OE2 GLU A 26 ZN ZN C 308 1555 2666 1.89
LINK OD1 ASP A 34 ZN ZN A 310 1555 1555 2.01
LINK ND1 HIS A 36 ZN ZN A 310 1555 1555 2.28
LINK OD1 ASP A 52 ZN ZN A 312 1555 1555 2.14
LINK OD2 ASP A 52 ZN ZN A 312 1555 1555 2.04
LINK NE2 HIS A 64 ZN ZN A 307 1555 1555 2.02
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 1.97
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 1.99
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.24
LINK OD1 ASP A 174 ZN ZN A 309 1555 1555 2.02
LINK OD2 ASP A 174 ZN ZN A 309 1555 1555 2.01
LINK OE1 GLU A 186 ZN ZN A 311 1555 1555 2.02
LINK OE2 GLU A 186 ZN ZN A 311 1555 1555 1.98
LINK OD1 ASP A 189 ZN ZN A 315 1555 1555 2.06
LINK OD2 ASP A 189 ZN ZN A 315 1555 1555 2.04
LINK OE2 GLU A 233 ZN ZN A 316 1555 1555 1.98
LINK OE2 GLU A 233 ZN ZN A 316 1555 2656 2.04
LINK ZN ZN A 301 S24 6H0 A 302 1555 1555 2.90
LINK ZN ZN A 301 O25 6H0 A 302 1555 1555 2.65
LINK ZN ZN A 301 N26 6H0 A 302 1555 1555 2.07
LINK O QVE A 306 ZN ZN A 307 1555 2656 2.32
LINK ZN ZN A 308 OE2 GLU C 26 2646 1555 1.99
LINK ZN ZN A 309 O HOH C 428 1555 1555 2.49
LINK ZN ZN A 310 O HOH A 401 1555 1555 1.99
LINK ZN ZN A 311 O HOH A 404 1555 1555 1.99
LINK ZN ZN A 311 O HOH A 433 1555 1555 1.99
LINK ZN ZN A 311 OD1 ASP B 189 1555 1555 2.04
LINK ZN ZN A 311 OD2 ASP B 189 1555 1555 2.00
LINK ZN ZN A 312 O HOH A 425 1555 1555 1.99
LINK ZN ZN A 312 OD1 ASP B 52 1555 1555 2.02
LINK ZN ZN A 312 OD2 ASP B 52 1555 1555 2.03
LINK ZN ZN A 312 O HOH B 418 1555 1555 1.99
LINK ZN ZN A 315 OE1 GLU B 186 1555 1555 2.02
LINK ZN ZN A 315 OE2 GLU B 186 1555 1555 2.00
LINK ZN ZN A 316 OE1 GLU C 233 1555 1555 2.38
LINK ZN ZN A 316 OE2 GLU C 233 1555 1555 2.00
LINK ZN ZN A 316 OE1 GLU C 233 2656 1555 2.60
LINK ZN ZN A 316 OE2 GLU C 233 2656 1555 2.47
LINK O HOH A 413 ZN ZN C 308 2646 1555 2.00
LINK O HOH A 417 ZN ZN C 308 2646 1555 1.99
LINK NE2 HIS B 4 ZN ZN B 307 1555 1555 2.24
LINK OE1 GLU B 14 ZN ZN C 310 1555 3454 2.06
LINK NE2 HIS B 17 ZN ZN B 308 1555 1555 2.08
LINK OE1 GLU B 26 ZN ZN D 307 1555 2655 1.99
LINK OD1 ASP B 34 ZN ZN B 310 1555 1555 2.00
LINK ND1 HIS B 36 ZN ZN B 310 1555 1555 2.16
LINK NE2 HIS B 64 ZN ZN B 307 1555 1555 1.95
LINK NE2 HIS B 94 ZN ZN B 301 1555 1555 1.94
LINK NE2 HIS B 96 ZN ZN B 301 1555 1555 2.03
LINK ND1 HIS B 119 ZN ZN B 301 1555 1555 2.16
LINK OD1 ASP B 174 ZN ZN B 309 1555 1555 2.01
LINK OD2 ASP B 174 ZN ZN B 309 1555 1555 2.01
LINK OE2 GLU B 233 ZN ZN D 311 1555 1565 1.88
LINK ZN ZN B 301 S24 6H0 B 302 1555 1555 2.95
LINK ZN ZN B 301 N26 6H0 B 302 1555 1555 2.07
LINK O QVE B 306 ZN ZN B 307 1555 2655 2.43
LINK OXT QVE B 306 ZN ZN B 307 1555 2655 2.65
LINK ZN ZN B 308 OE2 GLU D 26 2655 1555 1.91
LINK ZN ZN B 309 O HOH B 427 1555 1555 1.99
LINK ZN ZN B 310 O HOH B 401 1555 1555 1.99
LINK ZN ZN B 310 O HOH B 424 1555 1555 1.99
LINK O HOH B 415 ZN ZN D 307 2655 1555 2.00
LINK O HOH B 428 ZN ZN D 308 1545 1555 1.98
LINK NE2 HIS C 4 ZN ZN C 307 1555 1555 2.09
LINK NE2 HIS C 17 ZN ZN C 308 1555 1555 1.94
LINK OD1 ASP C 34 ZN ZN C 310 1555 1555 2.00
LINK ND1 HIS C 36 ZN ZN C 310 1555 1555 2.13
LINK NE2 HIS C 64 ZN ZN C 307 1555 1555 2.16
LINK NE2 HIS C 94 ZN ZN C 301 1555 1555 1.93
LINK NE2 HIS C 96 ZN ZN C 301 1555 1555 1.96
LINK ND1 HIS C 119 ZN ZN C 301 1555 1555 2.13
LINK OD1 ASP C 174 ZN ZN C 309 1555 1555 2.02
LINK OD2 ASP C 174 ZN ZN C 309 1555 1555 1.99
LINK ZN ZN C 301 N26 6H0 C 302 1555 1555 2.06
LINK OXT QVE C 306 ZN ZN C 307 1555 2656 2.15
LINK ZN ZN C 307 O HOH C 401 1555 1555 1.99
LINK ZN ZN C 310 O HOH C 413 1555 1555 1.99
LINK ZN ZN C 312 O HOH C 403 1555 1555 2.25
LINK NE2 HIS D 4 ZN ZN D 306 1555 1555 2.18
LINK NE2 HIS D 17 ZN ZN D 307 1555 1555 1.94
LINK OD1 ASP D 34 ZN ZN D 309 1555 1555 2.01
LINK NE2 HIS D 64 ZN ZN D 306 1555 1555 2.09
LINK NE2 HIS D 94 ZN ZN D 301 1555 1555 1.96
LINK NE2 HIS D 96 ZN ZN D 301 1555 1555 2.00
LINK ND1 HIS D 119 ZN ZN D 301 1555 1555 2.14
LINK OD2 ASP D 174 ZN ZN D 308 1555 1555 2.00
LINK OE1 GLU D 233 ZN ZN D 311 1555 1555 2.29
LINK OE2 GLU D 233 ZN ZN D 311 1555 1555 1.99
LINK OE1 GLU D 233 ZN ZN D 311 1555 2655 2.44
LINK OE2 GLU D 233 ZN ZN D 311 1555 2655 2.50
LINK ZN ZN D 301 N26 6H0 D 302 1555 1555 2.05
LINK ZN ZN D 301 S24 6H0 D 302 1555 1555 3.00
LINK O QVE D 305 ZN ZN D 306 1555 2655 2.08
LINK OXT QVE D 305 ZN ZN D 306 1555 2655 2.50
LINK ZN ZN D 307 O HOH D 402 1555 1555 2.00
LINK ZN ZN D 309 O HOH D 425 1555 1555 2.37
CISPEP 1 SER A 29 PRO A 30 0 2.05
CISPEP 2 PRO A 200 PRO A 201 0 12.96
CISPEP 3 SER B 29 PRO B 30 0 4.97
CISPEP 4 PRO B 200 PRO B 201 0 11.64
CISPEP 5 SER C 29 PRO C 30 0 3.35
CISPEP 6 PRO C 200 PRO C 201 0 11.76
CISPEP 7 SER D 29 PRO D 30 0 1.96
CISPEP 8 PRO D 200 PRO D 201 0 8.65
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 6H0 A 302
SITE 1 AC2 4 HIS A 4 HIS A 64 QVE A 304 QVE A 306
SITE 1 AC3 2 HIS A 17 GLU C 26
SITE 1 AC4 3 ASP A 174 HOH A 443 HOH C 428
SITE 1 AC5 3 ASP A 34 HIS A 36 HOH A 401
SITE 1 AC6 4 GLU A 186 HOH A 404 HOH A 433 ASP B 189
SITE 1 AC7 4 ASP A 52 HOH A 425 ASP B 52 HOH B 418
SITE 1 AC8 1 HIS A 15
SITE 1 AC9 6 ASN A 62 ALA A 65 ASN A 67 GLN A 92
SITE 2 AC9 6 6H0 A 302 HOH A 406
SITE 1 AD1 3 ASP A 189 LYS A 260 GLU B 186
SITE 1 AD2 3 GLU A 233 LYS C 171 GLU C 233
SITE 1 AD3 4 HIS B 94 HIS B 96 HIS B 119 6H0 B 302
SITE 1 AD4 4 HIS B 4 HIS B 64 QVE B 304 QVE B 306
SITE 1 AD5 3 HIS B 17 LYS B 18 GLU D 26
SITE 1 AD6 2 ASP B 174 HOH B 427
SITE 1 AD7 4 ASP B 34 HIS B 36 HOH B 401 HOH B 424
SITE 1 AD8 5 ASN B 62 ALA B 65 ASN B 67 GLN B 92
SITE 2 AD8 5 6H0 B 302
SITE 1 AD9 4 HIS C 94 HIS C 96 HIS C 119 6H0 C 302
SITE 1 AE1 5 HIS C 4 HIS C 64 QVE C 304 QVE C 306
SITE 2 AE1 5 HOH C 401
SITE 1 AE2 4 GLU A 26 HOH A 413 HOH A 417 HIS C 17
SITE 1 AE3 2 ASP C 174 HOH C 427
SITE 1 AE4 4 GLU B 14 ASP C 34 HIS C 36 HOH C 413
SITE 1 AE5 4 ASN C 62 ASN C 67 HIS C 94 THR C 199
SITE 1 AE6 3 HIS B 10 HIS C 36 HOH C 403
SITE 1 AE7 4 HIS D 94 HIS D 96 HIS D 119 6H0 D 302
SITE 1 AE8 4 HIS D 4 HIS D 64 QVE D 304 QVE D 305
SITE 1 AE9 4 GLU B 26 HOH B 415 HIS D 17 HOH D 402
SITE 1 AF1 2 HOH B 428 ASP D 174
SITE 1 AF2 3 ASP D 34 HIS D 36 HOH D 425
SITE 1 AF3 5 ASN D 62 ALA D 65 ASN D 67 GLN D 92
SITE 2 AF3 5 6H0 D 302
SITE 1 AF4 2 GLU B 233 GLU D 233
SITE 1 AF5 13 HIS A 94 HIS A 96 HIS A 119 PHE A 130
SITE 2 AF5 13 LEU A 197 THR A 198 THR A 199 TRP A 208
SITE 3 AF5 13 ZN A 301 QVE A 304 QUJ A 305 QVE A 306
SITE 4 AF5 13 GOL A 314
SITE 1 AF6 6 HIS A 4 LYS A 169 6H0 A 302 QUJ A 305
SITE 2 AF6 6 QVE A 306 ZN A 307
SITE 1 AF7 10 HIS A 4 ASP A 19 PHE A 20 LYS A 169
SITE 2 AF7 10 PRO A 201 6H0 A 302 QUJ A 303 QVE A 306
SITE 3 AF7 10 ZN A 307 HOH A 419
SITE 1 AF8 11 HIS A 4 TRP A 5 ASP A 19 PHE A 20
SITE 2 AF8 11 HIS A 64 PRO A 201 6H0 A 302 QUJ A 303
SITE 3 AF8 11 QVE A 304 ZN A 307 HOH A 419
SITE 1 AF9 14 HIS B 94 HIS B 96 HIS B 119 PHE B 130
SITE 2 AF9 14 LEU B 197 THR B 198 THR B 199 TRP B 208
SITE 3 AF9 14 ZN B 301 QVE B 304 QUJ B 305 QVE B 306
SITE 4 AF9 14 GOL B 311 HOH B 421
SITE 1 AG1 5 HIS B 4 6H0 B 302 QUJ B 305 QVE B 306
SITE 2 AG1 5 ZN B 307
SITE 1 AG2 8 HIS B 4 ASP B 19 PHE B 20 6H0 B 302
SITE 2 AG2 8 QUJ B 303 QVE B 306 ZN B 307 HOH B 414
SITE 1 AG3 11 HIS B 4 TRP B 5 ASP B 19 PHE B 20
SITE 2 AG3 11 HIS B 64 PRO B 201 6H0 B 302 QUJ B 303
SITE 3 AG3 11 QVE B 304 ZN B 307 HOH B 414
SITE 1 AG4 13 HIS B 4 QUJ B 303 QUJ B 305 QVE B 306
SITE 2 AG4 13 ZN B 307 HIS D 4 ASP D 19 PHE D 20
SITE 3 AG4 13 LYS D 169 6H0 D 302 QUJ D 303 QVE D 305
SITE 4 AG4 13 ZN D 306
SITE 1 AG5 16 ASP B 19 PHE B 20 6H0 B 302 QUJ B 303
SITE 2 AG5 16 QVE B 304 QVE B 306 HOH B 414 HIS D 4
SITE 3 AG5 16 TRP D 5 ASP D 19 PHE D 20 HIS D 64
SITE 4 AG5 16 6H0 D 302 QUJ D 303 QVE D 304 ZN D 306
SITE 1 AG6 13 GLN C 92 HIS C 94 HIS C 96 HIS C 119
SITE 2 AG6 13 PHE C 130 LEU C 197 THR C 198 THR C 199
SITE 3 AG6 13 TRP C 208 ZN C 301 QVE C 304 QUJ C 305
SITE 4 AG6 13 QVE C 306
SITE 1 AG7 7 HIS C 4 LYS C 169 6H0 C 302 QUJ C 305
SITE 2 AG7 7 QVE C 306 ZN C 307 HOH C 401
SITE 1 AG8 9 HIS C 4 ASP C 19 PHE C 20 LYS C 169
SITE 2 AG8 9 6H0 C 302 QUJ C 303 QVE C 306 ZN C 307
SITE 3 AG8 9 HOH C 401
SITE 1 AG9 9 HIS C 4 TRP C 5 ASP C 19 PHE C 20
SITE 2 AG9 9 HIS C 64 6H0 C 302 QUJ C 303 QVE C 304
SITE 3 AG9 9 ZN C 307
SITE 1 AH1 15 QUJ B 312 GLN D 92 HIS D 94 HIS D 96
SITE 2 AH1 15 HIS D 119 PHE D 130 LEU D 197 THR D 198
SITE 3 AH1 15 THR D 199 TRP D 208 ZN D 301 QVE D 304
SITE 4 AH1 15 QVE D 305 GOL D 310 HOH D 406
SITE 1 AH2 6 QUJ B 312 HIS D 4 LYS D 169 6H0 D 302
SITE 2 AH2 6 QVE D 305 ZN D 306
CRYST1 125.972 75.140 141.098 90.00 100.08 90.00 I 1 2 1 16
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 0.007938 0.000000 0.001411 0.00000
SCALE2 0.000000 0.013308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
