HEADER LYASE 28-JUL-16 5LLP
TITLE CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE ISOZYME XII WITH 3-
TITLE 2 [(1S)-1,2,3,4-TETRAHYDRONAPTHALEN-1-YLAMINO)-2,5,6-TRIFLUORO-4-[(2-
TITLE 3 HYDROXYETHYL)SULFONYL]BENZENESULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 12;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: HUMAN CARBONIC ANHYDRASE XII;
COMPND 5 SYNONYM: CARBONATE DEHYDRATASE XII,CARBONIC ANHYDRASE XII,CA-XII,
COMPND 6 TUMOR ANTIGEN HOM-RCC-3.1.3;
COMPND 7 EC: 4.2.1.1;
COMPND 8 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: CA12;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS DRUG DESIGN, CARBONIC ANHYDRASE, BENZENESULFONAMIDE, METAL-BINDING,
KEYWDS 2 LYASE-LYASE INHIBITOR COMPLE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SMIRNOV,E.MANAKOVA,S.GRAZULIS
REVDAT 5 10-JAN-24 5LLP 1 REMARK LINK
REVDAT 4 16-MAY-18 5LLP 1 JRNL
REVDAT 3 29-NOV-17 5LLP 1 REMARK
REVDAT 2 22-NOV-17 5LLP 1 TITLE JRNL
REVDAT 1 16-AUG-17 5LLP 0
JRNL AUTH A.SMIRNOV,A.ZUBRIENE,E.MANAKOVA,S.GRAZULIS,D.MATULIS
JRNL TITL CRYSTAL STRUCTURE CORRELATIONS WITH THE INTRINSIC
JRNL TITL 2 THERMODYNAMICS OF HUMAN CARBONIC ANHYDRASE INHIBITOR
JRNL TITL 3 BINDING.
JRNL REF PEERJ V. 6 E4412 2018
JRNL REFN ESSN 2167-8359
JRNL PMID 29503769
JRNL DOI 10.7717/PEERJ.4412
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 144263
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 15901
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) : 1.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10373
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.1800
REMARK 3 BIN FREE R VALUE SET COUNT : 1171
REMARK 3 BIN FREE R VALUE : 0.2330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8362
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 1184
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
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 : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9062 ; 0.024 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12409 ; 2.339 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1098 ; 7.487 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 450 ;37.214 ;24.578
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1409 ;13.348 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;15.036 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1285 ; 0.160 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7192 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5LLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000962.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.826606
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 160218
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 73.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1JD0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION BUFFER: 0.1M AMMONIUM
REMARK 280 CITRATE (PH 7), 0.2M AMMONIUM SULFATE AND 26% PEG4000, PH 7.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 37.14400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 SER A 2
REMARK 465 GLN A 263
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 263
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 263
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 NZ LYS B 166 O HOH B 401 1.77
REMARK 500 OD1 ASP D 75 O HOH D 401 1.98
REMARK 500 O HOH B 590 O HOH B 624 2.06
REMARK 500 O HOH D 425 O HOH D 673 2.08
REMARK 500 O HOH D 610 O HOH D 659 2.08
REMARK 500 CD ARG D 255 O HOH D 537 2.08
REMARK 500 O HOH B 490 O HOH B 644 2.09
REMARK 500 O HOH D 597 O HOH D 644 2.12
REMARK 500 OD2 ASP B 253 O HOH B 402 2.19
REMARK 500 OD1 ASN A 134 O HOH A 401 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 642 O HOH B 641 1655 2.00
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 HIS A 33 CG HIS A 33 CD2 0.060
REMARK 500 HIS B 161 CG HIS B 161 CD2 0.055
REMARK 500 HIS B 164 CG HIS B 164 CD2 0.063
REMARK 500 ARG B 255 CZ ARG B 255 NH2 0.078
REMARK 500 HIS C 101 CG HIS C 101 CD2 0.059
REMARK 500 HIS C 117 CG HIS C 117 CD2 0.067
REMARK 500 HIS D 91 CG HIS D 91 CD2 0.057
REMARK 500 HIS D 117 CG HIS D 117 CD2 0.069
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 ASP D 253 CB - CG - OD1 ANGL. DEV. = 6.8 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 ASN A 245 56.15 -93.26
REMARK 500 ASP B 99 79.99 -157.16
REMARK 500 GLN B 163 -7.46 -59.01
REMARK 500 SER B 238 77.87 -119.26
REMARK 500 ASN B 245 59.38 -92.70
REMARK 500 GLU B 254 -37.07 73.77
REMARK 500 GLU B 254 -42.58 73.77
REMARK 500 ASN C 245 58.57 -95.02
REMARK 500 ASP D 99 80.84 -151.93
REMARK 500 SER D 238 75.92 -119.87
REMARK 500 ASN D 245 56.97 -95.55
REMARK 500 PHE D 252 73.36 -102.96
REMARK 500 ASP D 253 55.02 -23.95
REMARK 500 GLU D 254 -19.80 81.41
REMARK 500 GLU D 254 -46.50 81.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE D 252 ASP D 253 -97.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 691 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 692 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH B 706 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 707 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH C 668 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH C 669 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH D 716 DISTANCE = 5.95 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 91 NE2
REMARK 620 2 HIS A 93 NE2 103.2
REMARK 620 3 HIS A 117 ND1 108.7 99.5
REMARK 620 4 6Z9 A 302 S2 94.1 139.3 109.5
REMARK 620 5 6Z9 A 302 N29 121.3 114.5 107.4 29.9
REMARK 620 6 6Z9 A 302 N29 121.8 114.4 107.0 30.2 0.5
REMARK 620 N 1 2 3 4 5
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 91 NE2
REMARK 620 2 HIS B 93 NE2 104.3
REMARK 620 3 HIS B 117 ND1 110.9 99.8
REMARK 620 4 6Z9 B 302 N29 118.8 113.4 108.0
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 91 NE2
REMARK 620 2 HIS C 93 NE2 101.3
REMARK 620 3 HIS C 117 ND1 113.5 98.9
REMARK 620 4 6Z9 C 302 N29 117.6 115.3 108.6
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 91 NE2
REMARK 620 2 HIS D 93 NE2 104.0
REMARK 620 3 HIS D 117 ND1 110.9 99.5
REMARK 620 4 6Z9 D 302 N29 118.5 114.3 108.1
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 6Z9 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 6Z9 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 6Z9 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 6Z9 D 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5LLC RELATED DB: PDB
REMARK 900 RELATED ID: 5LLE RELATED DB: PDB
REMARK 900 RELATED ID: 5LLG RELATED DB: PDB
REMARK 900 RELATED ID: 5LLH RELATED DB: PDB
REMARK 900 RELATED ID: 5LLN RELATED DB: PDB
REMARK 900 RELATED ID: 5LLO RELATED DB: PDB
DBREF 5LLP A 2 263 UNP O43570 CAH12_HUMAN 30 291
DBREF 5LLP B 2 263 UNP O43570 CAH12_HUMAN 30 291
DBREF 5LLP C 2 263 UNP O43570 CAH12_HUMAN 30 291
DBREF 5LLP D 2 263 UNP O43570 CAH12_HUMAN 30 291
SEQADV 5LLP MET A 1 UNP O43570 INITIATING METHIONINE
SEQADV 5LLP MET B 1 UNP O43570 INITIATING METHIONINE
SEQADV 5LLP MET C 1 UNP O43570 INITIATING METHIONINE
SEQADV 5LLP MET D 1 UNP O43570 INITIATING METHIONINE
SEQRES 1 A 263 MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN
SEQRES 2 A 263 SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU
SEQRES 3 A 263 GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR
SEQRES 4 A 263 ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN
SEQRES 5 A 263 LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY
SEQRES 6 A 263 HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE
SEQRES 7 A 263 GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS
SEQRES 8 A 263 LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU
SEQRES 9 A 263 HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS
SEQRES 10 A 263 ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER
SEQRES 11 A 263 THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA
SEQRES 12 A 263 VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP
SEQRES 13 A 263 LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY
SEQRES 14 A 263 GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU
SEQRES 15 A 263 LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY
SEQRES 16 A 263 SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP
SEQRES 17 A 263 THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN
SEQRES 18 A 263 LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET
SEQRES 19 A 263 ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG
SEQRES 20 A 263 GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER
SEQRES 21 A 263 PHE SER GLN
SEQRES 1 B 263 MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN
SEQRES 2 B 263 SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU
SEQRES 3 B 263 GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR
SEQRES 4 B 263 ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN
SEQRES 5 B 263 LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY
SEQRES 6 B 263 HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE
SEQRES 7 B 263 GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS
SEQRES 8 B 263 LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU
SEQRES 9 B 263 HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS
SEQRES 10 B 263 ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER
SEQRES 11 B 263 THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA
SEQRES 12 B 263 VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP
SEQRES 13 B 263 LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY
SEQRES 14 B 263 GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU
SEQRES 15 B 263 LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY
SEQRES 16 B 263 SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP
SEQRES 17 B 263 THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN
SEQRES 18 B 263 LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET
SEQRES 19 B 263 ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG
SEQRES 20 B 263 GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER
SEQRES 21 B 263 PHE SER GLN
SEQRES 1 C 263 MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN
SEQRES 2 C 263 SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU
SEQRES 3 C 263 GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR
SEQRES 4 C 263 ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN
SEQRES 5 C 263 LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY
SEQRES 6 C 263 HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE
SEQRES 7 C 263 GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS
SEQRES 8 C 263 LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU
SEQRES 9 C 263 HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS
SEQRES 10 C 263 ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER
SEQRES 11 C 263 THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA
SEQRES 12 C 263 VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP
SEQRES 13 C 263 LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY
SEQRES 14 C 263 GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU
SEQRES 15 C 263 LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY
SEQRES 16 C 263 SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP
SEQRES 17 C 263 THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN
SEQRES 18 C 263 LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET
SEQRES 19 C 263 ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG
SEQRES 20 C 263 GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER
SEQRES 21 C 263 PHE SER GLN
SEQRES 1 D 263 MET SER LYS TRP THR TYR PHE GLY PRO ASP GLY GLU ASN
SEQRES 2 D 263 SER TRP SER LYS LYS TYR PRO SER CYS GLY GLY LEU LEU
SEQRES 3 D 263 GLN SER PRO ILE ASP LEU HIS SER ASP ILE LEU GLN TYR
SEQRES 4 D 263 ASP ALA SER LEU THR PRO LEU GLU PHE GLN GLY TYR ASN
SEQRES 5 D 263 LEU SER ALA ASN LYS GLN PHE LEU LEU THR ASN ASN GLY
SEQRES 6 D 263 HIS SER VAL LYS LEU ASN LEU PRO SER ASP MET HIS ILE
SEQRES 7 D 263 GLN GLY LEU GLN SER ARG TYR SER ALA THR GLN LEU HIS
SEQRES 8 D 263 LEU HIS TRP GLY ASN PRO ASN ASP PRO HIS GLY SER GLU
SEQRES 9 D 263 HIS THR VAL SER GLY GLN HIS PHE ALA ALA GLU LEU HIS
SEQRES 10 D 263 ILE VAL HIS TYR ASN SER ASP LEU TYR PRO ASP ALA SER
SEQRES 11 D 263 THR ALA SER ASN LYS SER GLU GLY LEU ALA VAL LEU ALA
SEQRES 12 D 263 VAL LEU ILE GLU MET GLY SER PHE ASN PRO SER TYR ASP
SEQRES 13 D 263 LYS ILE PHE SER HIS LEU GLN HIS VAL LYS TYR LYS GLY
SEQRES 14 D 263 GLN GLU ALA PHE VAL PRO GLY PHE ASN ILE GLU GLU LEU
SEQRES 15 D 263 LEU PRO GLU ARG THR ALA GLU TYR TYR ARG TYR ARG GLY
SEQRES 16 D 263 SER LEU THR THR PRO PRO CYS ASN PRO THR VAL LEU TRP
SEQRES 17 D 263 THR VAL PHE ARG ASN PRO VAL GLN ILE SER GLN GLU GLN
SEQRES 18 D 263 LEU LEU ALA LEU GLU THR ALA LEU TYR CYS THR HIS MET
SEQRES 19 D 263 ASP ASP PRO SER PRO ARG GLU MET ILE ASN ASN PHE ARG
SEQRES 20 D 263 GLN VAL GLN LYS PHE ASP GLU ARG LEU VAL TYR THR SER
SEQRES 21 D 263 PHE SER GLN
HET ZN A 301 1
HET 6Z9 A 302 60
HET ZN B 301 1
HET 6Z9 B 302 30
HET ZN C 301 1
HET 6Z9 C 302 30
HET ZN D 301 1
HET 6Z9 D 302 30
HETNAM ZN ZINC ION
HETNAM 6Z9 3-[(1S)-1,2,3,4-TETRAHYDRONAPTHALEN-1-YLAMINO)-2,5,6-
HETNAM 2 6Z9 TRIFLUORO-4-[(2-HYDROXYETHYL)
HETNAM 3 6Z9 SULFONYL]BENZENESULFONAMIDE
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 6Z9 4(C18 H19 F3 N2 O5 S2)
FORMUL 13 HOH *1184(H2 O)
HELIX 1 AA1 PHE A 7 TRP A 15 5 9
HELIX 2 AA2 TYR A 19 GLY A 24 5 6
HELIX 3 AA3 HIS A 33 ASP A 35 5 3
HELIX 4 AA4 ASP A 128 ASN A 134 1 7
HELIX 5 AA5 ASN A 152 SER A 160 1 9
HELIX 6 AA6 HIS A 161 LYS A 166 5 6
HELIX 7 AA7 ASN A 178 LEU A 183 5 6
HELIX 8 AA8 SER A 218 ALA A 228 1 11
HELIX 9 AA9 GLY B 11 LYS B 18 5 8
HELIX 10 AB1 TYR B 19 GLY B 24 5 6
HELIX 11 AB2 HIS B 33 ASP B 35 5 3
HELIX 12 AB3 ASP B 128 SER B 133 1 6
HELIX 13 AB4 ASN B 152 SER B 160 1 9
HELIX 14 AB5 HIS B 161 VAL B 165 5 5
HELIX 15 AB6 ASN B 178 LEU B 183 5 6
HELIX 16 AB7 SER B 218 ALA B 228 1 11
HELIX 17 AB8 PHE C 7 GLY C 11 5 5
HELIX 18 AB9 SER C 14 LYS C 18 5 5
HELIX 19 AC1 TYR C 19 GLY C 24 5 6
HELIX 20 AC2 HIS C 33 ASP C 35 5 3
HELIX 21 AC3 ASP C 128 SER C 133 1 6
HELIX 22 AC4 ASN C 152 SER C 160 1 9
HELIX 23 AC5 HIS C 161 VAL C 165 5 5
HELIX 24 AC6 ASN C 178 LEU C 183 5 6
HELIX 25 AC7 SER C 218 LEU C 229 1 12
HELIX 26 AC8 GLY D 11 LYS D 18 5 8
HELIX 27 AC9 TYR D 19 GLY D 24 5 6
HELIX 28 AD1 HIS D 33 ASP D 35 5 3
HELIX 29 AD2 ASP D 128 SER D 133 1 6
HELIX 30 AD3 ASN D 152 SER D 160 1 9
HELIX 31 AD4 HIS D 161 LYS D 166 5 6
HELIX 32 AD5 ASN D 178 LEU D 183 5 6
HELIX 33 AD6 SER D 218 ALA D 228 1 11
SHEET 1 AA1 2 ASP A 31 LEU A 32 0
SHEET 2 AA1 2 THR A 106 VAL A 107 1 O THR A 106 N LEU A 32
SHEET 1 AA210 LEU A 37 TYR A 39 0
SHEET 2 AA210 VAL A 257 THR A 259 1 O THR A 259 N GLN A 38
SHEET 3 AA210 TYR A 190 GLY A 195 -1 N ARG A 192 O TYR A 258
SHEET 4 AA210 VAL A 206 PHE A 211 -1 O VAL A 206 N GLY A 195
SHEET 5 AA210 LEU A 139 MET A 148 1 N ALA A 143 O THR A 209
SHEET 6 AA210 ALA A 114 ASN A 122 -1 N ALA A 114 O ILE A 146
SHEET 7 AA210 TYR A 85 TRP A 94 -1 N GLN A 89 O VAL A 119
SHEET 8 AA210 VAL A 68 ASN A 71 -1 N LEU A 70 O LEU A 90
SHEET 9 AA210 GLN A 58 ASN A 63 -1 N LEU A 60 O ASN A 71
SHEET 10 AA210 GLU A 171 PRO A 175 -1 O ALA A 172 N LEU A 61
SHEET 1 AA3 6 GLU A 47 GLN A 49 0
SHEET 2 AA3 6 HIS A 77 GLN A 79 -1 O HIS A 77 N GLN A 49
SHEET 3 AA3 6 TYR A 85 TRP A 94 -1 O TYR A 85 N ILE A 78
SHEET 4 AA3 6 ALA A 114 ASN A 122 -1 O VAL A 119 N GLN A 89
SHEET 5 AA3 6 LEU A 139 MET A 148 -1 O ILE A 146 N ALA A 114
SHEET 6 AA3 6 VAL A 215 ILE A 217 1 O VAL A 215 N GLU A 147
SHEET 1 AA4 2 ASP B 31 LEU B 32 0
SHEET 2 AA4 2 THR B 106 VAL B 107 1 O THR B 106 N LEU B 32
SHEET 1 AA510 LEU B 37 TYR B 39 0
SHEET 2 AA510 VAL B 257 THR B 259 1 O VAL B 257 N GLN B 38
SHEET 3 AA510 TYR B 190 GLY B 195 -1 N ARG B 192 O TYR B 258
SHEET 4 AA510 VAL B 206 PHE B 211 -1 O VAL B 206 N GLY B 195
SHEET 5 AA510 LEU B 139 MET B 148 1 N ALA B 143 O THR B 209
SHEET 6 AA510 ALA B 114 ASN B 122 -1 N ALA B 114 O ILE B 146
SHEET 7 AA510 TYR B 85 TRP B 94 -1 N GLN B 89 O VAL B 119
SHEET 8 AA510 VAL B 68 ASN B 71 -1 N LEU B 70 O LEU B 90
SHEET 9 AA510 GLN B 58 ASN B 63 -1 N LEU B 60 O ASN B 71
SHEET 10 AA510 GLU B 171 PRO B 175 -1 O ALA B 172 N LEU B 61
SHEET 1 AA6 6 GLU B 47 GLN B 49 0
SHEET 2 AA6 6 HIS B 77 GLN B 79 -1 O HIS B 77 N GLN B 49
SHEET 3 AA6 6 TYR B 85 TRP B 94 -1 O TYR B 85 N ILE B 78
SHEET 4 AA6 6 ALA B 114 ASN B 122 -1 O VAL B 119 N GLN B 89
SHEET 5 AA6 6 LEU B 139 MET B 148 -1 O ILE B 146 N ALA B 114
SHEET 6 AA6 6 VAL B 215 ILE B 217 1 O VAL B 215 N GLU B 147
SHEET 1 AA7 2 ASP C 31 LEU C 32 0
SHEET 2 AA7 2 THR C 106 VAL C 107 1 O THR C 106 N LEU C 32
SHEET 1 AA810 LEU C 37 TYR C 39 0
SHEET 2 AA810 VAL C 257 THR C 259 1 O THR C 259 N GLN C 38
SHEET 3 AA810 TYR C 190 GLY C 195 -1 N ARG C 192 O TYR C 258
SHEET 4 AA810 VAL C 206 PHE C 211 -1 O VAL C 206 N GLY C 195
SHEET 5 AA810 LEU C 139 MET C 148 1 N ALA C 143 O THR C 209
SHEET 6 AA810 ALA C 114 ASN C 122 -1 N LEU C 116 O VAL C 144
SHEET 7 AA810 TYR C 85 TRP C 94 -1 N GLN C 89 O VAL C 119
SHEET 8 AA810 VAL C 68 ASN C 71 -1 N LEU C 70 O LEU C 90
SHEET 9 AA810 GLN C 58 ASN C 63 -1 N LEU C 60 O ASN C 71
SHEET 10 AA810 GLU C 171 PRO C 175 -1 O ALA C 172 N LEU C 61
SHEET 1 AA9 6 GLU C 47 GLN C 49 0
SHEET 2 AA9 6 HIS C 77 GLN C 79 -1 O HIS C 77 N GLN C 49
SHEET 3 AA9 6 TYR C 85 TRP C 94 -1 O TYR C 85 N ILE C 78
SHEET 4 AA9 6 ALA C 114 ASN C 122 -1 O VAL C 119 N GLN C 89
SHEET 5 AA9 6 LEU C 139 MET C 148 -1 O VAL C 144 N LEU C 116
SHEET 6 AA9 6 VAL C 215 ILE C 217 1 O VAL C 215 N GLU C 147
SHEET 1 AB1 2 ASP D 31 LEU D 32 0
SHEET 2 AB1 2 THR D 106 VAL D 107 1 O THR D 106 N LEU D 32
SHEET 1 AB210 LEU D 37 TYR D 39 0
SHEET 2 AB210 VAL D 257 THR D 259 1 O THR D 259 N GLN D 38
SHEET 3 AB210 TYR D 190 GLY D 195 -1 N ARG D 192 O TYR D 258
SHEET 4 AB210 VAL D 206 PHE D 211 -1 O VAL D 206 N GLY D 195
SHEET 5 AB210 LEU D 139 MET D 148 1 N ALA D 143 O THR D 209
SHEET 6 AB210 ALA D 114 ASN D 122 -1 N LEU D 116 O VAL D 144
SHEET 7 AB210 TYR D 85 TRP D 94 -1 N HIS D 91 O HIS D 117
SHEET 8 AB210 VAL D 68 ASN D 71 -1 N LEU D 70 O LEU D 90
SHEET 9 AB210 GLN D 58 ASN D 63 -1 N LEU D 60 O ASN D 71
SHEET 10 AB210 GLU D 171 PRO D 175 -1 O ALA D 172 N LEU D 61
SHEET 1 AB3 6 GLU D 47 GLN D 49 0
SHEET 2 AB3 6 HIS D 77 GLN D 79 -1 O HIS D 77 N GLN D 49
SHEET 3 AB3 6 TYR D 85 TRP D 94 -1 O TYR D 85 N ILE D 78
SHEET 4 AB3 6 ALA D 114 ASN D 122 -1 O HIS D 117 N HIS D 91
SHEET 5 AB3 6 LEU D 139 MET D 148 -1 O VAL D 144 N LEU D 116
SHEET 6 AB3 6 VAL D 215 ILE D 217 1 O VAL D 215 N GLU D 147
SSBOND 1 CYS A 22 CYS A 202 1555 1555 2.09
SSBOND 2 CYS B 22 CYS B 202 1555 1555 2.06
SSBOND 3 CYS C 22 CYS C 202 1555 1555 2.05
SSBOND 4 CYS D 22 CYS D 202 1555 1555 2.04
LINK NE2 HIS A 91 ZN ZN A 301 1555 1555 2.01
LINK NE2 HIS A 93 ZN ZN A 301 1555 1555 2.00
LINK ND1 HIS A 117 ZN ZN A 301 1555 1555 1.98
LINK ZN ZN A 301 S2 A6Z9 A 302 1555 1555 2.99
LINK ZN ZN A 301 N29A6Z9 A 302 1555 1555 1.92
LINK ZN ZN A 301 N29B6Z9 A 302 1555 1555 1.91
LINK NE2 HIS B 91 ZN ZN B 301 1555 1555 2.02
LINK NE2 HIS B 93 ZN ZN B 301 1555 1555 2.05
LINK ND1 HIS B 117 ZN ZN B 301 1555 1555 2.01
LINK ZN ZN B 301 N29 6Z9 B 302 1555 1555 1.86
LINK NE2 HIS C 91 ZN ZN C 301 1555 1555 2.01
LINK NE2 HIS C 93 ZN ZN C 301 1555 1555 2.04
LINK ND1 HIS C 117 ZN ZN C 301 1555 1555 1.98
LINK ZN ZN C 301 N29 6Z9 C 302 1555 1555 1.90
LINK NE2 HIS D 91 ZN ZN D 301 1555 1555 1.99
LINK NE2 HIS D 93 ZN ZN D 301 1555 1555 2.01
LINK ND1 HIS D 117 ZN ZN D 301 1555 1555 2.01
LINK ZN ZN D 301 N29 6Z9 D 302 1555 1555 1.95
CISPEP 1 SER A 28 PRO A 29 0 -0.35
CISPEP 2 PRO A 200 PRO A 201 0 6.72
CISPEP 3 SER B 28 PRO B 29 0 -2.03
CISPEP 4 PRO B 200 PRO B 201 0 10.52
CISPEP 5 SER C 28 PRO C 29 0 3.56
CISPEP 6 PRO C 200 PRO C 201 0 9.35
CISPEP 7 SER D 28 PRO D 29 0 1.39
CISPEP 8 PRO D 200 PRO D 201 0 2.45
SITE 1 AC1 4 HIS A 91 HIS A 93 HIS A 117 6Z9 A 302
SITE 1 AC2 16 TRP A 4 ASN A 64 LYS A 69 GLN A 89
SITE 2 AC2 16 HIS A 91 HIS A 93 GLU A 104 HIS A 117
SITE 3 AC2 16 ALA A 129 SER A 133 LEU A 197 THR A 198
SITE 4 AC2 16 THR A 199 PRO A 200 ZN A 301 HOH A 623
SITE 1 AC3 4 HIS B 91 HIS B 93 HIS B 117 6Z9 B 302
SITE 1 AC4 12 ASN B 64 SER B 67 HIS B 91 HIS B 93
SITE 2 AC4 12 HIS B 117 ALA B 129 LEU B 197 THR B 198
SITE 3 AC4 12 THR B 199 PRO B 200 ZN B 301 HOH B 439
SITE 1 AC5 4 HIS C 91 HIS C 93 HIS C 117 6Z9 C 302
SITE 1 AC6 13 ASN C 64 LYS C 69 GLN C 89 HIS C 91
SITE 2 AC6 13 HIS C 93 GLU C 104 HIS C 117 ALA C 129
SITE 3 AC6 13 LEU C 197 THR C 198 THR C 199 PRO C 201
SITE 4 AC6 13 ZN C 301
SITE 1 AC7 4 HIS D 91 HIS D 93 HIS D 117 6Z9 D 302
SITE 1 AC8 14 ASN D 64 HIS D 91 HIS D 93 HIS D 117
SITE 2 AC8 14 VAL D 119 ALA D 129 SER D 130 LEU D 197
SITE 3 AC8 14 THR D 198 THR D 199 PRO D 200 ZN D 301
SITE 4 AC8 14 HOH D 406 HOH D 513
CRYST1 77.488 74.288 91.658 90.00 108.97 90.00 P 1 21 1 8
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 0.012905 0.000000 0.004436 0.00000
SCALE2 0.000000 0.013461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011537 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
