HEADER CELL CYCLE 31-OCT-11 4A63
TITLE CRYSTAL STRUCTURE OF THE P73-ASPP2 COMPLEX AT 2.6A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOUR PROTEIN 73;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN, RESIDUES 1-208;
COMPND 5 SYNONYM: P53-LIKE TRANSCRIPTION FACTOR, P53-RELATED PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: APOPTOSIS STIMULATING OF P53 PROTEIN 2;
COMPND 9 CHAIN: B, D, F, H, J, L;
COMPND 10 FRAGMENT: ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128;
COMPND 11 SYNONYM: BCL2-BINDING PROTEIN, BBP, RENAL CARCINOMA ANTIGEN NY-REN-
COMPND 12 51,TUMOR SUPPRESSOR P53-BINDING PROTEIN 2,53BP2, P53-BINDING PROTEIN
COMPND 13 2, P53BP2;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PNIC-CTHF;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: R3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR: PCOEX-LIC1
KEYWDS CELL CYCLE, TP53BP2, TUMOUR SUPPRESSOR, ANKYRINS, APOPTOSIS
KEYWDS 2 REGULATORY PROTEINS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CANNING,T.SHARPE,T.KROJER,P.SAVITSKY,C.D.O.COOPER,E.SALAH,T.KEATES,
AUTHOR 2 J.MUNIZ,M.VOLLMAR,F.VON DELFT,J.WEIGELT,C.ARROWSMITH,C.BOUNTRA,
AUTHOR 3 A.EDWARDS,A.N.BULLOCK
REVDAT 5 20-DEC-23 4A63 1 REMARK LINK
REVDAT 4 24-JAN-18 4A63 1 AUTHOR JRNL
REVDAT 3 31-OCT-12 4A63 1 JRNL
REVDAT 2 26-SEP-12 4A63 1 AUTHOR JRNL
REVDAT 1 21-DEC-11 4A63 0
JRNL AUTH P.CANNING,F.VON DELFT,A.N.BULLOCK
JRNL TITL STRUCTURAL BASIS FOR ASPP2 RECOGNITION BY THE TUMOR
JRNL TITL 2 SUPPRESSOR P73.
JRNL REF J.MOL.BIOL. V. 423 515 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22917970
JRNL DOI 10.1016/J.JMB.2012.08.005
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 175926
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 8824
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.33
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.07
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 13092
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2432
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12399
REMARK 3 BIN R VALUE (WORKING SET) : 0.2422
REMARK 3 BIN FREE R VALUE : 0.2617
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.29
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 693
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18374
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 671
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.01350
REMARK 3 B22 (A**2) : -6.42610
REMARK 3 B33 (A**2) : 7.43950
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.28470
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.305
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.212
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.181
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.217
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.184
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.782
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 18918 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 25841 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 8430 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 466 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2792 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 18918 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 7 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 2517 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 21358 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.05
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.64
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: INITIAL REFINEMENT WITH REFMAC BUSTER
REMARK 3 2.1 PHENIX.XTRIAGE. THE ANALYSES OF THE PATTERSON FUNCTION
REMARK 3 REVEALS A SIGNIFICANT OFF-ORIGIN PEAK THAT IS 47.52 PERCENT OF
REMARK 3 THE ORIGIN PEAK, INDICATING PSEUDO TRANSLATIONAL SYMMETRY. IDEAL-
REMARK 3 DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM
REMARK 3 TYPE IN LIBRARY=ZN. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=
REMARK 3 19288. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=0 NUMBER
REMARK 3 TREATED BY BAD NON-BONDED CONTACTS=6.
REMARK 4
REMARK 4 4A63 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1290050156.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 111026
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 88.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2XWC AND 1YCS CHAIN B
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.00M NA/KPO4, 0.1M ACETATE PH 4.5
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 63.33768
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 85.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 88.72450
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.33768
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 85.05000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 88.72450
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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: 1580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.4 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: 1590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.6 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 350
REMARK 350 BIOMOLECULE: 3
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: 1510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
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: 1620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
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 111
REMARK 465 ALA A 112
REMARK 465 PRO A 113
REMARK 465 SER B 890
REMARK 465 MET B 891
REMARK 465 PRO B 892
REMARK 465 GLU B 893
REMARK 465 ILE B 894
REMARK 465 THR B 895
REMARK 465 GLY B 896
REMARK 465 GLN B 897
REMARK 465 VAL B 898
REMARK 465 SER B 899
REMARK 465 LEU B 900
REMARK 465 PRO B 901
REMARK 465 PRO B 902
REMARK 465 GLY B 903
REMARK 465 LYS B 904
REMARK 465 ARG B 905
REMARK 465 THR B 906
REMARK 465 ASN B 907
REMARK 465 LEU B 908
REMARK 465 ARG B 909
REMARK 465 LYS B 910
REMARK 465 THR B 911
REMARK 465 GLY B 912
REMARK 465 SER B 913
REMARK 465 GLU B 914
REMARK 465 ARG B 915
REMARK 465 ILE B 916
REMARK 465 ALA B 917
REMARK 465 HIS B 918
REMARK 465 GLY B 919
REMARK 465 PRO B 1122
REMARK 465 ARG B 1123
REMARK 465 GLN B 1124
REMARK 465 ARG B 1125
REMARK 465 SER B 1126
REMARK 465 LEU B 1127
REMARK 465 ALA B 1128
REMARK 465 MET C 111
REMARK 465 ALA C 112
REMARK 465 PRO C 113
REMARK 465 SER D 890
REMARK 465 MET D 891
REMARK 465 PRO D 892
REMARK 465 GLU D 893
REMARK 465 ILE D 894
REMARK 465 THR D 895
REMARK 465 GLY D 896
REMARK 465 GLN D 897
REMARK 465 VAL D 898
REMARK 465 SER D 899
REMARK 465 LEU D 900
REMARK 465 PRO D 901
REMARK 465 PRO D 902
REMARK 465 GLY D 903
REMARK 465 LYS D 904
REMARK 465 ARG D 905
REMARK 465 THR D 906
REMARK 465 ASN D 907
REMARK 465 LEU D 908
REMARK 465 ARG D 909
REMARK 465 LYS D 910
REMARK 465 THR D 911
REMARK 465 GLY D 912
REMARK 465 SER D 913
REMARK 465 GLU D 914
REMARK 465 ARG D 915
REMARK 465 ILE D 916
REMARK 465 ALA D 917
REMARK 465 HIS D 918
REMARK 465 GLY D 919
REMARK 465 MET D 920
REMARK 465 ARG D 921
REMARK 465 VAL D 922
REMARK 465 LYS D 923
REMARK 465 PHE D 924
REMARK 465 LYS D 1121
REMARK 465 PRO D 1122
REMARK 465 ARG D 1123
REMARK 465 GLN D 1124
REMARK 465 ARG D 1125
REMARK 465 SER D 1126
REMARK 465 LEU D 1127
REMARK 465 ALA D 1128
REMARK 465 MET E 111
REMARK 465 ALA E 112
REMARK 465 PRO E 113
REMARK 465 SER F 890
REMARK 465 MET F 891
REMARK 465 PRO F 892
REMARK 465 GLU F 893
REMARK 465 ILE F 894
REMARK 465 THR F 895
REMARK 465 GLY F 896
REMARK 465 GLN F 897
REMARK 465 VAL F 898
REMARK 465 SER F 899
REMARK 465 LEU F 900
REMARK 465 PRO F 901
REMARK 465 PRO F 902
REMARK 465 GLY F 903
REMARK 465 LYS F 904
REMARK 465 ARG F 905
REMARK 465 THR F 906
REMARK 465 ASN F 907
REMARK 465 LEU F 908
REMARK 465 ARG F 909
REMARK 465 LYS F 910
REMARK 465 THR F 911
REMARK 465 GLY F 912
REMARK 465 SER F 913
REMARK 465 GLU F 914
REMARK 465 ARG F 915
REMARK 465 ILE F 916
REMARK 465 ALA F 917
REMARK 465 HIS F 918
REMARK 465 GLY F 919
REMARK 465 MET F 920
REMARK 465 ARG F 921
REMARK 465 VAL F 922
REMARK 465 LYS F 923
REMARK 465 PHE F 924
REMARK 465 PRO F 1122
REMARK 465 ARG F 1123
REMARK 465 GLN F 1124
REMARK 465 ARG F 1125
REMARK 465 SER F 1126
REMARK 465 LEU F 1127
REMARK 465 ALA F 1128
REMARK 465 MET G 111
REMARK 465 ALA G 112
REMARK 465 PRO G 113
REMARK 465 SER H 890
REMARK 465 MET H 891
REMARK 465 PRO H 892
REMARK 465 GLU H 893
REMARK 465 ILE H 894
REMARK 465 THR H 895
REMARK 465 GLY H 896
REMARK 465 GLN H 897
REMARK 465 VAL H 898
REMARK 465 SER H 899
REMARK 465 LEU H 900
REMARK 465 PRO H 901
REMARK 465 PRO H 902
REMARK 465 GLY H 903
REMARK 465 LYS H 904
REMARK 465 ARG H 905
REMARK 465 THR H 906
REMARK 465 ASN H 907
REMARK 465 LEU H 908
REMARK 465 ARG H 909
REMARK 465 LYS H 910
REMARK 465 THR H 911
REMARK 465 GLY H 912
REMARK 465 SER H 913
REMARK 465 GLU H 914
REMARK 465 ARG H 915
REMARK 465 ILE H 916
REMARK 465 ALA H 917
REMARK 465 HIS H 918
REMARK 465 GLY H 919
REMARK 465 MET H 920
REMARK 465 ARG H 921
REMARK 465 VAL H 922
REMARK 465 LYS H 1121
REMARK 465 PRO H 1122
REMARK 465 ARG H 1123
REMARK 465 GLN H 1124
REMARK 465 ARG H 1125
REMARK 465 SER H 1126
REMARK 465 LEU H 1127
REMARK 465 ALA H 1128
REMARK 465 MET I 111
REMARK 465 ALA I 112
REMARK 465 PRO I 113
REMARK 465 SER J 890
REMARK 465 MET J 891
REMARK 465 PRO J 892
REMARK 465 GLU J 893
REMARK 465 ILE J 894
REMARK 465 THR J 895
REMARK 465 GLY J 896
REMARK 465 GLN J 897
REMARK 465 VAL J 898
REMARK 465 SER J 899
REMARK 465 LEU J 900
REMARK 465 PRO J 901
REMARK 465 PRO J 902
REMARK 465 GLY J 903
REMARK 465 LYS J 904
REMARK 465 ARG J 905
REMARK 465 THR J 906
REMARK 465 ASN J 907
REMARK 465 LEU J 908
REMARK 465 ARG J 909
REMARK 465 LYS J 910
REMARK 465 THR J 911
REMARK 465 GLY J 912
REMARK 465 SER J 913
REMARK 465 GLU J 914
REMARK 465 ARG J 915
REMARK 465 ILE J 916
REMARK 465 ALA J 917
REMARK 465 HIS J 918
REMARK 465 GLY J 919
REMARK 465 MET J 920
REMARK 465 ARG J 921
REMARK 465 VAL J 922
REMARK 465 ARG J 1123
REMARK 465 GLN J 1124
REMARK 465 ARG J 1125
REMARK 465 SER J 1126
REMARK 465 LEU J 1127
REMARK 465 ALA J 1128
REMARK 465 MET K 111
REMARK 465 ALA K 112
REMARK 465 PRO K 113
REMARK 465 SER L 890
REMARK 465 MET L 891
REMARK 465 PRO L 892
REMARK 465 GLU L 893
REMARK 465 ILE L 894
REMARK 465 THR L 895
REMARK 465 GLY L 896
REMARK 465 GLN L 897
REMARK 465 VAL L 898
REMARK 465 SER L 899
REMARK 465 LEU L 900
REMARK 465 PRO L 901
REMARK 465 PRO L 902
REMARK 465 GLY L 903
REMARK 465 LYS L 904
REMARK 465 ARG L 905
REMARK 465 THR L 906
REMARK 465 ASN L 907
REMARK 465 LEU L 908
REMARK 465 ARG L 909
REMARK 465 LYS L 910
REMARK 465 THR L 911
REMARK 465 GLY L 912
REMARK 465 SER L 913
REMARK 465 GLU L 914
REMARK 465 ARG L 915
REMARK 465 ILE L 916
REMARK 465 ALA L 917
REMARK 465 HIS L 918
REMARK 465 GLY L 919
REMARK 465 MET L 920
REMARK 465 ARG L 921
REMARK 465 VAL L 922
REMARK 465 LYS L 923
REMARK 465 PHE L 924
REMARK 465 LYS L 1121
REMARK 465 PRO L 1122
REMARK 465 ARG L 1123
REMARK 465 GLN L 1124
REMARK 465 ARG L 1125
REMARK 465 SER L 1126
REMARK 465 LEU L 1127
REMARK 465 ALA L 1128
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 GLN A 133 CG CD OE1 NE2
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 LYS A 183 CE NZ
REMARK 470 LYS A 192 CD CE NZ
REMARK 470 ARG A 201 NE CZ NH1 NH2
REMARK 470 LYS A 303 CD CE NZ
REMARK 470 GLU A 311 CD OE1 OE2
REMARK 470 MET B 920 CG SD CE
REMARK 470 ARG B 921 CD NE CZ NH1 NH2
REMARK 470 LYS B 923 CG CD CE NZ
REMARK 470 LEU B 929 CG CD1 CD2
REMARK 470 LEU B 931 CG CD1 CD2
REMARK 470 ASP B 932 CG OD1 OD2
REMARK 470 ILE B 945 CG1 CG2 CD1
REMARK 470 ASP B 950 CG OD1 OD2
REMARK 470 GLU B 958 CG CD OE1 OE2
REMARK 470 LYS B 976 CG CD CE NZ
REMARK 470 MET B1036 CG SD CE
REMARK 470 LYS B1059 CG CD CE NZ
REMARK 470 GLU B1069 CG CD OE1 OE2
REMARK 470 ASP B1093 CG OD1 OD2
REMARK 470 ARG B1101 CG CD NE CZ NH1 NH2
REMARK 470 ASN B1103 CG OD1 ND2
REMARK 470 LYS B1105 CG CD CE NZ
REMARK 470 LYS B1121 CG CD CE NZ
REMARK 470 GLN C 133 CG CD OE1 NE2
REMARK 470 LYS C 138 CG CD CE NZ
REMARK 470 GLU C 205 CG CD OE1 OE2
REMARK 470 GLN C 207 CG CD OE1 NE2
REMARK 470 ARG C 280 CD NE CZ NH1 NH2
REMARK 470 ARG C 300 NE CZ NH1 NH2
REMARK 470 GLN C 318 CG CD OE1 NE2
REMARK 470 ASN D 925 CG OD1 ND2
REMARK 470 LEU D 927 CG CD1 CD2
REMARK 470 LEU D 929 CG CD1 CD2
REMARK 470 LEU D 931 CG CD1 CD2
REMARK 470 GLU D 936 CG CD OE1 OE2
REMARK 470 GLU D 938 CG CD OE1 OE2
REMARK 470 PHE D 939 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 940 CG OD1 OD2
REMARK 470 LEU D 941 CG CD1 CD2
REMARK 470 ARG D 944 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 946 CG1 CG2 CD1
REMARK 470 GLU D 948 CG CD OE1 OE2
REMARK 470 ASP D 950 CG OD1 OD2
REMARK 470 LEU D 954 CG CD1 CD2
REMARK 470 ASP D 957 CG OD1 OD2
REMARK 470 GLU D 958 CG CD OE1 OE2
REMARK 470 GLU D 973 CG CD OE1 OE2
REMARK 470 PHE D 977 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN D 980 CG CD OE1 NE2
REMARK 470 PHE D 981 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 989 CG OD1 OD2
REMARK 470 ASP D1025 CG OD1 OD2
REMARK 470 GLU D1034 CG CD OE1 OE2
REMARK 470 GLU D1035 CG CD OE1 OE2
REMARK 470 GLU D1038 CG CD OE1 OE2
REMARK 470 GLU D1052 CG CD OE1 OE2
REMARK 470 LYS D1059 CG CD CE NZ
REMARK 470 GLU D1069 CG CD OE1 OE2
REMARK 470 LYS D1079 CG CD CE NZ
REMARK 470 GLU D1080 CD OE1 OE2
REMARK 470 GLU D1092 CG CD OE1 OE2
REMARK 470 ASP D1093 CG OD1 OD2
REMARK 470 ARG D1101 CG CD NE CZ NH1 NH2
REMARK 470 ASN D1103 CG OD1 ND2
REMARK 470 ASP D1104 CG OD1 OD2
REMARK 470 LYS D1105 CG CD CE NZ
REMARK 470 GLN E 133 CG CD OE1 NE2
REMARK 470 LYS E 138 CG CD CE NZ
REMARK 470 LYS E 149 CG CD CE NZ
REMARK 470 LYS E 183 CD CE NZ
REMARK 470 GLU E 185 CD OE1 OE2
REMARK 470 ARG E 201 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 205 CG CD OE1 OE2
REMARK 470 GLN E 207 CG CD OE1 NE2
REMARK 470 SER E 208 OG
REMARK 470 GLU E 241 CG CD OE1 OE2
REMARK 470 ARG E 280 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 300 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 303 CG CD CE NZ
REMARK 470 GLN E 318 CG CD OE1 NE2
REMARK 470 ASN F 925 CG OD1 ND2
REMARK 470 LEU F 927 CG CD1 CD2
REMARK 470 LEU F 929 CG CD1 CD2
REMARK 470 GLU F 938 CG CD OE1 OE2
REMARK 470 ASP F 940 CG OD1 OD2
REMARK 470 GLN F 943 CG CD OE1 NE2
REMARK 470 ARG F 944 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 946 CG1 CG2 CD1
REMARK 470 VAL F 949 CG1 CG2
REMARK 470 ASP F 950 CG OD1 OD2
REMARK 470 GLU F 958 CG CD OE1 OE2
REMARK 470 VAL F 967 CG1 CG2
REMARK 470 GLU F 973 CG CD OE1 OE2
REMARK 470 ILE F 974 CG1 CG2 CD1
REMARK 470 LYS F 976 CG CD CE NZ
REMARK 470 PHE F 977 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN F 980 CG CD OE1 NE2
REMARK 470 PHE F 981 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN F1006 CG CD OE1 NE2
REMARK 470 LYS F1009 CG CD CE NZ
REMARK 470 GLU F1035 CD OE1 OE2
REMARK 470 MET F1036 SD CE
REMARK 470 GLU F1038 CG CD OE1 OE2
REMARK 470 LYS F1053 CD CE NZ
REMARK 470 LYS F1059 CG CD CE NZ
REMARK 470 GLU F1069 CG CD OE1 OE2
REMARK 470 LYS F1079 CG CD CE NZ
REMARK 470 ASP F1093 CG OD1 OD2
REMARK 470 ARG F1101 CG CD NE CZ NH1 NH2
REMARK 470 ASN F1103 CG OD1 ND2
REMARK 470 ASP F1104 CG OD1 OD2
REMARK 470 LYS F1105 CG CD CE NZ
REMARK 470 LYS F1121 CG CD CE NZ
REMARK 470 GLN G 133 CG CD OE1 NE2
REMARK 470 LYS G 138 CG CD CE NZ
REMARK 470 LYS G 183 CE NZ
REMARK 470 GLU G 185 CD OE1 OE2
REMARK 470 LYS H 923 CG CD CE NZ
REMARK 470 ASN H 925 CG OD1 ND2
REMARK 470 LEU H 929 CG CD1 CD2
REMARK 470 ASP H 932 CG OD1 OD2
REMARK 470 LEU H 935 CG CD1 CD2
REMARK 470 GLU H 936 CG CD OE1 OE2
REMARK 470 GLU H 938 CG CD OE1 OE2
REMARK 470 GLN H 943 CG CD OE1 NE2
REMARK 470 ARG H 944 CG CD NE CZ NH1 NH2
REMARK 470 ILE H 946 CG1 CG2 CD1
REMARK 470 GLU H 948 CG CD OE1 OE2
REMARK 470 ASP H 950 CG OD1 OD2
REMARK 470 GLU H 958 CG CD OE1 OE2
REMARK 470 GLU H 973 CG CD OE1 OE2
REMARK 470 LYS H 976 CG CD CE NZ
REMARK 470 GLN H 980 CG CD OE1 NE2
REMARK 470 GLN H1006 CG CD OE1 NE2
REMARK 470 ASP H1025 CG OD1 OD2
REMARK 470 MET H1036 CG SD CE
REMARK 470 GLU H1052 CD OE1 OE2
REMARK 470 LYS H1053 CG CD CE NZ
REMARK 470 GLU H1069 CG CD OE1 OE2
REMARK 470 LYS H1079 CG CD CE NZ
REMARK 470 ASP H1093 CG OD1 OD2
REMARK 470 ARG H1101 NE CZ NH1 NH2
REMARK 470 ASN H1103 CG OD1 ND2
REMARK 470 ASP H1104 CG OD1 OD2
REMARK 470 LYS H1105 CG CD CE NZ
REMARK 470 GLN I 133 CG CD OE1 NE2
REMARK 470 LYS I 138 CG CD CE NZ
REMARK 470 GLU I 185 CG CD OE1 OE2
REMARK 470 ARG I 300 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 303 CG CD CE NZ
REMARK 470 LYS J 923 CG CD CE NZ
REMARK 470 ASP J 932 CG OD1 OD2
REMARK 470 ASP J 950 CG OD1 OD2
REMARK 470 GLU J 958 CG CD OE1 OE2
REMARK 470 GLU J 973 CG CD OE1 OE2
REMARK 470 LYS J 976 CG CD CE NZ
REMARK 470 GLN J1006 CG CD OE1 NE2
REMARK 470 MET J1036 CG SD CE
REMARK 470 GLU J1052 CG CD OE1 OE2
REMARK 470 GLU J1069 CG CD OE1 OE2
REMARK 470 ASP J1093 CG OD1 OD2
REMARK 470 ASN J1103 CG OD1 ND2
REMARK 470 ASP J1104 CG OD1 OD2
REMARK 470 LYS J1105 CG CD CE NZ
REMARK 470 LYS J1121 CG CD CE NZ
REMARK 470 GLN K 133 CG CD OE1 NE2
REMARK 470 SER K 135 OG
REMARK 470 ARG K 201 CG CD NE CZ NH1 NH2
REMARK 470 GLU K 205 CG CD OE1 OE2
REMARK 470 GLN K 244 CG CD OE1 NE2
REMARK 470 LYS K 303 CG CD CE NZ
REMARK 470 GLN K 318 CG CD OE1 NE2
REMARK 470 ASN L 925 CG OD1 ND2
REMARK 470 LEU L 929 CG CD1 CD2
REMARK 470 ASP L 932 CG OD1 OD2
REMARK 470 ARG L 944 CG CD NE CZ NH1 NH2
REMARK 470 ILE L 946 CG1 CG2 CD1
REMARK 470 GLU L 948 CG CD OE1 OE2
REMARK 470 ASP L 950 CG OD1 OD2
REMARK 470 GLU L 958 CG CD OE1 OE2
REMARK 470 GLU L 973 CG CD OE1 OE2
REMARK 470 LYS L 976 CD CE NZ
REMARK 470 PHE L 981 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER L1024 OG
REMARK 470 ASP L1025 CG OD1 OD2
REMARK 470 MET L1036 CG SD CE
REMARK 470 GLU L1052 CG CD OE1 OE2
REMARK 470 LYS L1053 CD CE NZ
REMARK 470 LYS L1059 CG CD CE NZ
REMARK 470 GLU L1069 CG CD OE1 OE2
REMARK 470 ASP L1093 CG OD1 OD2
REMARK 470 ASN L1103 CG OD1 ND2
REMARK 470 LYS L1105 CG CD CE NZ
REMARK 470 ASN L1112 CG OD1 ND2
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 CB ILE E 275 O HOH E 2047 0.39
REMARK 500 CA GLY K 206 O HOH K 2061 0.62
REMARK 500 N ASN G 221 O HOH G 2081 0.70
REMARK 500 OE2 GLU C 311 O HOH C 2095 0.81
REMARK 500 O HOH G 2034 O HOH G 2036 0.83
REMARK 500 C ASN G 220 O HOH G 2081 0.89
REMARK 500 O PRO G 146 O HOH G 2025 0.89
REMARK 500 CA LYS G 138 O HOH G 2022 0.94
REMARK 500 CD GLU C 313 O HOH C 2100 0.97
REMARK 500 CA TYR K 152 O HOH K 2025 0.98
REMARK 500 O HOH C 2091 O HOH C 2092 1.10
REMARK 500 CB TYR K 152 O HOH K 2025 1.11
REMARK 500 O PHE C 317 O HOH C 2101 1.11
REMARK 500 N PRO G 229 O HOH G 2088 1.12
REMARK 500 O HOH G 2110 O HOH G 2114 1.13
REMARK 500 N GLU K 205 O HOH K 2060 1.15
REMARK 500 OE1 GLU C 313 O HOH C 2100 1.17
REMARK 500 OE2 GLU C 313 O HOH C 2100 1.18
REMARK 500 CA GLU K 205 O HOH K 2060 1.20
REMARK 500 CB ASP I 228 O HOH I 2086 1.20
REMARK 500 CD GLU C 311 O HOH C 2095 1.21
REMARK 500 O ILE G 155 O HOH G 2032 1.21
REMARK 500 CE3 TRP K 142 O HOH K 2020 1.22
REMARK 500 CB ASP C 307 O HOH C 2084 1.22
REMARK 500 O HOH G 2105 O HOH G 2106 1.23
REMARK 500 OXT ACT I 1320 O HOH I 2022 1.24
REMARK 500 N LYS G 138 O HOH G 2022 1.25
REMARK 500 N GLY K 206 O HOH K 2061 1.27
REMARK 500 CG MET K 266 O HOH K 2085 1.29
REMARK 500 CB TYR G 121 O HOH G 2010 1.31
REMARK 500 C ASP G 228 O HOH G 2088 1.35
REMARK 500 O GLY C 286 O HOH C 2073 1.38
REMARK 500 C GLU K 205 O HOH K 2060 1.40
REMARK 500 C PRO G 146 O HOH G 2025 1.43
REMARK 500 N CYS G 262 O HOH G 2094 1.49
REMARK 500 CA ARG C 287 O HOH C 2073 1.54
REMARK 500 CG2 ILE E 275 O HOH E 2047 1.54
REMARK 500 C ARG C 310 O HOH C 2093 1.55
REMARK 500 SD MET K 266 O HOH K 2085 1.57
REMARK 500 CB ASP E 301 O HOH E 2055 1.58
REMARK 500 CG1 VAL G 226 O HOH G 2085 1.59
REMARK 500 C GLY C 286 O HOH C 2073 1.60
REMARK 500 C PHE C 317 O HOH C 2101 1.60
REMARK 500 N ARG C 287 O HOH C 2073 1.61
REMARK 500 O ARG C 310 O HOH C 2093 1.62
REMARK 500 CA ASN K 255 O HOH K 2032 1.63
REMARK 500 CB LYS G 138 O HOH G 2022 1.63
REMARK 500 NH2 ARG K 280 O HOH E 2049 1.69
REMARK 500 OE1 GLU C 311 O HOH C 2095 1.70
REMARK 500 O TYR G 121 O HOH G 2010 1.72
REMARK 500
REMARK 500 THIS ENTRY HAS 110 CLOSE CONTACTS
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 C 2062 O HOH C 2076 2656 0.87
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 MET E 266 CB - CG - SD ANGL. DEV. = -19.7 DEGREES
REMARK 500 ASP J1025 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP J1025 CB - CG - OD2 ANGL. DEV. = 6.1 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 GLN A 133 102.32 -40.82
REMARK 500 CYS A 262 109.93 -53.54
REMARK 500 ARG A 268 -1.34 75.48
REMARK 500 ASN B 984 108.86 -57.91
REMARK 500 ASP B 989 -172.98 -66.08
REMARK 500 MET B1026 60.72 -104.55
REMARK 500 GLU B1094 78.53 61.19
REMARK 500 ASN B1103 -111.45 60.03
REMARK 500 GLN C 133 105.12 -44.24
REMARK 500 ARG C 268 -1.69 73.67
REMARK 500 ASN D 984 109.36 -57.52
REMARK 500 ILE D1056 -55.25 -121.96
REMARK 500 GLU D1094 81.19 61.55
REMARK 500 ASN D1103 -109.54 59.23
REMARK 500 GLN E 133 103.58 -42.89
REMARK 500 CYS E 262 109.34 -55.32
REMARK 500 ARG E 268 -5.03 69.40
REMARK 500 ASN F 984 109.94 -55.64
REMARK 500 ILE F1056 -55.11 -120.17
REMARK 500 GLU F1094 79.16 62.16
REMARK 500 ASN F1103 -110.35 58.22
REMARK 500 GLN G 133 103.68 -43.05
REMARK 500 ARG G 268 -4.52 74.33
REMARK 500 ASN H 984 109.77 -57.87
REMARK 500 ILE H1056 -54.87 -120.02
REMARK 500 GLU H1094 79.13 62.46
REMARK 500 ASN H1103 -111.27 55.24
REMARK 500 GLN I 133 102.08 -39.87
REMARK 500 ARG I 268 -5.08 76.17
REMARK 500 ASP J 989 -167.57 -77.37
REMARK 500 GLU J1094 77.68 62.35
REMARK 500 ASN J1103 -110.65 58.40
REMARK 500 GLN K 133 103.93 -44.47
REMARK 500 VAL K 230 -60.57 -91.13
REMARK 500 ARG K 268 -6.84 77.48
REMARK 500 ASN L 984 107.73 -55.44
REMARK 500 SER L1024 -73.48 -51.94
REMARK 500 MET L1026 38.18 -67.08
REMARK 500 ILE L1056 -55.86 -121.12
REMARK 500 GLU L1094 80.70 62.32
REMARK 500 ASN L1103 -109.93 57.06
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 C2064 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH L2017 DISTANCE = 9.45 ANGSTROMS
REMARK 525 HOH L2018 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH L2019 DISTANCE = 8.76 ANGSTROMS
REMARK 525 HOH L2020 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH L2021 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH L2023 DISTANCE = 8.24 ANGSTROMS
REMARK 525 HOH L2024 DISTANCE = 9.73 ANGSTROMS
REMARK 525 HOH L2025 DISTANCE = 9.90 ANGSTROMS
REMARK 525 HOH L2026 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH L2027 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH L2028 DISTANCE = 9.97 ANGSTROMS
REMARK 525 HOH L2029 DISTANCE = 9.95 ANGSTROMS
REMARK 525 HOH L2030 DISTANCE = 6.98 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ACETATE (ACT): PRESENT IN CRYSTALLIZATION BUFFER
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 C 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 194 SG
REMARK 620 2 HIS C 197 ND1 108.9
REMARK 620 3 CYS C 258 SG 119.0 99.5
REMARK 620 4 CYS C 262 SG 116.8 99.4 109.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 194 SG
REMARK 620 2 HIS E 197 ND1 107.3
REMARK 620 3 CYS E 258 SG 113.6 101.1
REMARK 620 4 CYS E 262 SG 116.3 99.3 116.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 194 SG
REMARK 620 2 HIS G 197 ND1 109.7
REMARK 620 3 CYS G 258 SG 112.3 106.8
REMARK 620 4 CYS G 262 SG 112.3 105.0 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 194 SG
REMARK 620 2 HIS I 197 ND1 110.2
REMARK 620 3 CYS I 258 SG 112.8 105.5
REMARK 620 4 CYS I 262 SG 110.4 105.2 112.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 194 SG
REMARK 620 2 HIS K 197 ND1 107.4
REMARK 620 3 CYS K 258 SG 109.3 103.9
REMARK 620 4 CYS K 262 SG 112.7 104.4 118.1
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 C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT G 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT I 1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT K 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT K 1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT L 1522
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DXS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL STERILE ALPHA MOTIF (SAM)
REMARK 900 DOMAIN OF HUMAN P73 ALPHA
REMARK 900 RELATED ID: 2WQJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A TRUNCATED VARIANT OF THE HUMAN P73
REMARK 900 TETRAMERIZATION DOMAIN
REMARK 900 RELATED ID: 1YCS RELATED DB: PDB
REMARK 900 P53-53BP2 COMPLEX
REMARK 900 RELATED ID: 2XWC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DNA BINDING DOMAIN OF HUMAN TP73 REFINED
REMARK 900 AT 1.8 A RESOLUTION
REMARK 900 RELATED ID: 2WQI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN P73 TETRAMERIZATION DOMAIN
REMARK 900 RELATED ID: 2UWQ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF ASPP2 N-TERMINUS
REMARK 900 RELATED ID: 2WTT RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN P73 TETRAMERIZATION DOMAIN ( CRYSTAL FORM II)
REMARK 900 RELATED ID: 1COK RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C-TERMINAL DOMAIN OF P73
DBREF 4A63 A 112 311 UNP O15350 P73_HUMAN 112 311
DBREF 4A63 B 892 1128 UNP Q13625 ASPP2_HUMAN 892 1128
DBREF 4A63 C 112 311 UNP O15350 P73_HUMAN 112 311
DBREF 4A63 D 892 1128 UNP Q13625 ASPP2_HUMAN 892 1128
DBREF 4A63 E 112 311 UNP O15350 P73_HUMAN 112 311
DBREF 4A63 F 892 1128 UNP Q13625 ASPP2_HUMAN 892 1128
DBREF 4A63 G 112 311 UNP O15350 P73_HUMAN 112 311
DBREF 4A63 H 892 1128 UNP Q13625 ASPP2_HUMAN 892 1128
DBREF 4A63 I 112 311 UNP O15350 P73_HUMAN 112 311
DBREF 4A63 J 892 1128 UNP Q13625 ASPP2_HUMAN 892 1128
DBREF 4A63 K 112 311 UNP O15350 P73_HUMAN 112 311
DBREF 4A63 L 892 1128 UNP Q13625 ASPP2_HUMAN 892 1128
SEQADV 4A63 MET A 111 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ALA A 312 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLU A 313 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ASN A 314 UNP O15350 EXPRESSION TAG
SEQADV 4A63 LEU A 315 UNP O15350 EXPRESSION TAG
SEQADV 4A63 TYR A 316 UNP O15350 EXPRESSION TAG
SEQADV 4A63 PHE A 317 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLN A 318 UNP O15350 EXPRESSION TAG
SEQADV 4A63 SER B 890 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET B 891 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET C 111 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ALA C 312 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLU C 313 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ASN C 314 UNP O15350 EXPRESSION TAG
SEQADV 4A63 LEU C 315 UNP O15350 EXPRESSION TAG
SEQADV 4A63 TYR C 316 UNP O15350 EXPRESSION TAG
SEQADV 4A63 PHE C 317 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLN C 318 UNP O15350 EXPRESSION TAG
SEQADV 4A63 SER D 890 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET D 891 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET E 111 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ALA E 312 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLU E 313 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ASN E 314 UNP O15350 EXPRESSION TAG
SEQADV 4A63 LEU E 315 UNP O15350 EXPRESSION TAG
SEQADV 4A63 TYR E 316 UNP O15350 EXPRESSION TAG
SEQADV 4A63 PHE E 317 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLN E 318 UNP O15350 EXPRESSION TAG
SEQADV 4A63 SER F 890 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET F 891 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET G 111 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ALA G 312 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLU G 313 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ASN G 314 UNP O15350 EXPRESSION TAG
SEQADV 4A63 LEU G 315 UNP O15350 EXPRESSION TAG
SEQADV 4A63 TYR G 316 UNP O15350 EXPRESSION TAG
SEQADV 4A63 PHE G 317 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLN G 318 UNP O15350 EXPRESSION TAG
SEQADV 4A63 SER H 890 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET H 891 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET I 111 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ALA I 312 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLU I 313 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ASN I 314 UNP O15350 EXPRESSION TAG
SEQADV 4A63 LEU I 315 UNP O15350 EXPRESSION TAG
SEQADV 4A63 TYR I 316 UNP O15350 EXPRESSION TAG
SEQADV 4A63 PHE I 317 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLN I 318 UNP O15350 EXPRESSION TAG
SEQADV 4A63 SER J 890 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET J 891 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET K 111 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ALA K 312 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLU K 313 UNP O15350 EXPRESSION TAG
SEQADV 4A63 ASN K 314 UNP O15350 EXPRESSION TAG
SEQADV 4A63 LEU K 315 UNP O15350 EXPRESSION TAG
SEQADV 4A63 TYR K 316 UNP O15350 EXPRESSION TAG
SEQADV 4A63 PHE K 317 UNP O15350 EXPRESSION TAG
SEQADV 4A63 GLN K 318 UNP O15350 EXPRESSION TAG
SEQADV 4A63 SER L 890 UNP Q13625 EXPRESSION TAG
SEQADV 4A63 MET L 891 UNP Q13625 EXPRESSION TAG
SEQRES 1 A 208 MET ALA PRO VAL ILE PRO SER ASN THR ASP TYR PRO GLY
SEQRES 2 A 208 PRO HIS HIS PHE GLU VAL THR PHE GLN GLN SER SER THR
SEQRES 3 A 208 ALA LYS SER ALA THR TRP THR TYR SER PRO LEU LEU LYS
SEQRES 4 A 208 LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE GLN
SEQRES 5 A 208 ILE LYS VAL SER THR PRO PRO PRO PRO GLY THR ALA ILE
SEQRES 6 A 208 ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL THR
SEQRES 7 A 208 ASP VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU GLY ARG
SEQRES 8 A 208 ASP PHE ASN GLU GLY GLN SER ALA PRO ALA SER HIS LEU
SEQRES 9 A 208 ILE ARG VAL GLU GLY ASN ASN LEU SER GLN TYR VAL ASP
SEQRES 10 A 208 ASP PRO VAL THR GLY ARG GLN SER VAL VAL VAL PRO TYR
SEQRES 11 A 208 GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR ILE LEU
SEQRES 12 A 208 TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY MET
SEQRES 13 A 208 ASN ARG ARG PRO ILE LEU ILE ILE ILE THR LEU GLU MET
SEQRES 14 A 208 ARG ASP GLY GLN VAL LEU GLY ARG ARG SER PHE GLU GLY
SEQRES 15 A 208 ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA ASP
SEQRES 16 A 208 GLU ASP HIS TYR ARG GLU ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 B 239 SER MET PRO GLU ILE THR GLY GLN VAL SER LEU PRO PRO
SEQRES 2 B 239 GLY LYS ARG THR ASN LEU ARG LYS THR GLY SER GLU ARG
SEQRES 3 B 239 ILE ALA HIS GLY MET ARG VAL LYS PHE ASN PRO LEU ALA
SEQRES 4 B 239 LEU LEU LEU ASP SER SER LEU GLU GLY GLU PHE ASP LEU
SEQRES 5 B 239 VAL GLN ARG ILE ILE TYR GLU VAL ASP ASP PRO SER LEU
SEQRES 6 B 239 PRO ASN ASP GLU GLY ILE THR ALA LEU HIS ASN ALA VAL
SEQRES 7 B 239 CYS ALA GLY HIS THR GLU ILE VAL LYS PHE LEU VAL GLN
SEQRES 8 B 239 PHE GLY VAL ASN VAL ASN ALA ALA ASP SER ASP GLY TRP
SEQRES 9 B 239 THR PRO LEU HIS CYS ALA ALA SER CYS ASN ASN VAL GLN
SEQRES 10 B 239 VAL CYS LYS PHE LEU VAL GLU SER GLY ALA ALA VAL PHE
SEQRES 11 B 239 ALA MET THR TYR SER ASP MET GLN THR ALA ALA ASP LYS
SEQRES 12 B 239 CYS GLU GLU MET GLU GLU GLY TYR THR GLN CYS SER GLN
SEQRES 13 B 239 PHE LEU TYR GLY VAL GLN GLU LYS MET GLY ILE MET ASN
SEQRES 14 B 239 LYS GLY VAL ILE TYR ALA LEU TRP ASP TYR GLU PRO GLN
SEQRES 15 B 239 ASN ASP ASP GLU LEU PRO MET LYS GLU GLY ASP CYS MET
SEQRES 16 B 239 THR ILE ILE HIS ARG GLU ASP GLU ASP GLU ILE GLU TRP
SEQRES 17 B 239 TRP TRP ALA ARG LEU ASN ASP LYS GLU GLY TYR VAL PRO
SEQRES 18 B 239 ARG ASN LEU LEU GLY LEU TYR PRO ARG ILE LYS PRO ARG
SEQRES 19 B 239 GLN ARG SER LEU ALA
SEQRES 1 C 208 MET ALA PRO VAL ILE PRO SER ASN THR ASP TYR PRO GLY
SEQRES 2 C 208 PRO HIS HIS PHE GLU VAL THR PHE GLN GLN SER SER THR
SEQRES 3 C 208 ALA LYS SER ALA THR TRP THR TYR SER PRO LEU LEU LYS
SEQRES 4 C 208 LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE GLN
SEQRES 5 C 208 ILE LYS VAL SER THR PRO PRO PRO PRO GLY THR ALA ILE
SEQRES 6 C 208 ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL THR
SEQRES 7 C 208 ASP VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU GLY ARG
SEQRES 8 C 208 ASP PHE ASN GLU GLY GLN SER ALA PRO ALA SER HIS LEU
SEQRES 9 C 208 ILE ARG VAL GLU GLY ASN ASN LEU SER GLN TYR VAL ASP
SEQRES 10 C 208 ASP PRO VAL THR GLY ARG GLN SER VAL VAL VAL PRO TYR
SEQRES 11 C 208 GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR ILE LEU
SEQRES 12 C 208 TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY MET
SEQRES 13 C 208 ASN ARG ARG PRO ILE LEU ILE ILE ILE THR LEU GLU MET
SEQRES 14 C 208 ARG ASP GLY GLN VAL LEU GLY ARG ARG SER PHE GLU GLY
SEQRES 15 C 208 ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA ASP
SEQRES 16 C 208 GLU ASP HIS TYR ARG GLU ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 D 239 SER MET PRO GLU ILE THR GLY GLN VAL SER LEU PRO PRO
SEQRES 2 D 239 GLY LYS ARG THR ASN LEU ARG LYS THR GLY SER GLU ARG
SEQRES 3 D 239 ILE ALA HIS GLY MET ARG VAL LYS PHE ASN PRO LEU ALA
SEQRES 4 D 239 LEU LEU LEU ASP SER SER LEU GLU GLY GLU PHE ASP LEU
SEQRES 5 D 239 VAL GLN ARG ILE ILE TYR GLU VAL ASP ASP PRO SER LEU
SEQRES 6 D 239 PRO ASN ASP GLU GLY ILE THR ALA LEU HIS ASN ALA VAL
SEQRES 7 D 239 CYS ALA GLY HIS THR GLU ILE VAL LYS PHE LEU VAL GLN
SEQRES 8 D 239 PHE GLY VAL ASN VAL ASN ALA ALA ASP SER ASP GLY TRP
SEQRES 9 D 239 THR PRO LEU HIS CYS ALA ALA SER CYS ASN ASN VAL GLN
SEQRES 10 D 239 VAL CYS LYS PHE LEU VAL GLU SER GLY ALA ALA VAL PHE
SEQRES 11 D 239 ALA MET THR TYR SER ASP MET GLN THR ALA ALA ASP LYS
SEQRES 12 D 239 CYS GLU GLU MET GLU GLU GLY TYR THR GLN CYS SER GLN
SEQRES 13 D 239 PHE LEU TYR GLY VAL GLN GLU LYS MET GLY ILE MET ASN
SEQRES 14 D 239 LYS GLY VAL ILE TYR ALA LEU TRP ASP TYR GLU PRO GLN
SEQRES 15 D 239 ASN ASP ASP GLU LEU PRO MET LYS GLU GLY ASP CYS MET
SEQRES 16 D 239 THR ILE ILE HIS ARG GLU ASP GLU ASP GLU ILE GLU TRP
SEQRES 17 D 239 TRP TRP ALA ARG LEU ASN ASP LYS GLU GLY TYR VAL PRO
SEQRES 18 D 239 ARG ASN LEU LEU GLY LEU TYR PRO ARG ILE LYS PRO ARG
SEQRES 19 D 239 GLN ARG SER LEU ALA
SEQRES 1 E 208 MET ALA PRO VAL ILE PRO SER ASN THR ASP TYR PRO GLY
SEQRES 2 E 208 PRO HIS HIS PHE GLU VAL THR PHE GLN GLN SER SER THR
SEQRES 3 E 208 ALA LYS SER ALA THR TRP THR TYR SER PRO LEU LEU LYS
SEQRES 4 E 208 LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE GLN
SEQRES 5 E 208 ILE LYS VAL SER THR PRO PRO PRO PRO GLY THR ALA ILE
SEQRES 6 E 208 ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL THR
SEQRES 7 E 208 ASP VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU GLY ARG
SEQRES 8 E 208 ASP PHE ASN GLU GLY GLN SER ALA PRO ALA SER HIS LEU
SEQRES 9 E 208 ILE ARG VAL GLU GLY ASN ASN LEU SER GLN TYR VAL ASP
SEQRES 10 E 208 ASP PRO VAL THR GLY ARG GLN SER VAL VAL VAL PRO TYR
SEQRES 11 E 208 GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR ILE LEU
SEQRES 12 E 208 TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY MET
SEQRES 13 E 208 ASN ARG ARG PRO ILE LEU ILE ILE ILE THR LEU GLU MET
SEQRES 14 E 208 ARG ASP GLY GLN VAL LEU GLY ARG ARG SER PHE GLU GLY
SEQRES 15 E 208 ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA ASP
SEQRES 16 E 208 GLU ASP HIS TYR ARG GLU ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 F 239 SER MET PRO GLU ILE THR GLY GLN VAL SER LEU PRO PRO
SEQRES 2 F 239 GLY LYS ARG THR ASN LEU ARG LYS THR GLY SER GLU ARG
SEQRES 3 F 239 ILE ALA HIS GLY MET ARG VAL LYS PHE ASN PRO LEU ALA
SEQRES 4 F 239 LEU LEU LEU ASP SER SER LEU GLU GLY GLU PHE ASP LEU
SEQRES 5 F 239 VAL GLN ARG ILE ILE TYR GLU VAL ASP ASP PRO SER LEU
SEQRES 6 F 239 PRO ASN ASP GLU GLY ILE THR ALA LEU HIS ASN ALA VAL
SEQRES 7 F 239 CYS ALA GLY HIS THR GLU ILE VAL LYS PHE LEU VAL GLN
SEQRES 8 F 239 PHE GLY VAL ASN VAL ASN ALA ALA ASP SER ASP GLY TRP
SEQRES 9 F 239 THR PRO LEU HIS CYS ALA ALA SER CYS ASN ASN VAL GLN
SEQRES 10 F 239 VAL CYS LYS PHE LEU VAL GLU SER GLY ALA ALA VAL PHE
SEQRES 11 F 239 ALA MET THR TYR SER ASP MET GLN THR ALA ALA ASP LYS
SEQRES 12 F 239 CYS GLU GLU MET GLU GLU GLY TYR THR GLN CYS SER GLN
SEQRES 13 F 239 PHE LEU TYR GLY VAL GLN GLU LYS MET GLY ILE MET ASN
SEQRES 14 F 239 LYS GLY VAL ILE TYR ALA LEU TRP ASP TYR GLU PRO GLN
SEQRES 15 F 239 ASN ASP ASP GLU LEU PRO MET LYS GLU GLY ASP CYS MET
SEQRES 16 F 239 THR ILE ILE HIS ARG GLU ASP GLU ASP GLU ILE GLU TRP
SEQRES 17 F 239 TRP TRP ALA ARG LEU ASN ASP LYS GLU GLY TYR VAL PRO
SEQRES 18 F 239 ARG ASN LEU LEU GLY LEU TYR PRO ARG ILE LYS PRO ARG
SEQRES 19 F 239 GLN ARG SER LEU ALA
SEQRES 1 G 208 MET ALA PRO VAL ILE PRO SER ASN THR ASP TYR PRO GLY
SEQRES 2 G 208 PRO HIS HIS PHE GLU VAL THR PHE GLN GLN SER SER THR
SEQRES 3 G 208 ALA LYS SER ALA THR TRP THR TYR SER PRO LEU LEU LYS
SEQRES 4 G 208 LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE GLN
SEQRES 5 G 208 ILE LYS VAL SER THR PRO PRO PRO PRO GLY THR ALA ILE
SEQRES 6 G 208 ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL THR
SEQRES 7 G 208 ASP VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU GLY ARG
SEQRES 8 G 208 ASP PHE ASN GLU GLY GLN SER ALA PRO ALA SER HIS LEU
SEQRES 9 G 208 ILE ARG VAL GLU GLY ASN ASN LEU SER GLN TYR VAL ASP
SEQRES 10 G 208 ASP PRO VAL THR GLY ARG GLN SER VAL VAL VAL PRO TYR
SEQRES 11 G 208 GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR ILE LEU
SEQRES 12 G 208 TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY MET
SEQRES 13 G 208 ASN ARG ARG PRO ILE LEU ILE ILE ILE THR LEU GLU MET
SEQRES 14 G 208 ARG ASP GLY GLN VAL LEU GLY ARG ARG SER PHE GLU GLY
SEQRES 15 G 208 ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA ASP
SEQRES 16 G 208 GLU ASP HIS TYR ARG GLU ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 H 239 SER MET PRO GLU ILE THR GLY GLN VAL SER LEU PRO PRO
SEQRES 2 H 239 GLY LYS ARG THR ASN LEU ARG LYS THR GLY SER GLU ARG
SEQRES 3 H 239 ILE ALA HIS GLY MET ARG VAL LYS PHE ASN PRO LEU ALA
SEQRES 4 H 239 LEU LEU LEU ASP SER SER LEU GLU GLY GLU PHE ASP LEU
SEQRES 5 H 239 VAL GLN ARG ILE ILE TYR GLU VAL ASP ASP PRO SER LEU
SEQRES 6 H 239 PRO ASN ASP GLU GLY ILE THR ALA LEU HIS ASN ALA VAL
SEQRES 7 H 239 CYS ALA GLY HIS THR GLU ILE VAL LYS PHE LEU VAL GLN
SEQRES 8 H 239 PHE GLY VAL ASN VAL ASN ALA ALA ASP SER ASP GLY TRP
SEQRES 9 H 239 THR PRO LEU HIS CYS ALA ALA SER CYS ASN ASN VAL GLN
SEQRES 10 H 239 VAL CYS LYS PHE LEU VAL GLU SER GLY ALA ALA VAL PHE
SEQRES 11 H 239 ALA MET THR TYR SER ASP MET GLN THR ALA ALA ASP LYS
SEQRES 12 H 239 CYS GLU GLU MET GLU GLU GLY TYR THR GLN CYS SER GLN
SEQRES 13 H 239 PHE LEU TYR GLY VAL GLN GLU LYS MET GLY ILE MET ASN
SEQRES 14 H 239 LYS GLY VAL ILE TYR ALA LEU TRP ASP TYR GLU PRO GLN
SEQRES 15 H 239 ASN ASP ASP GLU LEU PRO MET LYS GLU GLY ASP CYS MET
SEQRES 16 H 239 THR ILE ILE HIS ARG GLU ASP GLU ASP GLU ILE GLU TRP
SEQRES 17 H 239 TRP TRP ALA ARG LEU ASN ASP LYS GLU GLY TYR VAL PRO
SEQRES 18 H 239 ARG ASN LEU LEU GLY LEU TYR PRO ARG ILE LYS PRO ARG
SEQRES 19 H 239 GLN ARG SER LEU ALA
SEQRES 1 I 208 MET ALA PRO VAL ILE PRO SER ASN THR ASP TYR PRO GLY
SEQRES 2 I 208 PRO HIS HIS PHE GLU VAL THR PHE GLN GLN SER SER THR
SEQRES 3 I 208 ALA LYS SER ALA THR TRP THR TYR SER PRO LEU LEU LYS
SEQRES 4 I 208 LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE GLN
SEQRES 5 I 208 ILE LYS VAL SER THR PRO PRO PRO PRO GLY THR ALA ILE
SEQRES 6 I 208 ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL THR
SEQRES 7 I 208 ASP VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU GLY ARG
SEQRES 8 I 208 ASP PHE ASN GLU GLY GLN SER ALA PRO ALA SER HIS LEU
SEQRES 9 I 208 ILE ARG VAL GLU GLY ASN ASN LEU SER GLN TYR VAL ASP
SEQRES 10 I 208 ASP PRO VAL THR GLY ARG GLN SER VAL VAL VAL PRO TYR
SEQRES 11 I 208 GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR ILE LEU
SEQRES 12 I 208 TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY MET
SEQRES 13 I 208 ASN ARG ARG PRO ILE LEU ILE ILE ILE THR LEU GLU MET
SEQRES 14 I 208 ARG ASP GLY GLN VAL LEU GLY ARG ARG SER PHE GLU GLY
SEQRES 15 I 208 ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA ASP
SEQRES 16 I 208 GLU ASP HIS TYR ARG GLU ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 J 239 SER MET PRO GLU ILE THR GLY GLN VAL SER LEU PRO PRO
SEQRES 2 J 239 GLY LYS ARG THR ASN LEU ARG LYS THR GLY SER GLU ARG
SEQRES 3 J 239 ILE ALA HIS GLY MET ARG VAL LYS PHE ASN PRO LEU ALA
SEQRES 4 J 239 LEU LEU LEU ASP SER SER LEU GLU GLY GLU PHE ASP LEU
SEQRES 5 J 239 VAL GLN ARG ILE ILE TYR GLU VAL ASP ASP PRO SER LEU
SEQRES 6 J 239 PRO ASN ASP GLU GLY ILE THR ALA LEU HIS ASN ALA VAL
SEQRES 7 J 239 CYS ALA GLY HIS THR GLU ILE VAL LYS PHE LEU VAL GLN
SEQRES 8 J 239 PHE GLY VAL ASN VAL ASN ALA ALA ASP SER ASP GLY TRP
SEQRES 9 J 239 THR PRO LEU HIS CYS ALA ALA SER CYS ASN ASN VAL GLN
SEQRES 10 J 239 VAL CYS LYS PHE LEU VAL GLU SER GLY ALA ALA VAL PHE
SEQRES 11 J 239 ALA MET THR TYR SER ASP MET GLN THR ALA ALA ASP LYS
SEQRES 12 J 239 CYS GLU GLU MET GLU GLU GLY TYR THR GLN CYS SER GLN
SEQRES 13 J 239 PHE LEU TYR GLY VAL GLN GLU LYS MET GLY ILE MET ASN
SEQRES 14 J 239 LYS GLY VAL ILE TYR ALA LEU TRP ASP TYR GLU PRO GLN
SEQRES 15 J 239 ASN ASP ASP GLU LEU PRO MET LYS GLU GLY ASP CYS MET
SEQRES 16 J 239 THR ILE ILE HIS ARG GLU ASP GLU ASP GLU ILE GLU TRP
SEQRES 17 J 239 TRP TRP ALA ARG LEU ASN ASP LYS GLU GLY TYR VAL PRO
SEQRES 18 J 239 ARG ASN LEU LEU GLY LEU TYR PRO ARG ILE LYS PRO ARG
SEQRES 19 J 239 GLN ARG SER LEU ALA
SEQRES 1 K 208 MET ALA PRO VAL ILE PRO SER ASN THR ASP TYR PRO GLY
SEQRES 2 K 208 PRO HIS HIS PHE GLU VAL THR PHE GLN GLN SER SER THR
SEQRES 3 K 208 ALA LYS SER ALA THR TRP THR TYR SER PRO LEU LEU LYS
SEQRES 4 K 208 LYS LEU TYR CYS GLN ILE ALA LYS THR CYS PRO ILE GLN
SEQRES 5 K 208 ILE LYS VAL SER THR PRO PRO PRO PRO GLY THR ALA ILE
SEQRES 6 K 208 ARG ALA MET PRO VAL TYR LYS LYS ALA GLU HIS VAL THR
SEQRES 7 K 208 ASP VAL VAL LYS ARG CYS PRO ASN HIS GLU LEU GLY ARG
SEQRES 8 K 208 ASP PHE ASN GLU GLY GLN SER ALA PRO ALA SER HIS LEU
SEQRES 9 K 208 ILE ARG VAL GLU GLY ASN ASN LEU SER GLN TYR VAL ASP
SEQRES 10 K 208 ASP PRO VAL THR GLY ARG GLN SER VAL VAL VAL PRO TYR
SEQRES 11 K 208 GLU PRO PRO GLN VAL GLY THR GLU PHE THR THR ILE LEU
SEQRES 12 K 208 TYR ASN PHE MET CYS ASN SER SER CYS VAL GLY GLY MET
SEQRES 13 K 208 ASN ARG ARG PRO ILE LEU ILE ILE ILE THR LEU GLU MET
SEQRES 14 K 208 ARG ASP GLY GLN VAL LEU GLY ARG ARG SER PHE GLU GLY
SEQRES 15 K 208 ARG ILE CYS ALA CYS PRO GLY ARG ASP ARG LYS ALA ASP
SEQRES 16 K 208 GLU ASP HIS TYR ARG GLU ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 L 239 SER MET PRO GLU ILE THR GLY GLN VAL SER LEU PRO PRO
SEQRES 2 L 239 GLY LYS ARG THR ASN LEU ARG LYS THR GLY SER GLU ARG
SEQRES 3 L 239 ILE ALA HIS GLY MET ARG VAL LYS PHE ASN PRO LEU ALA
SEQRES 4 L 239 LEU LEU LEU ASP SER SER LEU GLU GLY GLU PHE ASP LEU
SEQRES 5 L 239 VAL GLN ARG ILE ILE TYR GLU VAL ASP ASP PRO SER LEU
SEQRES 6 L 239 PRO ASN ASP GLU GLY ILE THR ALA LEU HIS ASN ALA VAL
SEQRES 7 L 239 CYS ALA GLY HIS THR GLU ILE VAL LYS PHE LEU VAL GLN
SEQRES 8 L 239 PHE GLY VAL ASN VAL ASN ALA ALA ASP SER ASP GLY TRP
SEQRES 9 L 239 THR PRO LEU HIS CYS ALA ALA SER CYS ASN ASN VAL GLN
SEQRES 10 L 239 VAL CYS LYS PHE LEU VAL GLU SER GLY ALA ALA VAL PHE
SEQRES 11 L 239 ALA MET THR TYR SER ASP MET GLN THR ALA ALA ASP LYS
SEQRES 12 L 239 CYS GLU GLU MET GLU GLU GLY TYR THR GLN CYS SER GLN
SEQRES 13 L 239 PHE LEU TYR GLY VAL GLN GLU LYS MET GLY ILE MET ASN
SEQRES 14 L 239 LYS GLY VAL ILE TYR ALA LEU TRP ASP TYR GLU PRO GLN
SEQRES 15 L 239 ASN ASP ASP GLU LEU PRO MET LYS GLU GLY ASP CYS MET
SEQRES 16 L 239 THR ILE ILE HIS ARG GLU ASP GLU ASP GLU ILE GLU TRP
SEQRES 17 L 239 TRP TRP ALA ARG LEU ASN ASP LYS GLU GLY TYR VAL PRO
SEQRES 18 L 239 ARG ASN LEU LEU GLY LEU TYR PRO ARG ILE LYS PRO ARG
SEQRES 19 L 239 GLN ARG SER LEU ALA
HET ZN C 1 1
HET ACT C1319 7
HET ACT C1320 7
HET ACT C1321 7
HET ZN E 1 1
HET ZN G 1 1
HET ACT G1319 7
HET ZN I 1 1
HET ACT I1319 7
HET ACT I1320 7
HET ZN K 1 1
HET ACT K1319 7
HET ACT K1320 7
HET ACT L1522 7
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
FORMUL 13 ZN 5(ZN 2+)
FORMUL 14 ACT 9(C2 H3 O2 1-)
FORMUL 27 HOH *671(H2 O)
HELIX 1 1 CYS A 194 GLY A 200 1 7
HELIX 2 2 CYS A 297 GLU A 313 1 17
HELIX 3 3 ASN B 925 GLY B 937 1 13
HELIX 4 4 GLU B 938 ILE B 946 1 9
HELIX 5 5 TYR B 947 VAL B 949 5 3
HELIX 6 6 THR B 961 ALA B 969 1 9
HELIX 7 7 HIS B 971 GLY B 982 1 12
HELIX 8 8 THR B 994 CYS B 1002 1 9
HELIX 9 9 ASN B 1004 SER B 1014 1 11
HELIX 10 10 THR B 1028 CYS B 1033 5 6
HELIX 11 11 GLY B 1039 MET B 1054 1 16
HELIX 12 12 MET B 1057 LYS B 1059 5 3
HELIX 13 13 CYS C 194 GLY C 200 1 7
HELIX 14 14 CYS C 297 GLU C 313 1 17
HELIX 15 15 ASN D 925 GLY D 937 1 13
HELIX 16 16 GLU D 938 ILE D 946 1 9
HELIX 17 17 THR D 961 ALA D 969 1 9
HELIX 18 18 HIS D 971 GLY D 982 1 12
HELIX 19 19 THR D 994 CYS D 1002 1 9
HELIX 20 20 ASN D 1004 SER D 1014 1 11
HELIX 21 21 THR D 1028 CYS D 1033 5 6
HELIX 22 22 GLY D 1039 MET D 1054 1 16
HELIX 23 23 MET D 1057 LYS D 1059 5 3
HELIX 24 24 CYS E 194 GLY E 200 1 7
HELIX 25 25 CYS E 297 GLU E 313 1 17
HELIX 26 26 ASN F 925 GLY F 937 1 13
HELIX 27 27 GLU F 938 ILE F 946 1 9
HELIX 28 28 THR F 961 ALA F 969 1 9
HELIX 29 29 HIS F 971 GLY F 982 1 12
HELIX 30 30 THR F 994 CYS F 1002 1 9
HELIX 31 31 ASN F 1004 SER F 1014 1 11
HELIX 32 32 THR F 1028 CYS F 1033 5 6
HELIX 33 33 GLY F 1039 MET F 1054 1 16
HELIX 34 34 MET F 1057 LYS F 1059 5 3
HELIX 35 35 CYS G 194 GLY G 200 1 7
HELIX 36 36 CYS G 297 GLU G 313 1 17
HELIX 37 37 ASN H 925 GLY H 937 1 13
HELIX 38 38 GLU H 938 ILE H 946 1 9
HELIX 39 39 THR H 961 GLY H 970 1 10
HELIX 40 40 HIS H 971 GLY H 982 1 12
HELIX 41 41 THR H 994 CYS H 1002 1 9
HELIX 42 42 ASN H 1004 SER H 1014 1 11
HELIX 43 43 ALA H 1029 CYS H 1033 5 5
HELIX 44 44 GLY H 1039 MET H 1054 1 16
HELIX 45 45 MET H 1057 LYS H 1059 5 3
HELIX 46 46 CYS I 194 GLY I 200 1 7
HELIX 47 47 CYS I 297 GLU I 313 1 17
HELIX 48 48 ASN J 925 GLY J 937 1 13
HELIX 49 49 GLU J 938 ILE J 946 1 9
HELIX 50 50 TYR J 947 VAL J 949 5 3
HELIX 51 51 THR J 961 GLY J 970 1 10
HELIX 52 52 HIS J 971 GLY J 982 1 12
HELIX 53 53 THR J 994 CYS J 1002 1 9
HELIX 54 54 ASN J 1004 SER J 1014 1 11
HELIX 55 55 THR J 1028 CYS J 1033 5 6
HELIX 56 56 GLY J 1039 MET J 1054 1 16
HELIX 57 57 MET J 1057 LYS J 1059 5 3
HELIX 58 58 CYS K 194 GLY K 200 1 7
HELIX 59 59 CYS K 297 GLU K 313 1 17
HELIX 60 60 ASN L 925 GLY L 937 1 13
HELIX 61 61 GLU L 938 ILE L 946 1 9
HELIX 62 62 THR L 961 ALA L 969 1 9
HELIX 63 63 HIS L 971 GLY L 982 1 12
HELIX 64 64 THR L 994 CYS L 1002 1 9
HELIX 65 65 ASN L 1004 SER L 1014 1 11
HELIX 66 66 THR L 1028 CYS L 1033 5 6
HELIX 67 67 GLY L 1039 MET L 1054 1 16
HELIX 68 68 MET L 1057 LYS L 1059 5 3
SHEET 1 AA 4 GLU A 128 THR A 130 0
SHEET 2 AA 4 CYS A 159 LYS A 164 -1 O GLN A 162 N THR A 130
SHEET 3 AA 4 THR A 250 PHE A 256 -1 O THR A 250 N ILE A 163
SHEET 4 AA 4 ILE A 215 GLU A 218 -1 O ARG A 216 N ASN A 255
SHEET 1 AB 7 TRP A 142 SER A 145 0
SHEET 2 AB 7 LYS A 150 CYS A 153 -1 O LYS A 150 N SER A 145
SHEET 3 AB 7 VAL A 284 ILE A 294 1 O GLU A 291 N LEU A 151
SHEET 4 AB 7 ILE A 271 GLU A 278 -1 O ILE A 271 N GLY A 292
SHEET 5 AB 7 ALA A 174 TYR A 181 -1 O ALA A 174 N GLU A 278
SHEET 6 AB 7 GLN A 234 PRO A 239 -1 O VAL A 236 N ALA A 177
SHEET 7 AB 7 GLN A 224 ASP A 227 -1 O GLN A 224 N VAL A 237
SHEET 1 BA 5 LYS B1105 PRO B1110 0
SHEET 2 BA 5 TRP B1097 LEU B1102 -1 O TRP B1098 N VAL B1109
SHEET 3 BA 5 CYS B1083 HIS B1088 -1 O THR B1085 N ARG B1101
SHEET 4 BA 5 VAL B1061 ALA B1064 -1 O ILE B1062 N MET B1084
SHEET 5 BA 5 LEU B1114 GLY B1115 -1 O GLY B1115 N TYR B1063
SHEET 1 CA 4 GLU C 128 THR C 130 0
SHEET 2 CA 4 CYS C 159 LYS C 164 -1 O GLN C 162 N THR C 130
SHEET 3 CA 4 THR C 250 PHE C 256 -1 O THR C 250 N ILE C 163
SHEET 4 CA 4 ILE C 215 GLU C 218 -1 O ARG C 216 N ASN C 255
SHEET 1 CB 7 TRP C 142 SER C 145 0
SHEET 2 CB 7 LYS C 150 CYS C 153 -1 O LYS C 150 N SER C 145
SHEET 3 CB 7 VAL C 284 ILE C 294 1 O GLU C 291 N LEU C 151
SHEET 4 CB 7 ILE C 271 GLU C 278 -1 O ILE C 271 N GLY C 292
SHEET 5 CB 7 ALA C 174 TYR C 181 -1 O ALA C 174 N GLU C 278
SHEET 6 CB 7 GLN C 234 PRO C 239 -1 O VAL C 236 N ALA C 177
SHEET 7 CB 7 GLN C 224 ASP C 227 -1 O GLN C 224 N VAL C 237
SHEET 1 DA 5 LYS D1105 PRO D1110 0
SHEET 2 DA 5 TRP D1097 LEU D1102 -1 O TRP D1098 N VAL D1109
SHEET 3 DA 5 CYS D1083 HIS D1088 -1 O THR D1085 N ARG D1101
SHEET 4 DA 5 VAL D1061 ALA D1064 -1 O ILE D1062 N MET D1084
SHEET 5 DA 5 LEU D1114 GLY D1115 -1 O GLY D1115 N TYR D1063
SHEET 1 EA 4 GLU E 128 THR E 130 0
SHEET 2 EA 4 CYS E 159 LYS E 164 -1 O GLN E 162 N THR E 130
SHEET 3 EA 4 THR E 250 PHE E 256 -1 O THR E 250 N ILE E 163
SHEET 4 EA 4 ILE E 215 GLU E 218 -1 O ARG E 216 N ASN E 255
SHEET 1 EB 7 TRP E 142 SER E 145 0
SHEET 2 EB 7 LYS E 150 CYS E 153 -1 O LYS E 150 N SER E 145
SHEET 3 EB 7 VAL E 284 ILE E 294 1 O GLU E 291 N LEU E 151
SHEET 4 EB 7 ILE E 271 GLU E 278 -1 O ILE E 271 N GLY E 292
SHEET 5 EB 7 ALA E 174 TYR E 181 -1 O ALA E 174 N GLU E 278
SHEET 6 EB 7 GLN E 234 PRO E 239 -1 O VAL E 236 N ALA E 177
SHEET 7 EB 7 GLN E 224 ASP E 227 -1 O GLN E 224 N VAL E 237
SHEET 1 FA 5 LYS F1105 PRO F1110 0
SHEET 2 FA 5 TRP F1097 LEU F1102 -1 O TRP F1098 N VAL F1109
SHEET 3 FA 5 CYS F1083 HIS F1088 -1 O THR F1085 N ARG F1101
SHEET 4 FA 5 VAL F1061 ALA F1064 -1 O ILE F1062 N MET F1084
SHEET 5 FA 5 LEU F1114 GLY F1115 -1 O GLY F1115 N TYR F1063
SHEET 1 GA 4 GLU G 128 THR G 130 0
SHEET 2 GA 4 CYS G 159 LYS G 164 -1 O GLN G 162 N THR G 130
SHEET 3 GA 4 THR G 250 PHE G 256 -1 O THR G 250 N ILE G 163
SHEET 4 GA 4 ILE G 215 GLU G 218 -1 O ARG G 216 N ASN G 255
SHEET 1 GB 7 TRP G 142 SER G 145 0
SHEET 2 GB 7 LYS G 150 CYS G 153 -1 O LYS G 150 N SER G 145
SHEET 3 GB 7 VAL G 284 ILE G 294 1 O GLU G 291 N LEU G 151
SHEET 4 GB 7 ILE G 271 GLU G 278 -1 O ILE G 271 N GLY G 292
SHEET 5 GB 7 ALA G 174 TYR G 181 -1 O ALA G 174 N GLU G 278
SHEET 6 GB 7 GLN G 234 PRO G 239 -1 O VAL G 236 N ALA G 177
SHEET 7 GB 7 GLN G 224 ASP G 227 -1 O GLN G 224 N VAL G 237
SHEET 1 HA 5 LYS H1105 PRO H1110 0
SHEET 2 HA 5 TRP H1097 LEU H1102 -1 O TRP H1098 N VAL H1109
SHEET 3 HA 5 CYS H1083 HIS H1088 -1 O THR H1085 N ARG H1101
SHEET 4 HA 5 VAL H1061 ALA H1064 -1 O ILE H1062 N MET H1084
SHEET 5 HA 5 LEU H1114 GLY H1115 -1 O GLY H1115 N TYR H1063
SHEET 1 IA 4 GLU I 128 THR I 130 0
SHEET 2 IA 4 CYS I 159 LYS I 164 -1 O GLN I 162 N THR I 130
SHEET 3 IA 4 THR I 250 PHE I 256 -1 O THR I 250 N ILE I 163
SHEET 4 IA 4 ILE I 215 GLU I 218 -1 O ARG I 216 N ASN I 255
SHEET 1 IB 7 TRP I 142 SER I 145 0
SHEET 2 IB 7 LYS I 150 CYS I 153 -1 O LYS I 150 N SER I 145
SHEET 3 IB 7 VAL I 284 ILE I 294 1 O GLU I 291 N LEU I 151
SHEET 4 IB 7 ILE I 271 GLU I 278 -1 O ILE I 271 N GLY I 292
SHEET 5 IB 7 ALA I 174 TYR I 181 -1 O ALA I 174 N GLU I 278
SHEET 6 IB 7 GLN I 234 PRO I 239 -1 O VAL I 236 N ALA I 177
SHEET 7 IB 7 GLN I 224 ASP I 227 -1 O GLN I 224 N VAL I 237
SHEET 1 JA 5 LYS J1105 PRO J1110 0
SHEET 2 JA 5 TRP J1097 LEU J1102 -1 O TRP J1098 N VAL J1109
SHEET 3 JA 5 CYS J1083 HIS J1088 -1 O THR J1085 N ARG J1101
SHEET 4 JA 5 VAL J1061 ALA J1064 -1 O ILE J1062 N MET J1084
SHEET 5 JA 5 LEU J1114 GLY J1115 -1 O GLY J1115 N TYR J1063
SHEET 1 KA 4 GLU K 128 THR K 130 0
SHEET 2 KA 4 CYS K 159 LYS K 164 -1 O GLN K 162 N THR K 130
SHEET 3 KA 4 THR K 250 PHE K 256 -1 O THR K 250 N ILE K 163
SHEET 4 KA 4 ILE K 215 GLU K 218 -1 O ARG K 216 N ASN K 255
SHEET 1 KB 7 TRP K 142 SER K 145 0
SHEET 2 KB 7 LYS K 150 CYS K 153 -1 O LYS K 150 N SER K 145
SHEET 3 KB 7 VAL K 284 ILE K 294 1 O GLU K 291 N LEU K 151
SHEET 4 KB 7 ILE K 271 GLU K 278 -1 O ILE K 271 N GLY K 292
SHEET 5 KB 7 ALA K 174 TYR K 181 -1 O ALA K 174 N GLU K 278
SHEET 6 KB 7 GLN K 234 PRO K 239 -1 O VAL K 236 N ALA K 177
SHEET 7 KB 7 GLN K 224 ASP K 227 -1 O GLN K 224 N VAL K 237
SHEET 1 LA 5 LYS L1105 PRO L1110 0
SHEET 2 LA 5 TRP L1097 LEU L1102 -1 O TRP L1098 N VAL L1109
SHEET 3 LA 5 CYS L1083 HIS L1088 -1 O THR L1085 N ARG L1101
SHEET 4 LA 5 VAL L1061 ALA L1064 -1 O ILE L1062 N MET L1084
SHEET 5 LA 5 LEU L1114 GLY L1115 -1 O GLY L1115 N TYR L1063
SSBOND 1 CYS G 153 CYS G 159 1555 1555 2.54
LINK ZN ZN C 1 SG CYS C 194 1555 1555 2.11
LINK ZN ZN C 1 ND1 HIS C 197 1555 1555 2.14
LINK ZN ZN C 1 SG CYS C 258 1555 1555 2.16
LINK ZN ZN C 1 SG CYS C 262 1555 1555 2.49
LINK ZN ZN E 1 SG CYS E 194 1555 1555 2.14
LINK ZN ZN E 1 ND1 HIS E 197 1555 1555 2.13
LINK ZN ZN E 1 SG CYS E 258 1555 1555 2.39
LINK ZN ZN E 1 SG CYS E 262 1555 1555 2.34
LINK ZN ZN G 1 SG CYS G 194 1555 1555 2.26
LINK ZN ZN G 1 ND1 HIS G 197 1555 1555 1.99
LINK ZN ZN G 1 SG CYS G 258 1555 1555 2.23
LINK ZN ZN G 1 SG CYS G 262 1555 1555 2.30
LINK ZN ZN I 1 SG CYS I 194 1555 1555 2.22
LINK ZN ZN I 1 ND1 HIS I 197 1555 1555 1.98
LINK ZN ZN I 1 SG CYS I 258 1555 1555 2.22
LINK ZN ZN I 1 SG CYS I 262 1555 1555 2.36
LINK ZN ZN K 1 SG CYS K 194 1555 1555 2.24
LINK ZN ZN K 1 ND1 HIS K 197 1555 1555 2.09
LINK ZN ZN K 1 SG CYS K 258 1555 1555 2.43
LINK ZN ZN K 1 SG CYS K 262 1555 1555 2.34
SITE 1 AC1 4 CYS C 194 HIS C 197 CYS C 258 CYS C 262
SITE 1 AC2 4 PRO C 122 HIS C 126 GLU C 128 ARG C 288
SITE 1 AC3 6 TYR C 309 GLU C 313 SER I 117 THR I 119
SITE 2 AC3 6 TYR I 121 ARG I 287
SITE 1 AC4 6 SER C 117 THR C 119 TYR C 121 ARG C 287
SITE 2 AC4 6 TYR I 309 GLU I 313
SITE 1 AC5 4 CYS E 194 HIS E 197 CYS E 258 CYS E 262
SITE 1 AC6 4 CYS G 194 HIS G 197 CYS G 258 CYS G 262
SITE 1 AC7 6 SER G 117 THR G 119 TYR G 121 ARG G 287
SITE 2 AC7 6 TYR G 309 GLU G 313
SITE 1 AC8 4 CYS I 194 HIS I 197 CYS I 258 CYS I 262
SITE 1 AC9 2 TYR I 121 GLY I 123
SITE 1 BC1 7 ASP I 120 VAL I 129 TYR I 144 LYS I 149
SITE 2 BC1 7 SER I 289 HOH I2012 HOH I2022
SITE 1 BC2 4 CYS K 194 HIS K 197 CYS K 258 CYS K 262
SITE 1 BC3 5 TYR A 309 SER K 117 THR K 119 TYR K 121
SITE 2 BC3 5 ARG K 287
SITE 1 BC4 5 ASP K 120 VAL K 129 TYR K 144 LYS K 149
SITE 2 BC4 5 SER K 289
SITE 1 BC5 4 SER K 261 CYS K 295 ALA K 296 GLU L1096
CRYST1 132.810 170.100 177.555 90.00 91.98 90.00 I 1 2 1 24
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 0.007530 0.000000 0.000260 0.00000
SCALE2 0.000000 0.005879 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005635 0.00000
MTRIX1 1 -0.997800 -0.041800 0.052100 118.59320 1
MTRIX2 1 -0.038500 0.997300 0.062500 2.65530 1
MTRIX3 1 -0.054600 0.060300 -0.996700 125.00050 1
MTRIX1 2 0.998200 -0.050900 -0.031300 -4.93790 1
MTRIX2 2 0.051100 0.998700 0.006500 -1.00560 1
MTRIX3 2 0.030900 -0.008100 0.999500 59.69420 1
MTRIX1 3 0.999900 0.003000 0.012700 -66.47350 1
MTRIX2 3 0.003300 -0.999700 -0.023900 46.35940 1
MTRIX3 3 0.012600 0.024000 -0.999600 117.16610 1
MTRIX1 4 -0.998500 0.025800 -0.048700 56.54170 1
MTRIX2 4 -0.027800 -0.998800 0.040600 44.50600 1
MTRIX3 4 -0.047600 0.041900 0.998000 1.67320 1
MTRIX1 5 -0.999000 0.026300 -0.035100 59.98010 1
MTRIX2 5 -0.027200 -0.999300 0.024600 46.56600 1
MTRIX3 5 -0.034400 0.025500 0.999100 60.17400 1
MTRIX1 6 -0.999800 0.016700 -0.011400 54.24970 1
MTRIX2 6 -0.017900 -0.993000 0.116400 38.95860 1
MTRIX3 6 -0.009400 0.116600 0.993100 -3.25150 1
MTRIX1 7 -0.998200 -0.058300 0.011800 -12.13150 1
MTRIX2 7 -0.058900 0.996300 -0.062600 3.13590 1
MTRIX3 7 -0.008100 -0.063200 -0.998000 118.58370 1
MTRIX1 8 -0.999700 0.025300 -0.003400 59.47350 1
MTRIX2 8 -0.025400 -0.999500 0.021000 46.63060 1
MTRIX3 8 -0.002800 0.021100 0.999800 58.42100 1
MTRIX1 9 0.999300 -0.038400 -0.003300 -5.31510 1
MTRIX2 9 0.038500 0.997700 0.055300 -0.85830 1
MTRIX3 9 0.001200 -0.055400 0.998500 59.93420 1
MTRIX1 10 0.999400 0.034400 -0.002700 -67.05430 1
MTRIX2 10 0.034400 -0.999400 0.007000 42.56250 1
MTRIX3 10 -0.002500 -0.007100 -1.000000 119.11910 1
(ATOM LINES ARE NOT SHOWN.)
END
