HEADER TRANSCRIPTION 11-FEB-09 2WAQ
TITLE THE COMPLETE STRUCTURE OF THE ARCHAEAL 13-SUBUNIT DNA-DIRECTED RNA
TITLE 2 POLYMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO1N SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO2 SUBUNIT;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO1C SUBUNIT;
COMPND 9 CHAIN: C;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO3 SUBUNIT;
COMPND 12 CHAIN: D;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO7 SUBUNIT;
COMPND 15 CHAIN: E;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO4 SUBUNIT;
COMPND 18 CHAIN: F;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO8 SUBUNIT;
COMPND 21 CHAIN: G;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO5 SUBUNIT;
COMPND 24 CHAIN: H;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO6 SUBUNIT;
COMPND 27 CHAIN: K;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO11 SUBUNIT;
COMPND 30 CHAIN: L;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO10 SUBUNIT;
COMPND 33 CHAIN: N;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO12 SUBUNIT;
COMPND 36 CHAIN: P;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO13 SUBUNIT;
COMPND 39 CHAIN: Q
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 3 ORGANISM_TAXID: 2286;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 6 ORGANISM_TAXID: 2286;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 9 ORGANISM_TAXID: 2286;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 12 ORGANISM_TAXID: 2286;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 15 ORGANISM_TAXID: 2286;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 18 ORGANISM_TAXID: 2286;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 21 ORGANISM_TAXID: 2286;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 24 ORGANISM_TAXID: 2286;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 27 ORGANISM_TAXID: 2286;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 30 ORGANISM_TAXID: 2286;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 33 ORGANISM_TAXID: 2286;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 36 ORGANISM_TAXID: 2286;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;
SOURCE 39 ORGANISM_TAXID: 2286
KEYWDS MULTI-SUBUNIT, RNA POLYMERASE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KORKHIN,U.M.UNLIGIL,O.LITTLEFIELD,P.J.NELSON,D.I.STUART,P.B.SIGLER,
AUTHOR 2 S.D.BELL,N.G.A.ABRESCIA
REVDAT 5 13-DEC-23 2WAQ 1 REMARK
REVDAT 4 28-APR-21 2WAQ 1 REMARK LINK
REVDAT 3 28-AUG-19 2WAQ 1 JRNL REMARK
REVDAT 2 30-JAN-19 2WAQ 1 JRNL REMARK
REVDAT 1 19-MAY-09 2WAQ 0
JRNL AUTH Y.KORKHIN,U.M.UNLIGIL,O.LITTLEFIELD,P.J.NELSON,D.I.STUART,
JRNL AUTH 2 P.B.SIGLER,S.D.BELL,N.G.ABRESCIA
JRNL TITL EVOLUTION OF COMPLEX RNA POLYMERASES: THE COMPLETE ARCHAEAL
JRNL TITL 2 RNA POLYMERASE STRUCTURE.
JRNL REF PLOS BIOL. V. 7 00102 2009
JRNL REFN ESSN 1545-7885
JRNL PMID 19419240
JRNL DOI 10.1371/JOURNAL.PBIO.1000102
REMARK 2
REMARK 2 RESOLUTION. 3.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.0
REMARK 3 NUMBER OF REFLECTIONS : 56389
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) : 0.274
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.341
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3012
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) : 3.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2580
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 26454
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 88.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.869
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.652
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 87.522
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.857
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.769
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 26946 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 36436 ; 1.027 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3313 ; 4.881 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1189 ;36.250 ;23.743
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5003 ;17.898 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 220 ;13.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4160 ; 0.066 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19918 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 12722 ; 0.179 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 18153 ; 0.296 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 656 ; 0.123 ; 0.200
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): 48 ; 0.114 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.005 ; 0.200
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. THE REFINEMENT HAS ALSO BEEN CARRIED OUT USING NORMAL-
REMARK 3 MODE TO ANISOTROPICALLY REFINE THE OVERALL THERMAL MOTIONS.
REMARK 3 PLEASE SEE ARTICLE FOR MORE DETAILS.
REMARK 4
REMARK 4 2WAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1290038536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59401
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.350
REMARK 200 RESOLUTION RANGE LOW (A) : 42.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 44.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: GLRF, MOLREP, SOLVE
REMARK 200 STARTING MODEL: PDB ENTRY 1EN0
REMARK 200
REMARK 200 REMARK: THE STATISTICS FOR THIS DATA ARE DERIVED FROM MERGED IOBS
REMARK 200 AND SIGMAIOBS PRESENT IN THE ONLY MTZ AVAILABLE. RAW IMAGES
REMARK 200 COLLECTED IN 2001-2002 AND PROCESSING LOG-FILES HAVE BEEN LOST.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7MG/ML ENZYME, 150MM KCL, 100MM SRCL2,
REMARK 280 1MM ZNCL2, 100MM CACODYLATE PH 6.5, 12% PEG MME 5K, 5% GLYCEROL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 96.75050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 106.31000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 96.75050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 106.31000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: TRIDECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIDECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 71970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 172810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -446.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, K, L,
REMARK 350 AND CHAINS: N, P, Q
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 GLU A 3
REMARK 465 ASP A 31
REMARK 465 VAL A 32
REMARK 465 TYR A 33
REMARK 465 ASP A 34
REMARK 465 GLU A 35
REMARK 465 ASP A 36
REMARK 465 GLY A 37
REMARK 465 THR A 38
REMARK 465 PRO A 39
REMARK 465 ILE A 40
REMARK 465 GLU A 41
REMARK 465 LYS A 157
REMARK 465 LEU A 158
REMARK 465 GLU A 159
REMARK 465 LYS A 160
REMARK 465 PRO A 161
REMARK 465 TYR A 162
REMARK 465 ASN A 163
REMARK 465 PHE A 164
REMARK 465 TYR A 165
REMARK 465 GLU A 166
REMARK 465 GLU A 167
REMARK 465 ARG A 168
REMARK 465 LYS A 169
REMARK 465 GLU A 170
REMARK 465 GLY A 171
REMARK 465 VAL A 172
REMARK 465 ALA A 173
REMARK 465 LYS A 174
REMARK 465 ILE A 225
REMARK 465 GLU A 226
REMARK 465 SER A 227
REMARK 465 GLY A 228
REMARK 465 ILE A 229
REMARK 465 ARG A 230
REMARK 465 THR A 880
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 GLU B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 ASN B 7
REMARK 465 GLY B 198
REMARK 465 TYR B 199
REMARK 465 GLU B 509
REMARK 465 GLY B 510
REMARK 465 GLY B 511
REMARK 465 GLU B 512
REMARK 465 ASP B 513
REMARK 465 GLN B 514
REMARK 465 ASN B 515
REMARK 465 GLU B 516
REMARK 465 TYR B 517
REMARK 465 LEU B 518
REMARK 465 ARG B 821
REMARK 465 PHE B 822
REMARK 465 LEU B 823
REMARK 465 GLN B 824
REMARK 465 GLU B 825
REMARK 465 PHE B 826
REMARK 465 LYS B 827
REMARK 465 GLU B 828
REMARK 465 LEU B 829
REMARK 465 SER B 830
REMARK 465 PRO B 831
REMARK 465 GLU B 832
REMARK 465 GLN B 833
REMARK 465 GLY B 1123
REMARK 465 LEU B 1124
REMARK 465 SER B 1125
REMARK 465 GLY B 1126
REMARK 465 GLY B 1127
REMARK 465 LYS B 1128
REMARK 465 GLY B 1129
REMARK 465 ASN B 1130
REMARK 465 GLU B 1131
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 ASN C 3
REMARK 465 VAL C 4
REMARK 465 ILE C 5
REMARK 465 ASP C 6
REMARK 465 GLU C 7
REMARK 465 LYS C 8
REMARK 465 ASP C 9
REMARK 465 LYS C 10
REMARK 465 MET C 85
REMARK 465 THR C 86
REMARK 465 LEU C 87
REMARK 465 ARG C 88
REMARK 465 THR C 89
REMARK 465 PHE C 90
REMARK 465 HIS C 91
REMARK 465 PHE C 92
REMARK 465 ALA C 93
REMARK 465 GLY C 94
REMARK 465 ILE C 95
REMARK 465 ARG C 96
REMARK 465 GLU C 97
REMARK 465 LEU C 98
REMARK 465 ASN C 99
REMARK 465 VAL C 100
REMARK 465 THR C 101
REMARK 465 ARG C 395
REMARK 465 MET D 1
REMARK 465 THR D 86
REMARK 465 GLU D 87
REMARK 465 ASN D 88
REMARK 465 LYS D 265
REMARK 465 THR E 154
REMARK 465 GLY E 155
REMARK 465 ARG E 156
REMARK 465 ALA E 178
REMARK 465 LYS E 179
REMARK 465 LYS E 180
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ARG F 93
REMARK 465 THR F 94
REMARK 465 TYR F 95
REMARK 465 THR F 96
REMARK 465 SER F 97
REMARK 465 GLU F 98
REMARK 465 ASP F 99
REMARK 465 ILE F 100
REMARK 465 GLN F 101
REMARK 465 LYS F 102
REMARK 465 ILE F 103
REMARK 465 ILE F 104
REMARK 465 ASP F 105
REMARK 465 ILE F 106
REMARK 465 ILE F 107
REMARK 465 ARG F 108
REMARK 465 LYS F 109
REMARK 465 TYR F 110
REMARK 465 ILE F 111
REMARK 465 LYS F 112
REMARK 465 SER F 113
REMARK 465 MET G 1
REMARK 465 MET G 2
REMARK 465 GLU G 3
REMARK 465 SER G 4
REMARK 465 LEU G 118
REMARK 465 ASN G 119
REMARK 465 VAL G 120
REMARK 465 MET G 121
REMARK 465 ASP G 122
REMARK 465 HIS G 123
REMARK 465 ILE G 124
REMARK 465 TYR G 125
REMARK 465 PHE G 126
REMARK 465 CYS G 127
REMARK 465 VAL G 128
REMARK 465 LYS G 129
REMARK 465 LYS G 130
REMARK 465 ASN G 131
REMARK 465 THR G 132
REMARK 465 MET H 1
REMARK 465 ARG H 2
REMARK 465 GLY H 3
REMARK 465 SER H 4
REMARK 465 SER H 5
REMARK 465 ASN H 6
REMARK 465 ARG H 7
REMARK 465 LYS H 8
REMARK 465 SER H 83
REMARK 465 GLY H 84
REMARK 465 MET K 1
REMARK 465 GLY K 2
REMARK 465 LEU K 3
REMARK 465 GLU K 4
REMARK 465 ARG K 5
REMARK 465 ASP K 6
REMARK 465 GLY K 7
REMARK 465 ILE K 8
REMARK 465 LEU K 9
REMARK 465 SER K 10
REMARK 465 ARG K 93
REMARK 465 LYS K 94
REMARK 465 SER K 95
REMARK 465 LYS L 92
REMARK 465 PRO N 65
REMARK 465 ILE N 66
REMARK 465 MET P 1
REMARK 465 ALA P 2
REMARK 465 VAL P 3
REMARK 465 TYR P 4
REMARK 465 ARG P 5
REMARK 465 MET Q 1
REMARK 465 VAL Q 2
REMARK 465 SER Q 3
REMARK 465 GLY Q 4
REMARK 465 MET Q 5
REMARK 465 SER Q 6
REMARK 465 THR Q 7
REMARK 465 GLU Q 8
REMARK 465 GLU Q 9
REMARK 465 GLU Q 10
REMARK 465 LYS Q 11
REMARK 465 GLU Q 12
REMARK 465 GLY Q 13
REMARK 465 THR Q 14
REMARK 465 ASN Q 15
REMARK 465 ASP Q 16
REMARK 465 GLU Q 17
REMARK 465 GLU Q 18
REMARK 465 VAL Q 19
REMARK 465 SER Q 20
REMARK 465 GLU Q 21
REMARK 465 GLU Q 22
REMARK 465 ARG Q 23
REMARK 465 GLU Q 24
REMARK 465 VAL Q 25
REMARK 465 GLU Q 26
REMARK 465 GLU Q 27
REMARK 465 THR Q 28
REMARK 465 SER Q 29
REMARK 465 GLU Q 30
REMARK 465 GLU Q 31
REMARK 465 GLU Q 32
REMARK 465 PHE Q 33
REMARK 465 PRO Q 34
REMARK 465 LYS Q 35
REMARK 465 LEU Q 36
REMARK 465 SER Q 37
REMARK 465 LYS Q 83
REMARK 465 ALA Q 84
REMARK 465 LYS Q 85
REMARK 465 LYS Q 86
REMARK 465 ALA Q 87
REMARK 465 ALA Q 88
REMARK 465 SER Q 89
REMARK 465 LYS Q 90
REMARK 465 LYS Q 91
REMARK 465 VAL Q 92
REMARK 465 LYS Q 93
REMARK 465 LYS Q 94
REMARK 465 THR Q 95
REMARK 465 LYS Q 96
REMARK 465 LYS Q 97
REMARK 465 LYS Q 98
REMARK 465 GLU Q 99
REMARK 465 LYS Q 100
REMARK 465 SER Q 101
REMARK 465 VAL Q 102
REMARK 465 GLU Q 103
REMARK 465 GLY Q 104
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 ILE A 223 CG1 CG2 CD1
REMARK 470 MET A 224 CG SD CE
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 MET A 22 -38.56 63.80
REMARK 500 ILE A 27 -47.06 -134.17
REMARK 500 VAL A 44 73.19 -100.04
REMARK 500 MET A 45 -40.46 -170.76
REMARK 500 ASP A 46 -68.29 -108.73
REMARK 500 ARG A 48 0.13 88.40
REMARK 500 GLU A 53 152.66 66.39
REMARK 500 GLN A 56 -147.90 -118.89
REMARK 500 CYS A 61 -91.19 -142.35
REMARK 500 LEU A 65 -172.48 63.69
REMARK 500 ARG A 79 95.51 86.56
REMARK 500 PRO A 80 150.76 -49.48
REMARK 500 ARG A 99 -33.34 82.23
REMARK 500 CYS A 101 -120.31 -129.05
REMARK 500 ARG A 103 -63.15 50.18
REMARK 500 ILE A 106 -108.69 -110.71
REMARK 500 TYR A 118 47.76 -96.82
REMARK 500 LYS A 142 -58.66 -122.38
REMARK 500 ALA A 143 -106.88 56.30
REMARK 500 VAL A 145 83.51 -152.82
REMARK 500 PRO A 147 59.44 -94.98
REMARK 500 HIS A 148 177.23 62.85
REMARK 500 GLU A 151 -107.26 -142.75
REMARK 500 LYS A 155 148.16 -37.33
REMARK 500 THR A 200 -62.71 -107.97
REMARK 500 SER A 252 38.56 -98.47
REMARK 500 ALA A 257 99.54 66.81
REMARK 500 PHE A 277 -72.07 -75.54
REMARK 500 GLU A 280 -45.35 -173.17
REMARK 500 PRO A 282 177.11 -57.07
REMARK 500 LEU A 284 66.99 39.93
REMARK 500 SER A 287 111.13 65.78
REMARK 500 ARG A 290 -86.68 61.97
REMARK 500 ARG A 308 -76.58 65.76
REMARK 500 ILE A 332 136.12 66.65
REMARK 500 PRO A 355 3.77 -61.29
REMARK 500 ASP A 393 108.48 63.92
REMARK 500 ASP A 413 100.97 -57.50
REMARK 500 VAL A 449 46.39 -100.16
REMARK 500 PHE A 457 77.00 -113.41
REMARK 500 ASP A 458 17.74 -142.46
REMARK 500 LYS A 477 -34.38 -132.25
REMARK 500 ALA A 499 -77.90 -77.34
REMARK 500 GLN A 500 -50.12 -144.76
REMARK 500 LYS A 531 41.07 -99.12
REMARK 500 GLU A 536 114.16 64.07
REMARK 500 ALA A 541 -81.96 -68.04
REMARK 500 ALA A 554 44.37 -83.11
REMARK 500 PHE A 555 -25.17 -140.79
REMARK 500 LYS A 558 20.76 -78.46
REMARK 500
REMARK 500 THIS ENTRY HAS 339 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 58 SG
REMARK 620 2 CYS A 68 SG 118.8
REMARK 620 3 HIS A 71 NE2 101.0 136.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1400 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 456 OD1
REMARK 620 2 ASP A 458 OD1 71.0
REMARK 620 3 ASP A 460 OD1 62.1 75.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1064 SG
REMARK 620 2 CYS B1067 SG 109.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S D1001 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 203 SG
REMARK 620 2 F3S D1001 S1 128.3
REMARK 620 3 F3S D1001 S3 103.2 108.6
REMARK 620 4 F3S D1001 S4 121.6 85.7 108.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S D1001 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 206 SG
REMARK 620 2 F3S D1001 S2 94.3
REMARK 620 3 F3S D1001 S3 114.2 108.3
REMARK 620 4 F3S D1001 S4 134.2 88.5 108.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S D1001 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 209 SG
REMARK 620 2 F3S D1001 S1 122.4
REMARK 620 3 F3S D1001 S2 107.5 84.0
REMARK 620 4 F3S D1001 S3 119.4 108.6 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN N 100 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 7 SG
REMARK 620 2 CYS N 10 SG 100.4
REMARK 620 3 CYS N 45 SG 131.6 54.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P 50 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 9 SG
REMARK 620 2 THR P 12 OG1 118.6
REMARK 620 3 CYS P 29 SG 127.4 113.2
REMARK 620 N 1 2
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BJ" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S D1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 50
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WB1 RELATED DB: PDB
REMARK 900 THE COMPLETE STRUCTURE OF THE ARCHAEAL 13- SUBUNIT DNA-DIRECTED RNA
REMARK 900 POLYMERASE
DBREF 2WAQ A 1 880 PDB 2WAQ 2WAQ 1 880
DBREF 2WAQ B 1 1131 PDB 2WAQ 2WAQ 1 1131
DBREF 2WAQ C 1 395 PDB 2WAQ 2WAQ 1 395
DBREF 2WAQ D 1 265 PDB 2WAQ 2WAQ 1 265
DBREF 2WAQ E 1 180 PDB 2WAQ 2WAQ 1 180
DBREF 2WAQ F 1 113 PDB 2WAQ 2WAQ 1 113
DBREF 2WAQ G 1 132 PDB 2WAQ 2WAQ 1 132
DBREF 2WAQ H 1 84 PDB 2WAQ 2WAQ 1 84
DBREF 2WAQ K 1 95 PDB 2WAQ 2WAQ 1 95
DBREF 2WAQ L 1 92 PDB 2WAQ 2WAQ 1 92
DBREF 2WAQ N 1 66 PDB 2WAQ 2WAQ 1 66
DBREF 2WAQ P 1 48 PDB 2WAQ 2WAQ 1 48
DBREF 2WAQ Q 1 104 PDB 2WAQ 2WAQ 1 104
SEQRES 1 A 880 MET SER GLU LYS ASN ILE LYS GLY ILE LYS PHE GLY ILE
SEQRES 2 A 880 LEU SER PRO ASP GLU ILE ARG LYS MET SER VAL THR ALA
SEQRES 3 A 880 ILE ILE THR PRO ASP VAL TYR ASP GLU ASP GLY THR PRO
SEQRES 4 A 880 ILE GLU GLY SER VAL MET ASP PRO ARG LEU GLY VAL ILE
SEQRES 5 A 880 GLU PRO GLY GLN LYS CYS PRO THR CYS GLY ASN THR LEU
SEQRES 6 A 880 GLY ASN CYS PRO GLY HIS PHE GLY HIS ILE GLU LEU VAL
SEQRES 7 A 880 ARG PRO VAL ILE HIS VAL GLY PHE VAL LYS HIS VAL TYR
SEQRES 8 A 880 GLU PHE LEU LYS ALA THR CYS ARG ARG CYS GLY ARG VAL
SEQRES 9 A 880 LYS ILE SER GLU ASP GLU ILE GLU LYS TYR SER ARG ILE
SEQRES 10 A 880 TYR ASN ALA ILE LYS LYS ARG TRP PRO SER ALA ALA ARG
SEQRES 11 A 880 ARG LEU THR GLU TYR VAL LYS LYS THR ALA MET LYS ALA
SEQRES 12 A 880 GLN VAL CYS PRO HIS CYS GLY GLU LYS GLN PHE LYS ILE
SEQRES 13 A 880 LYS LEU GLU LYS PRO TYR ASN PHE TYR GLU GLU ARG LYS
SEQRES 14 A 880 GLU GLY VAL ALA LYS LEU THR PRO SER ASP ILE ARG GLU
SEQRES 15 A 880 ARG LEU GLU LYS VAL PRO GLU SER ASP VAL GLU ILE LEU
SEQRES 16 A 880 GLY TYR ASP PRO THR THR SER ARG PRO GLU TRP MET ILE
SEQRES 17 A 880 LEU THR VAL LEU PRO VAL PRO PRO ILE THR ILE ARG PRO
SEQRES 18 A 880 SER ILE MET ILE GLU SER GLY ILE ARG ALA GLU ASP ASP
SEQRES 19 A 880 LEU THR HIS LYS LEU VAL ASP ILE VAL ARG ILE ASN GLU
SEQRES 20 A 880 ARG LEU LYS GLU SER ILE ASP ALA GLY ALA PRO GLN LEU
SEQRES 21 A 880 ILE ILE GLU ASP LEU TRP ASP LEU LEU GLN TYR HIS VAL
SEQRES 22 A 880 ALA THR TYR PHE ASP ASN GLU ILE PRO GLY LEU PRO PRO
SEQRES 23 A 880 SER LYS HIS ARG SER GLY ARG PRO LEU ARG THR LEU ALA
SEQRES 24 A 880 GLN ARG LEU LYS GLY LYS GLU GLY ARG PHE ARG GLY ASN
SEQRES 25 A 880 LEU SER GLY LYS ARG VAL ASP PHE SER SER ARG THR VAL
SEQRES 26 A 880 ILE SER PRO ASP PRO ASN ILE SER ILE ASP GLU VAL GLY
SEQRES 27 A 880 VAL PRO GLU ILE ILE ALA ARG THR LEU THR VAL PRO GLU
SEQRES 28 A 880 ARG ILE THR PRO TRP ASN ILE GLU LYS LEU ARG GLN PHE
SEQRES 29 A 880 VAL ILE ASN GLY PRO ASP LYS TRP PRO GLY ALA ASN TYR
SEQRES 30 A 880 VAL ILE ARG PRO ASP GLY ARG ARG ILE ASP LEU ARG TYR
SEQRES 31 A 880 VAL LYS ASP ARG LYS GLU LEU ALA SER THR LEU ALA PRO
SEQRES 32 A 880 GLY TYR VAL VAL GLU ARG HIS LEU THR ASP GLY ASP VAL
SEQRES 33 A 880 VAL LEU PHE ASN ARG GLN PRO SER LEU HIS ARG ILE SER
SEQRES 34 A 880 MET MET ALA HIS ARG VAL ARG VAL LEU LYS GLY LEU THR
SEQRES 35 A 880 PHE ARG LEU ASN LEU LEU VAL CYS PRO PRO TYR ASN ALA
SEQRES 36 A 880 ASP PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN
SEQRES 37 A 880 SER GLU GLU ALA ILE ALA GLU ALA LYS GLU ILE MET LEU
SEQRES 38 A 880 VAL HIS LYS ASN ILE ILE THR PRO ARG TYR GLY GLY PRO
SEQRES 39 A 880 ILE ILE GLY ALA ALA GLN ASP TYR ILE SER GLY ALA TYR
SEQRES 40 A 880 LEU LEU THR VAL LYS THR THR LEU LEU THR LYS GLU GLU
SEQRES 41 A 880 ALA GLN GLN ILE LEU GLY VAL ALA ASP VAL LYS ILE ASP
SEQRES 42 A 880 LEU GLY GLU PRO ALA ILE LEU ALA PRO ARG GLU TYR TYR
SEQRES 43 A 880 THR GLY LYS GLN VAL VAL SER ALA PHE LEU PRO LYS ASP
SEQRES 44 A 880 PHE ASN PHE HIS GLY GLN ALA ASN VAL SER SER GLY PRO
SEQRES 45 A 880 ARG LEU CYS LYS ASN GLU ASP CYS PRO HIS ASP SER TYR
SEQRES 46 A 880 VAL VAL ILE LYS ASN GLY ILE LEU LEU GLU GLY VAL PHE
SEQRES 47 A 880 ASP LYS LYS ALA ILE GLY ASN GLN GLN PRO GLU SER ILE
SEQRES 48 A 880 LEU HIS TRP LEU ILE LYS GLU TYR SER ASP GLU TYR GLY
SEQRES 49 A 880 LYS TRP LEU MET ASP ASN LEU PHE ARG VAL PHE ILE ARG
SEQRES 50 A 880 PHE VAL GLU LEU GLN GLY PHE THR MET ARG LEU GLU ASP
SEQRES 51 A 880 VAL SER LEU GLY ASP ASP VAL LYS LYS GLU ILE TYR ASN
SEQRES 52 A 880 GLU ILE ASP ARG ALA LYS VAL GLU VAL ASP ASN LEU ILE
SEQRES 53 A 880 GLN LYS TYR LYS ASN GLY GLU LEU GLU PRO ILE PRO GLY
SEQRES 54 A 880 ARG THR LEU GLU GLU SER LEU GLU ASN TYR ILE LEU ASP
SEQRES 55 A 880 THR LEU ASP LYS LEU ARG SER THR ALA GLY ASP ILE ALA
SEQRES 56 A 880 SER LYS TYR LEU ASP PRO PHE ASN PHE ALA TYR VAL MET
SEQRES 57 A 880 ALA ARG THR GLY ALA ARG GLY SER VAL LEU ASN ILE THR
SEQRES 58 A 880 GLN MET ALA ALA MET LEU GLY GLN GLN SER VAL ARG GLY
SEQRES 59 A 880 GLU ARG ILE LYS ARG GLY TYR MET THR ARG THR LEU PRO
SEQRES 60 A 880 HIS PHE LYS PRO TYR ASP ILE SER PRO GLU ALA ARG GLY
SEQRES 61 A 880 PHE ILE TYR SER SER PHE ARG THR GLY LEU LYS PRO THR
SEQRES 62 A 880 GLU LEU PHE PHE HIS ALA ALA GLY GLY ARG GLU GLY LEU
SEQRES 63 A 880 VAL ASP THR ALA VAL ARG THR SER GLN SER GLY TYR MET
SEQRES 64 A 880 GLN ARG ARG LEU ILE ASN ALA LEU SER ASP LEU ARG ALA
SEQRES 65 A 880 GLU TYR ASP GLY THR VAL ARG SER LEU TYR GLY GLU VAL
SEQRES 66 A 880 ILE GLN VAL ALA TYR GLY ASP ASP GLY VAL PHE PRO MET
SEQRES 67 A 880 TYR SER ALA HIS GLY LYS THR VAL ASP VAL ASN ARG ILE
SEQRES 68 A 880 PHE GLU ARG VAL VAL GLY TRP LYS THR
SEQRES 1 B 1131 MET ASN GLU LEU SER SER ASN LEU SER ILE ASP GLU ARG
SEQRES 2 B 1131 TRP LYS VAL ILE GLU ALA TYR PHE LYS SER LYS GLY LEU
SEQRES 3 B 1131 VAL ARG GLN HIS LEU ASP SER TYR ASN ASP PHE VAL ARG
SEQRES 4 B 1131 ASN LYS LEU GLN GLU ILE ILE ASP GLU GLN GLY GLU ILE
SEQRES 5 B 1131 PRO THR GLU ILE PRO GLY LEU LYS VAL ARG LEU GLY LYS
SEQRES 6 B 1131 ILE ARG ILE GLY LYS PRO ARG VAL ARG GLU SER ASP ARG
SEQRES 7 B 1131 GLY GLU ARG GLU ILE SER PRO MET GLU ALA ARG LEU ARG
SEQRES 8 B 1131 ASN LEU THR TYR ALA ALA PRO LEU TRP LEU THR MET ILE
SEQRES 9 B 1131 PRO VAL GLU ASN ASN ILE GLU ALA GLU PRO GLU GLU VAL
SEQRES 10 B 1131 TYR ILE GLY ASP LEU PRO ILE MET LEU LYS SER ALA ILE
SEQRES 11 B 1131 ASP PRO ILE SER GLN TYR THR LEU ASP LYS LEU ILE GLU
SEQRES 12 B 1131 ILE GLY GLU ASP PRO LYS ASP PRO GLY GLY TYR PHE ILE
SEQRES 13 B 1131 VAL ASN GLY SER GLU ARG VAL ILE VAL THR GLN GLU ASP
SEQRES 14 B 1131 LEU ALA PRO ASN ARG VAL LEU VAL ASP THR GLY LYS THR
SEQRES 15 B 1131 GLY SER ASN ILE THR HIS THR ALA LYS ILE ILE SER SER
SEQRES 16 B 1131 THR ALA GLY TYR ARG VAL PRO VAL THR ILE GLU ARG LEU
SEQRES 17 B 1131 LYS ASP GLY THR PHE HIS VAL SER PHE PRO ALA VAL PRO
SEQRES 18 B 1131 GLY LYS ILE PRO PHE VAL ILE LEU MET ARG ALA LEU GLY
SEQRES 19 B 1131 ILE LEU THR ASP ARG ASP ILE VAL TYR ALA VAL SER LEU
SEQRES 20 B 1131 ASP PRO GLU ILE GLN ASN GLU LEU PHE PRO SER LEU GLU
SEQRES 21 B 1131 GLN ALA SER SER ILE ALA ASN VAL ASP ASP ALA LEU ASP
SEQRES 22 B 1131 PHE ILE GLY SER ARG VAL ALA ILE GLY GLN LYS ARG GLU
SEQRES 23 B 1131 ASN ARG ILE GLU LYS ALA GLN GLN ILE ILE ASP LYS TYR
SEQRES 24 B 1131 PHE LEU PRO HIS LEU GLY THR SER ALA ASP ASP ARG ARG
SEQRES 25 B 1131 LYS LYS ALA TYR TYR LEU ALA TYR ALA ILE SER LYS VAL
SEQRES 26 B 1131 ILE GLU LEU TYR LEU GLY ARG ARG GLU PRO ASP ASP LYS
SEQRES 27 B 1131 ASP HIS TYR ALA ASN LYS ARG LEU ARG LEU ALA GLY ASP
SEQRES 28 B 1131 LEU PHE ALA SER LEU PHE ARG VAL ALA PHE LYS ALA PHE
SEQRES 29 B 1131 VAL LYS ASP LEU THR TYR GLN LEU GLU LYS SER LYS VAL
SEQRES 30 B 1131 ARG GLY ARG LYS LEU ALA LEU LYS ALA LEU VAL ARG PRO
SEQRES 31 B 1131 ASP ILE VAL THR GLU ARG ILE ARG HIS ALA LEU ALA THR
SEQRES 32 B 1131 GLY ASN TRP VAL GLY GLY ARG THR GLY VAL SER GLN LEU
SEQRES 33 B 1131 LEU ASP ARG THR ASN TRP LEU SER MET LEU SER HIS LEU
SEQRES 34 B 1131 ARG ARG VAL ILE SER SER LEU ALA ARG GLY GLN PRO ASN
SEQRES 35 B 1131 PHE GLU ALA ARG ASP LEU HIS GLY THR GLN TRP GLY ARG
SEQRES 36 B 1131 MET CYS PRO PHE GLU THR PRO GLU GLY PRO ASN SER GLY
SEQRES 37 B 1131 LEU VAL LYS ASN LEU ALA LEU MET ALA GLN ILE ALA VAL
SEQRES 38 B 1131 GLY ILE ASN GLU LYS ILE VAL GLU LYS THR LEU TYR GLU
SEQRES 39 B 1131 MET GLY VAL VAL PRO VAL GLU GLU VAL ILE ARG ARG VAL
SEQRES 40 B 1131 THR GLU GLY GLY GLU ASP GLN ASN GLU TYR LEU LYS TRP
SEQRES 41 B 1131 SER LYS VAL ILE LEU ASN GLY ARG LEU VAL GLY TYR TYR
SEQRES 42 B 1131 ARG ASP GLY GLU GLU LEU ALA LYS LYS ILE ARG GLU ARG
SEQRES 43 B 1131 ARG ARG LYS GLY GLU ILE SER ASP GLU VAL ASN VAL GLY
SEQRES 44 B 1131 HIS ILE VAL THR ASP PHE ILE ASN GLU VAL HIS VAL ASN
SEQRES 45 B 1131 CYS ASP SER GLY ARG VAL ARG ARG PRO LEU ILE ILE VAL
SEQRES 46 B 1131 SER ASN GLY ASN PRO LEU VAL THR ARG GLU ASP ILE GLU
SEQRES 47 B 1131 LYS LEU ASP SER GLY SER ILE THR PHE ASP ASP LEU VAL
SEQRES 48 B 1131 ARG GLN GLY LYS ILE GLU TYR LEU ASP ALA GLU GLU GLU
SEQRES 49 B 1131 GLU ASN ALA TYR VAL ALA LEU GLU PRO SER ASP LEU THR
SEQRES 50 B 1131 PRO GLU HIS THR HIS LEU GLU ILE TRP SER PRO ALA ILE
SEQRES 51 B 1131 LEU GLY ILE THR ALA SER ILE ILE PRO TYR PRO GLU HIS
SEQRES 52 B 1131 ASN GLN SER PRO ARG ASN THR TYR GLN SER ALA MET ALA
SEQRES 53 B 1131 LYS GLN ALA LEU GLY LEU TYR ALA ALA ASN TYR GLN LEU
SEQRES 54 B 1131 ARG THR ASP THR ARG ALA HIS LEU LEU HIS TYR PRO GLN
SEQRES 55 B 1131 ARG PRO LEU VAL GLN THR ARG ALA LEU ASP ILE ILE GLY
SEQRES 56 B 1131 TYR THR ASN ARG PRO ALA GLY ASN ASN ALA ILE LEU ALA
SEQRES 57 B 1131 VAL ILE SER PHE THR GLY TYR ASN MET GLU ASP SER ILE
SEQRES 58 B 1131 ILE MET ASN ARG SER SER VAL GLU ARG GLY MET TYR ARG
SEQRES 59 B 1131 SER THR PHE PHE ARG LEU TYR SER THR GLU GLU VAL LYS
SEQRES 60 B 1131 TYR PRO GLY GLY GLN GLU ASP LYS ILE VAL MET PRO GLU
SEQRES 61 B 1131 PRO GLY VAL ARG GLY TYR LYS GLY LYS GLU TYR TYR ARG
SEQRES 62 B 1131 LEU LEU GLU ASP ASN GLY VAL VAL SER PRO GLU VAL GLU
SEQRES 63 B 1131 VAL LYS GLY GLY ASP VAL LEU ILE GLY LYS VAL SER PRO
SEQRES 64 B 1131 PRO ARG PHE LEU GLN GLU PHE LYS GLU LEU SER PRO GLU
SEQRES 65 B 1131 GLN ALA LYS ARG ASP THR SER ILE VAL THR ARG HIS GLY
SEQRES 66 B 1131 GLU MET GLY ILE VAL ASP LEU VAL LEU ILE THR GLU THR
SEQRES 67 B 1131 ALA GLU GLY ASN LYS LEU VAL LYS VAL ARG VAL ARG ASP
SEQRES 68 B 1131 LEU ARG ILE PRO SER ILE GLY ASP LYS PHE ALA SER ARG
SEQRES 69 B 1131 HIS GLY GLN LYS GLY VAL ILE GLY MET LEU ILE PRO GLN
SEQRES 70 B 1131 VAL ASP MET PRO TYR THR VAL LYS GLY VAL VAL PRO ASP
SEQRES 71 B 1131 VAL ILE LEU ASN PRO HIS ALA LEU PRO SER ARG MET THR
SEQRES 72 B 1131 LEU GLY GLN ILE MET GLU GLY ILE ALA GLY LYS TYR ALA
SEQRES 73 B 1131 ALA LEU SER GLY ASN ILE VAL ASP ALA THR PRO PHE TYR
SEQRES 74 B 1131 LYS THR PRO ILE GLU GLN LEU GLN ASN GLU ILE LEU LYS
SEQRES 75 B 1131 TYR GLY TYR LEU PRO ASP ALA THR GLU VAL THR TYR ASP
SEQRES 76 B 1131 GLY ARG THR GLY GLN LYS ILE LYS SER ARG ILE TYR PHE
SEQRES 77 B 1131 GLY VAL VAL TYR TYR GLN LYS LEU HIS HIS MET VAL ALA
SEQRES 78 B 1131 ASP LYS ILE HIS ALA ARG ALA ARG GLY PRO VAL GLN ILE
SEQRES 79 B 1131 LEU THR ARG GLN PRO THR GLU GLY ARG ALA ARG GLU GLY
SEQRES 80 B 1131 GLY LEU ARG PHE GLY GLU MET GLU ARG ASP CYS LEU ILE
SEQRES 81 B 1131 GLY PHE GLY THR ALA MET LEU LEU LYS ASP ARG LEU LEU
SEQRES 82 B 1131 ASP ASN SER ASP ARG THR THR ILE TYR VAL CYS ASP GLN
SEQRES 83 B 1131 CYS GLY TYR ILE GLY TRP TYR ASP LYS ASN LYS ASN LYS
SEQRES 84 B 1131 TYR VAL CYS PRO ILE HIS GLY ASP LYS SER ASN LEU PHE
SEQRES 85 B 1131 PRO VAL THR VAL SER TYR ALA PHE LYS LEU LEU ILE GLN
SEQRES 86 B 1131 GLU LEU MET SER MET ILE ILE SER PRO ARG LEU ILE LEU
SEQRES 87 B 1131 GLU ASP ARG VAL GLY LEU SER GLY GLY LYS GLY ASN GLU
SEQRES 1 C 395 MET GLU ASN VAL ILE ASP GLU LYS ASP LYS SER TYR LEU
SEQRES 2 C 395 GLU GLU LYS VAL LYS GLN ALA SER ASN ILE LEU PRO GLN
SEQRES 3 C 395 LYS ILE VAL GLU ASP LEU LYS ASN LEU ILE SER ASN LYS
SEQRES 4 C 395 GLU VAL LEU VAL THR ARG ASP GLU ILE ASP LYS ILE PHE
SEQRES 5 C 395 ASP LEU ALA ILE LYS GLU TYR SER GLU GLY LEU ILE ALA
SEQRES 6 C 395 PRO GLY GLU ALA ILE GLY ILE VAL ALA ALA GLN SER VAL
SEQRES 7 C 395 GLY GLU PRO GLY THR GLN MET THR LEU ARG THR PHE HIS
SEQRES 8 C 395 PHE ALA GLY ILE ARG GLU LEU ASN VAL THR LEU GLY LEU
SEQRES 9 C 395 PRO ARG LEU ILE GLU ILE VAL ASP ALA LYS LYS VAL PRO
SEQRES 10 C 395 SER THR PRO MET MET THR ILE TYR LEU THR ASP GLU TYR
SEQRES 11 C 395 LYS HIS ASP LYS GLU LYS ALA LEU GLU VAL ALA ARG LYS
SEQRES 12 C 395 LEU GLU TYR THR LYS ILE GLU ASN VAL VAL SER SER THR
SEQRES 13 C 395 SER ILE ASP ILE ALA SER MET SER ILE ILE LEU GLN LEU
SEQRES 14 C 395 ASP ASN GLU MET LEU LYS ASP LYS GLY VAL THR VAL ASP
SEQRES 15 C 395 ASP VAL LYS LYS ALA ILE ASN ARG LEU LYS LEU GLY GLU
SEQRES 16 C 395 PHE VAL ILE ASP GLU SER GLU GLY THR THR LEU ASN ILE
SEQRES 17 C 395 SER PHE ALA ASN ILE ASP SER ILE ALA ALA LEU PHE LYS
SEQRES 18 C 395 LEU ARG ASP LYS ILE LEU ASN THR LYS ILE LYS GLY ILE
SEQRES 19 C 395 LYS GLY ILE LYS ARG ALA ILE VAL GLN LYS LYS GLY ASP
SEQRES 20 C 395 GLU TYR ILE ILE LEU THR ASP GLY SER ASN LEU SER GLY
SEQRES 21 C 395 VAL LEU SER VAL LYS GLY VAL ASP ILE ALA LYS VAL GLU
SEQRES 22 C 395 THR ASN ASN ILE ARG GLU ILE GLU GLU VAL PHE GLY ILE
SEQRES 23 C 395 GLU ALA ALA ARG GLU ILE ILE ILE ARG GLU ILE SER LYS
SEQRES 24 C 395 VAL LEU ALA GLU GLN GLY LEU ASP VAL ASP MET ARG HIS
SEQRES 25 C 395 ILE LEU LEU VAL ALA ASP VAL MET THR ARG THR GLY VAL
SEQRES 26 C 395 VAL ARG GLN ILE GLY ARG HIS GLY VAL THR GLY GLU LYS
SEQRES 27 C 395 ASN SER VAL LEU ALA ARG ALA ALA PHE GLU VAL THR VAL
SEQRES 28 C 395 LYS HIS LEU LEU ASP ALA ALA ALA ARG GLY ASP VAL GLU
SEQRES 29 C 395 GLU PHE LYS GLY VAL VAL GLU ASN ILE ILE ILE GLY HIS
SEQRES 30 C 395 PRO ILE LYS LEU GLY THR GLY MET VAL GLU LEU THR MET
SEQRES 31 C 395 ARG PRO ILE LEU ARG
SEQRES 1 D 265 MET SER ILE ASN LEU LEU HIS LYS ASP ASP LYS ARG ILE
SEQRES 2 D 265 ASP LEU VAL PHE GLU GLY TYR PRO LEU GLU PHE VAL ASN
SEQRES 3 D 265 ALA ILE ARG ARG ALA ALA MET LEU TYR VAL PRO VAL MET
SEQRES 4 D 265 SER ILE ASP ASP VAL TYR PHE ILE GLU ASN ASN SER PRO
SEQRES 5 D 265 LEU TYR ASP GLU ILE LEU ALA HIS ARG LEU ALA LEU ILE
SEQRES 6 D 265 PRO PHE THR SER GLU GLU ALA LEU ASP THR TYR ARG TRP
SEQRES 7 D 265 PRO GLU GLU CYS ILE ASP CYS THR GLU ASN CYS GLU LYS
SEQRES 8 D 265 CYS TYR THR LYS ILE TYR ILE GLU ALA GLU ALA LEU ASN
SEQRES 9 D 265 GLU PRO LYS MET LEU TYR SER LYS ASP ILE LYS SER GLU
SEQRES 10 D 265 ASP PRO SER ILE VAL PRO ILE SER GLY ASP ILE PRO ILE
SEQRES 11 D 265 VAL LEU LEU GLY ALA ASN GLN LYS ILE SER LEU GLU ALA
SEQRES 12 D 265 ARG LEU ARG LEU GLY TYR GLY LYS GLU HIS ALA LYS PHE
SEQRES 13 D 265 ILE PRO VAL SER LEU ALA ILE VAL ARG TYR TYR PRO LYS
SEQRES 14 D 265 VAL GLU ILE LEU GLY ASN CYS GLU LYS GLY ALA THR VAL
SEQRES 15 D 265 CYS PRO GLU GLY VAL PHE GLU LEU LYS ASP GLY LYS LEU
SEQRES 16 D 265 SER VAL LYS ASN GLU LEU ALA CYS THR LEU CYS GLU GLU
SEQRES 17 D 265 CYS LEU ARG TYR CYS ASN GLY LEU ILE ARG ILE SER SER
SEQRES 18 D 265 VAL GLU ASP LYS TYR ILE LEU GLU LEU GLU SER VAL GLY
SEQRES 19 D 265 SER LEU LYS PRO GLU ARG ILE LEU LEU GLU ALA GLY LYS
SEQRES 20 D 265 SER ILE ILE ARG LYS ILE GLU GLU LEU GLU LYS LYS LEU
SEQRES 21 D 265 VAL GLU VAL ILE LYS
SEQRES 1 E 180 MET TYR LYS LEU ILE LYS ALA ARG SER ILE VAL ARG ILE
SEQRES 2 E 180 PRO PRO ASN GLU PHE GLY LYS PRO LEU ASN GLU ILE ALA
SEQRES 3 E 180 LEU ASN GLU LEU ARG GLN GLN TYR GLN GLU LYS ILE LEU
SEQRES 4 E 180 LYS ASP LEU GLY LEU VAL LEU ALA ILE LEU ASN VAL LYS
SEQRES 5 E 180 THR SER GLU GLU GLY ILE LEU VAL PHE GLY ASP GLY ALA
SEQRES 6 E 180 THR TYR HIS GLU VAL GLU PHE ASP MET ILE THR TYR VAL
SEQRES 7 E 180 PRO VAL VAL GLN GLU VAL VAL GLU GLY GLU VAL LEU GLN
SEQRES 8 E 180 VAL ASP ASN TYR GLY ILE PHE VAL ASN LEU GLY PRO MET
SEQRES 9 E 180 ASP GLY LEU VAL HIS ILE SER GLN ILE THR ASP ASP THR
SEQRES 10 E 180 LEU LYS TYR ASP ASN VAL ARG GLY ILE ILE PHE GLY GLU
SEQRES 11 E 180 LYS SER LYS LYS VAL ILE GLN LYS GLY ASP LYS VAL ARG
SEQRES 12 E 180 ALA ARG VAL ILE SER VAL ALA SER THR VAL THR GLY ARG
SEQRES 13 E 180 LEU PRO ARG ILE ALA LEU THR MET ARG GLN PRO TYR LEU
SEQRES 14 E 180 GLY LYS LEU GLU TRP ILE THR GLN ALA LYS LYS
SEQRES 1 F 113 MET SER SER VAL TYR ILE VAL GLU GLU HIS TYR ILE PRO
SEQRES 2 F 113 TYR SER VAL ALA LYS LYS LEU LEU SER ASP VAL ILE LYS
SEQRES 3 F 113 SER GLY SER SER SER ASN LEU LEU GLN ARG THR TYR ASP
SEQRES 4 F 113 TYR LEU ASN SER VAL GLU LYS CYS ASP ALA GLU SER ALA
SEQRES 5 F 113 GLN LYS VAL VAL GLU GLU LEU SER SER ILE ILE SER ARG
SEQRES 6 F 113 GLU ASP VAL ARG ALA VAL LEU ALA SER ILE CYS PRO ILE
SEQRES 7 F 113 THR PRO ASP GLU VAL ARG SER ILE LEU ILE MET ASP SER
SEQRES 8 F 113 ASN ARG THR TYR THR SER GLU ASP ILE GLN LYS ILE ILE
SEQRES 9 F 113 ASP ILE ILE ARG LYS TYR ILE LYS SER
SEQRES 1 G 132 MET MET GLU SER LYS ALA GLN GLU ILE ILE LEU SER CYS
SEQRES 2 G 132 GLU ILE ASN SER ILE GLU ARG GLY SER LEU LYS ASN LEU
SEQRES 3 G 132 SER ILE ILE HIS MET SER CYS ASN ASP PHE ASN ILE SER
SEQRES 4 G 132 PHE ASP ILE ILE ASP SER ILE ASN ILE PHE SER GLN LYS
SEQRES 5 G 132 GLU LYS VAL LYS ALA PHE ILE SER LYS ASN ARG LEU SER
SEQRES 6 G 132 TYR THR ASN ASP ASP PHE CYS GLY HIS GLY TYR ILE VAL
SEQRES 7 G 132 THR GLU LEU LYS ASP SER SER SER ASN ASN GLY ASN ARG
SEQRES 8 G 132 TYR ILE THR ILE ILE SER LEU PHE GLY LEU LEU VAL LYS
SEQRES 9 G 132 ILE ILE SER ASN LYS GLU SER PHE LEU LYS ILE HIS GLN
SEQRES 10 G 132 LEU ASN VAL MET ASP HIS ILE TYR PHE CYS VAL LYS LYS
SEQRES 11 G 132 ASN THR
SEQRES 1 H 84 MET ARG GLY SER SER ASN ARG LYS ILE ASP PRO ARG ILE
SEQRES 2 H 84 HIS TYR LEU VAL PRO LYS HIS GLU VAL LEU SER ILE ASP
SEQRES 3 H 84 GLU ALA TYR LYS ILE LEU LYS GLU LEU GLY ILE ARG PRO
SEQRES 4 H 84 GLU GLN LEU PRO TRP ILE ARG ALA SER ASP PRO VAL ALA
SEQRES 5 H 84 ARG SER ILE ASN ALA LYS PRO GLY ASP ILE ILE ARG ILE
SEQRES 6 H 84 ILE ARG LYS SER GLN LEU TYR GLY GLU VAL VAL SER TYR
SEQRES 7 H 84 ARG TYR VAL ILE SER GLY
SEQRES 1 K 95 MET GLY LEU GLU ARG ASP GLY ILE LEU SER GLN ASP LEU
SEQRES 2 K 95 HIS PHE ASN GLU VAL PHE ILE SER LEU TRP GLN ASN ARG
SEQRES 3 K 95 LEU THR ARG TYR GLU ILE ALA ARG VAL ILE SER ALA ARG
SEQRES 4 K 95 ALA LEU GLN LEU ALA MET GLY ALA PRO ALA LEU ILE ASP
SEQRES 5 K 95 ILE ASN ASN LEU SER SER THR ASP VAL ILE SER ILE ALA
SEQRES 6 K 95 GLU GLU GLU PHE ARG ARG GLY VAL LEU PRO ILE THR ILE
SEQRES 7 K 95 ARG ARG ARG LEU PRO ASN GLY LYS ILE ILE LEU LEU SER
SEQRES 8 K 95 LEU ARG LYS SER
SEQRES 1 L 92 MET GLU ILE LYS ILE LEU LYS SER GLU SER ASN TYR LEU
SEQRES 2 L 92 GLU LEU GLU ILE GLU GLY GLU ASP HIS THR LEU GLY ASN
SEQRES 3 L 92 LEU ILE ALA GLY THR LEU ARG LYS ILE SER GLY VAL SER
SEQRES 4 L 92 PHE ALA SER TYR TYR GLN PRO HIS PRO LEU THR ASP LYS
SEQRES 5 L 92 ILE ILE VAL LYS ILE LEU THR ASP GLY SER ILE ALA PRO
SEQRES 6 L 92 LYS ASP ALA LEU LEU LYS ALA ILE GLU THR VAL ARG VAL
SEQRES 7 L 92 MET ALA SER HIS TYR ILE ASP GLU ILE LYS GLY LEU THR
SEQRES 8 L 92 LYS
SEQRES 1 N 66 MET MET ILE PRO ILE ARG CYS PHE THR CYS GLY SER LEU
SEQRES 2 N 66 ILE ALA ASP LYS TRP GLN PRO PHE ILE THR ARG VAL ASN
SEQRES 3 N 66 ALA GLY GLU ASN PRO GLY LYS VAL LEU ASP ASP LEU GLY
SEQRES 4 N 66 VAL LYS ARG TYR CYS CYS ARG ARG MET LEU LEU SER HIS
SEQRES 5 N 66 ILE ASP ILE ILE SER GLU VAL ILE HIS TYR THR ARG PRO
SEQRES 6 N 66 ILE
SEQRES 1 P 48 MET ALA VAL TYR ARG CYS GLY LYS CYS TRP LYS THR PHE
SEQRES 2 P 48 THR ASP GLU GLN LEU LYS VAL LEU PRO GLY VAL ARG CYS
SEQRES 3 P 48 PRO TYR CYS GLY TYR LYS ILE ILE PHE MET VAL ARG LYS
SEQRES 4 P 48 PRO THR ILE LYS ILE VAL LYS ALA ILE
SEQRES 1 Q 104 MET VAL SER GLY MET SER THR GLU GLU GLU LYS GLU GLY
SEQRES 2 Q 104 THR ASN ASP GLU GLU VAL SER GLU GLU ARG GLU VAL GLU
SEQRES 3 Q 104 GLU THR SER GLU GLU GLU PHE PRO LYS LEU SER ILE GLN
SEQRES 4 Q 104 ILE ILE GLU LEU LEU MET LYS ASN THR GLU ILE TRP ASP
SEQRES 5 Q 104 ASN LEU LEU ASN GLY LYS ILE SER VAL ASP GLU ALA LYS
SEQRES 6 Q 104 ARG LEU PHE GLU ASP ASN TYR LYS ASP TYR GLU LYS ARG
SEQRES 7 Q 104 ASP SER ARG ARG LYS ALA LYS LYS ALA ALA SER LYS LYS
SEQRES 8 Q 104 VAL LYS LYS THR LYS LYS LYS GLU LYS SER VAL GLU GLY
HET ZN A1300 1
HET ZN A1350 1
HET ZN A1360 1
HET MG A1400 1
HET ZN B1300 1
HET ZN B1400 1
HET ZN B1500 1
HET ZN C1000 1
HET F3S D1001 7
HET ZN N 100 1
HET ZN P 50 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM F3S FE3-S4 CLUSTER
FORMUL 14 ZN 9(ZN 2+)
FORMUL 17 MG MG 2+
FORMUL 22 F3S FE3 S4
HELIX 1 1 SER A 15 LYS A 21 1 7
HELIX 2 2 PHE A 86 ALA A 96 1 11
HELIX 3 3 LYS A 113 TYR A 118 1 6
HELIX 4 4 TRP A 125 ARG A 130 1 6
HELIX 5 5 THR A 133 LYS A 138 1 6
HELIX 6 6 THR A 176 GLU A 185 1 10
HELIX 7 7 PRO A 188 GLY A 196 1 9
HELIX 8 8 ARG A 203 MET A 207 1 5
HELIX 9 9 PRO A 216 ARG A 220 5 5
HELIX 10 10 ASP A 234 ARG A 244 1 11
HELIX 11 11 ARG A 244 SER A 252 1 9
HELIX 12 12 PRO A 258 ASP A 278 1 21
HELIX 13 13 THR A 297 GLY A 304 1 8
HELIX 14 14 LYS A 4 SER A 314 1 276
HELIX 15 15 PRO A 340 LEU A 347 1 8
HELIX 16 16 ASN A 357 GLY A 368 1 12
HELIX 17 17 GLU A 396 THR A 400 5 5
HELIX 18 18 ASN A 446 CYS A 450 5 5
HELIX 19 19 SER A 469 ILE A 479 1 11
HELIX 20 20 VAL A 482 ASN A 485 5 4
HELIX 21 21 GLN A 500 VAL A 511 1 12
HELIX 22 22 THR A 517 GLY A 526 1 10
HELIX 23 23 GLY A 548 ALA A 554 1 7
HELIX 24 24 SER A 570 LEU A 574 5 5
HELIX 25 25 SER A 610 GLU A 618 1 9
HELIX 26 26 SER A 620 GLY A 643 1 24
HELIX 27 27 ARG A 647 VAL A 651 5 5
HELIX 28 28 VAL A 657 LYS A 680 1 24
HELIX 29 29 THR A 691 TYR A 718 1 28
HELIX 30 30 ASN A 723 ALA A 729 1 7
HELIX 31 31 ASN A 739 ALA A 745 1 7
HELIX 32 32 SER A 775 ARG A 779 5 5
HELIX 33 33 LYS A 791 VAL A 811 1 21
HELIX 34 34 ARG A 812 ASN A 825 1 14
HELIX 35 35 ASN A 869 VAL A 875 1 7
HELIX 36 36 SER B 9 LYS B 24 1 16
HELIX 37 37 HIS B 30 ASN B 40 1 11
HELIX 38 38 LEU B 42 ASP B 47 1 6
HELIX 39 39 SER B 84 ASN B 92 1 9
HELIX 40 40 ASP B 131 GLN B 135 5 5
HELIX 41 41 THR B 137 GLY B 145 1 9
HELIX 42 42 PHE B 226 LEU B 233 1 8
HELIX 43 43 THR B 237 SER B 246 1 10
HELIX 44 44 ASN B 267 ALA B 280 1 14
HELIX 45 45 LYS B 284 PHE B 300 1 17
HELIX 46 46 SER B 307 ARG B 311 5 5
HELIX 47 47 ARG B 311 LYS B 313 5 3
HELIX 48 48 LYS B 314 LEU B 330 1 17
HELIX 49 49 HIS B 340 ALA B 342 5 3
HELIX 50 50 LEU B 348 LYS B 374 1 27
HELIX 51 51 THR B 394 HIS B 399 1 6
HELIX 52 52 ASN B 421 LEU B 429 1 9
HELIX 53 53 HIS B 449 GLN B 452 5 4
HELIX 54 54 ASN B 484 GLU B 489 1 6
HELIX 55 55 LYS B 490 LEU B 492 5 3
HELIX 56 56 PRO B 499 ARG B 505 1 7
HELIX 57 57 ASP B 535 GLY B 550 1 16
HELIX 58 58 LEU B 591 GLU B 595 5 5
HELIX 59 59 THR B 606 GLN B 613 1 8
HELIX 60 60 GLU B 622 ASN B 626 5 5
HELIX 61 61 GLU B 632 LEU B 636 5 5
HELIX 62 62 TRP B 646 LEU B 651 5 6
HELIX 63 63 ILE B 653 ILE B 658 5 6
HELIX 64 64 TYR B 660 ASN B 664 5 5
HELIX 65 65 GLN B 665 ALA B 676 1 12
HELIX 66 66 ARG B 709 GLY B 715 1 7
HELIX 67 67 ARG B 745 GLU B 749 1 5
HELIX 68 68 GLY B 788 ARG B 793 5 6
HELIX 69 69 PRO B 896 MET B 900 5 5
HELIX 70 70 THR B 923 GLY B 940 1 18
HELIX 71 71 PRO B 952 TYR B 963 1 12
HELIX 72 72 MET B 999 LYS B 1003 5 5
HELIX 73 73 GLY B 1022 GLU B 1026 5 5
HELIX 74 74 GLY B 1032 PHE B 1042 1 11
HELIX 75 75 THR B 1044 LEU B 1053 1 10
HELIX 76 76 TYR B 1098 SER B 1109 1 12
HELIX 77 77 LEU C 13 SER C 21 1 9
HELIX 78 78 ASN C 22 LYS C 27 5 6
HELIX 79 79 GLU C 30 LEU C 42 1 13
HELIX 80 80 LYS C 50 ALA C 55 1 6
HELIX 81 81 ALA C 69 GLU C 80 1 12
HELIX 82 82 PRO C 81 GLN C 84 5 4
HELIX 83 83 GLY C 103 VAL C 111 1 9
HELIX 84 84 ASP C 133 GLU C 145 1 13
HELIX 85 85 VAL C 181 ASP C 183 5 3
HELIX 86 86 VAL C 184 ASN C 189 1 6
HELIX 87 87 LEU C 222 LEU C 227 1 6
HELIX 88 88 ASN C 257 LEU C 262 1 6
HELIX 89 89 ASP C 268 VAL C 272 5 5
HELIX 90 90 GLU C 279 PHE C 284 1 6
HELIX 91 91 ILE C 286 GLU C 303 1 18
HELIX 92 92 ASP C 309 ARG C 322 1 14
HELIX 93 93 LEU C 342 PHE C 347 1 6
HELIX 94 94 GLU C 348 THR C 350 5 3
HELIX 95 95 VAL C 351 ARG C 360 1 10
HELIX 96 96 GLY C 368 ILE C 375 1 8
HELIX 97 97 LEU C 381 MET C 385 5 5
HELIX 98 98 PRO D 21 LEU D 34 1 14
HELIX 99 99 TYR D 54 ILE D 65 1 12
HELIX 100 100 GLU D 71 TYR D 76 1 6
HELIX 101 101 LYS D 112 ILE D 114 5 3
HELIX 102 102 TYR D 149 ALA D 154 1 6
HELIX 103 103 GLU D 177 VAL D 182 1 6
HELIX 104 104 GLU D 207 CYS D 213 1 7
HELIX 105 105 LYS D 237 VAL D 263 1 27
HELIX 106 106 PRO E 14 PHE E 18 5 5
HELIX 107 107 PRO E 21 GLN E 32 1 12
HELIX 108 108 LYS E 171 GLN E 177 1 7
HELIX 109 109 ALA F 17 SER F 22 1 6
HELIX 110 110 ASP F 23 ILE F 25 5 3
HELIX 111 111 SER F 31 GLU F 45 1 15
HELIX 112 112 SER F 51 SER F 60 1 10
HELIX 113 113 ARG F 65 CYS F 76 1 12
HELIX 114 114 GLU F 82 ILE F 86 5 5
HELIX 115 115 SER H 24 GLY H 36 1 13
HELIX 116 116 ARG H 38 LEU H 42 5 5
HELIX 117 117 ASP H 49 ASN H 56 1 8
HELIX 118 118 LEU K 13 TRP K 23 1 11
HELIX 119 119 THR K 28 ALA K 44 1 17
HELIX 120 120 ILE K 62 ARG K 71 1 10
HELIX 121 121 ASP L 21 THR L 31 1 11
HELIX 122 122 ALA L 64 GLY L 89 1 26
HELIX 123 123 ILE N 14 ASP N 16 5 3
HELIX 124 124 LYS N 17 ASN N 26 1 10
HELIX 125 125 ASN N 30 LEU N 38 1 9
HELIX 126 126 ARG N 42 SER N 51 1 10
HELIX 127 127 ILE N 55 ILE N 60 1 6
HELIX 128 128 GLU Q 42 ASN Q 53 1 12
HELIX 129 129 SER Q 60 LYS Q 73 1 14
SHEET 1 BA 3 ARG B1115 GLU B1119 0
SHEET 2 BA 3 ASN A 5 LYS A 10 -1 O ASN A 5 N GLU B1119
SHEET 3 BA 3 VAL C 363 GLU C 364 -1 O GLU C 364 N ILE A 9
SHEET 1 AA 2 GLY A 73 ILE A 82 0
SHEET 2 AA 2 ILE A 208 VAL A 214 -1 O LEU A 209 N VAL A 81
SHEET 1 AB 7 SER A 321 PRO A 328 0
SHEET 2 AB 7 GLU A 461 HIS A 465 -1 O MET A 462 N THR A 324
SHEET 3 AB 7 VAL A 416 ASN A 420 -1 O LEU A 418 N HIS A 465
SHEET 4 AB 7 MET A 430 VAL A 437 -1 O MET A 431 N PHE A 419
SHEET 5 AB 7 GLU A 336 VAL A 339 1 O VAL A 337 N ARG A 436
SHEET 6 AB 7 PHE A 443 LEU A 445 -1 O ARG A 444 N GLY A 338
SHEET 7 AB 7 SER A 321 PRO A 328 1 O VAL A 325 N PHE A 443
SHEET 1 AC 4 THR A 348 ARG A 352 0
SHEET 2 AC 4 VAL A 406 HIS A 410 -1 O VAL A 407 N GLU A 351
SHEET 3 AC 4 ALA A 375 ILE A 379 -1 N ASN A 376 O GLU A 408
SHEET 4 AC 4 ARG A 385 ASP A 387 -1 O ILE A 386 N VAL A 378
SHEET 1 AD 2 LEU A 515 LEU A 516 0
SHEET 2 AD 2 TYR A 546 THR A 547 -1 O TYR A 546 N LEU A 516
SHEET 1 AE 3 PHE A 562 GLN A 565 0
SHEET 2 AE 3 TYR A 585 LYS A 589 -1 O VAL A 586 N GLY A 564
SHEET 3 AE 3 ILE A 592 GLU A 595 -1 O ILE A 592 N LYS A 589
SHEET 1 AF 2 GLY A 748 GLN A 749 0
SHEET 2 AF 2 PHE A 781 ILE A 782 -1 O ILE A 782 N GLY A 748
SHEET 1 AG 2 SER A 751 VAL A 752 0
SHEET 2 AG 2 GLU A 755 ARG A 756 -1 O GLU A 755 N VAL A 752
SHEET 1 AH 3 ARG A 831 ALA A 832 0
SHEET 2 AH 3 THR A 837 ARG A 839 -1 O ARG A 839 N ARG A 831
SHEET 3 AH 3 VAL A 845 VAL A 848 -1 N ILE A 846 O VAL A 838
SHEET 1 BB 3 LEU B 59 ILE B 68 0
SHEET 2 BB 3 ALA B 96 GLU B 107 -1 O TRP B 100 N ARG B 67
SHEET 3 BB 3 GLU B 115 PRO B 123 -1 O GLU B 115 N MET B 103
SHEET 1 BC 2 ARG B 72 GLU B 75 0
SHEET 2 BC 2 GLY B 79 GLU B 82 -1 O GLY B 79 N GLU B 75
SHEET 1 BD 3 PHE B 155 VAL B 157 0
SHEET 2 BD 3 SER B 160 ILE B 164 -1 O SER B 160 N VAL B 157
SHEET 3 BD 3 SER B 414 LEU B 416 -1 O GLN B 415 N VAL B 163
SHEET 1 BE 3 LYS B 344 ARG B 347 0
SHEET 2 BE 3 THR B 166 LEU B 170 -1 O GLN B 167 N ARG B 347
SHEET 3 BE 3 VAL B 432 SER B 434 1 O ILE B 433 N GLU B 168
SHEET 1 BF 5 VAL B 175 THR B 179 0
SHEET 2 BF 5 HIS B 188 SER B 194 -1 O THR B 189 N ASP B 178
SHEET 3 BF 5 THR B 204 LYS B 209 -1 O THR B 204 N SER B 194
SHEET 4 BF 5 HIS B 214 SER B 216 -1 O HIS B 214 N LYS B 209
SHEET 5 BF 5 ILE B 224 PRO B 225 -1 O ILE B 224 N VAL B 215
SHEET 1 BG 7 GLN B 478 ILE B 479 0
SHEET 2 BG 7 VAL B 578 ILE B 584 -1 O ARG B 579 N GLN B 478
SHEET 3 BG 7 ILE B 616 LEU B 619 -1 O GLU B 617 N LEU B 582
SHEET 4 BG 7 VAL B 578 ILE B 584 -1 O ARG B 580 N LEU B 619
SHEET 5 BG 7 VAL B 629 ALA B 630 0
SHEET 6 BG 7 HIS B 642 GLU B 644 1 O HIS B 642 N ALA B 630
SHEET 7 BG 7 VAL B 578 ILE B 584 -1 O ILE B 583 N LEU B 643
SHEET 1 BH 4 LEU B 529 GLY B 531 0
SHEET 2 BH 4 LYS B 522 LEU B 525 -1 O VAL B 523 N VAL B 530
SHEET 3 BH 4 GLU B 568 ASN B 572 1 O VAL B 569 N ILE B 524
SHEET 4 BH 4 ASN B 557 ILE B 561 -1 O ASN B 557 N ASN B 572
SHEET 1 BI 8 ARG B 694 ALA B 695 0
SHEET 2 BI 8 SER B 755 GLU B 764 -1 O PHE B 758 N ALA B 695
SHEET 3 BI 8 LYS B 863 ARG B 873 -1 O VAL B 865 N THR B 763
SHEET 4 BI 8 GLY B 848 GLU B 857 -1 O ILE B 849 N ARG B 870
SHEET 5 BI 8 GLU B 806 VAL B 807 -1 O VAL B 807 N GLY B 848
SHEET 6 BI 8 GLY B 848 GLU B 857 -1 O GLY B 848 N VAL B 807
SHEET 7 BI 8 ILE P 34 PHE P 35 -1 O ILE P 34 N ILE B 855
SHEET 8 BI 8 GLY B 848 GLU B 857 -1 O ILE B 855 N ILE P 34
SHEET 1 BJ 7 ASN B 723 VAL B 729 0
SHEET 2 BJ 7 PHE B 988 LYS B 995 -1 O GLY B 989 N LEU B 727
SHEET 3 BJ 7 LYS B 880 SER B 883 -1 O ALA B 882 N GLN B 994
SHEET 4 BJ 7 LYS B 888 ILE B 895 -1 O GLY B 889 N PHE B 881
SHEET 5 BJ 7 ILE B 741 ASN B 744 1 O ILE B 741 N GLY B 892
SHEET 6 BJ 7 VAL B 911 LEU B 913 -1 O ILE B 912 N ILE B 742
SHEET 7 BJ 7 ASN B 723 VAL B 729 1 O ILE B 726 N VAL B 911
SHEET 1 BK 2 VAL B 812 ILE B 814 0
SHEET 2 BK 2 ILE B 840 VAL B 841 -1 O ILE B 840 N LEU B 813
SHEET 1 BL 2 TYR B 902 THR B 903 0
SHEET 2 BL 2 THR B 973 TYR B 974 -1 O TYR B 974 N TYR B 902
SHEET 1 BM 2 ARG B1058 VAL B1063 0
SHEET 2 BM 2 PHE B1092 SER B1097 -1 O PHE B1092 N VAL B1063
SHEET 1 CA 4 ALA C 240 GLN C 243 0
SHEET 2 CA 4 ILE C 250 THR C 253 -1 O ILE C 250 N GLN C 243
SHEET 3 CA 4 MET C 122 ILE C 124 -1 O MET C 122 N THR C 253
SHEET 4 CA 4 GLU C 273 THR C 274 -1 O GLU C 273 N THR C 123
SHEET 1 CB 4 VAL C 153 ILE C 158 0
SHEET 2 CB 4 SER C 164 LEU C 169 -1 O ILE C 166 N SER C 157
SHEET 3 CB 4 THR C 205 ILE C 208 -1 O THR C 205 N LEU C 167
SHEET 4 CB 4 ILE C 198 GLU C 200 -1 O ASP C 199 N LEU C 206
SHEET 1 EA11 ILE E 38 LEU E 39 0
SHEET 2 EA11 GLY E 43 THR E 53 -1 O GLY E 43 N LEU E 39
SHEET 3 EA11 THR E 66 TYR E 77 -1 O GLU E 71 N LYS E 52
SHEET 4 EA11 VAL F 4 ILE F 12 0
SHEET 5 EA11 TYR E 2 ILE E 13 -1 O TYR E 2 N ILE F 12
SHEET 6 EA11 THR E 66 TYR E 77 -1 O THR E 66 N ILE E 13
SHEET 7 EA11 ILE K 87 LEU K 89 0
SHEET 8 EA11 ILE K 76 ARG K 81 -1 O ARG K 80 N ILE K 88
SHEET 9 EA11 GLU C 387 MET C 390 -1 O GLU C 387 N ARG K 79
SHEET 10 EA11 GLY E 57 LEU E 59 -1 O GLY E 57 N MET C 390
SHEET 11 EA11 THR E 66 TYR E 77 -1 O TYR E 67 N ILE E 58
SHEET 1 DA 4 ILE D 3 LYS D 8 0
SHEET 2 DA 4 ARG D 12 GLU D 18 -1 O ASP D 14 N LEU D 6
SHEET 3 DA 4 LYS D 225 GLU D 231 -1 O TYR D 226 N PHE D 17
SHEET 4 DA 4 ILE D 163 TYR D 166 -1 O ILE D 163 N GLU D 229
SHEET 1 DB 4 THR D 94 ALA D 102 0
SHEET 2 DB 4 GLN D 137 GLY D 148 -1 O GLN D 137 N ALA D 102
SHEET 3 DB 4 VAL D 38 ASN D 49 -1 O VAL D 38 N GLY D 148
SHEET 4 DB 4 LYS P 43 LYS P 46 -1 O LYS P 43 N PHE D 46
SHEET 1 DC 2 MET D 108 TYR D 110 0
SHEET 2 DC 2 PRO D 129 LEU D 132 -1 N ILE D 130 O LEU D 109
SHEET 1 DD 2 VAL D 170 ILE D 172 0
SHEET 2 DD 2 ILE D 217 ILE D 219 -1 O ARG D 218 N GLU D 171
SHEET 1 EB 4 VAL E 108 HIS E 109 0
SHEET 2 EB 4 GLY E 96 VAL E 99 -1 O ILE E 97 N VAL E 108
SHEET 3 EB 4 GLY E 87 VAL E 92 -1 N LEU E 90 O PHE E 98
SHEET 4 EB 4 LYS E 141 VAL E 142 -1 O VAL E 142 N GLY E 87
SHEET 1 EC 2 ARG E 145 ALA E 150 0
SHEET 2 EC 2 ARG E 159 THR E 163 -1 O ARG E 159 N ALA E 150
SHEET 1 GA 9 PHE G 71 CYS G 72 0
SHEET 2 GA 9 PHE G 112 ILE G 115 -1 O ILE G 115 N PHE G 71
SHEET 3 GA 9 LYS G 54 SER G 60 -1 O PHE G 58 N LYS G 114
SHEET 4 GA 9 ILE G 9 ARG G 20 -1 O ILE G 9 N ILE G 59
SHEET 5 GA 9 LEU G 26 SER G 32 -1 O ILE G 28 N GLU G 19
SHEET 6 GA 9 ASN G 37 ILE G 43 -1 O ILE G 38 N MET G 31
SHEET 7 GA 9 ASN G 90 ILE G 95 -1 O ILE G 93 N SER G 39
SHEET 8 GA 9 ASP G 83 ASN G 87 -1 O ASP G 83 N THR G 94
SHEET 9 GA 9 TYR G 76 THR G 79 -1 O TYR G 76 N SER G 86
SHEET 1 HA 3 LYS H 19 VAL H 22 0
SHEET 2 HA 3 ILE H 63 SER H 69 -1 O ARG H 64 N GLU H 21
SHEET 3 HA 3 GLY H 73 TYR H 78 -1 O GLY H 73 N SER H 69
SHEET 1 LA 4 GLU L 2 GLU L 9 0
SHEET 2 LA 4 TYR L 12 GLU L 18 -1 O TYR L 12 N GLU L 9
SHEET 3 LA 4 ILE L 53 THR L 59 -1 O ILE L 53 N ILE L 17
SHEET 4 LA 4 VAL L 38 TYR L 44 -1 N SER L 39 O LEU L 58
SSBOND 1 CYS A 98 CYS A 101 1555 1555 2.04
SSBOND 2 CYS A 575 CYS A 580 1555 1555 2.03
SSBOND 3 CYS D 82 CYS D 92 1555 1555 2.04
SSBOND 4 CYS D 85 CYS D 89 1555 1555 2.03
SSBOND 5 CYS D 176 CYS D 213 1555 1555 2.03
SSBOND 6 CYS G 13 CYS G 33 1555 1555 2.03
SSBOND 7 CYS N 10 CYS N 45 1555 1555 2.04
SSBOND 8 CYS P 26 CYS P 29 1555 1555 2.04
LINK SG CYS A 58 ZN ZN A1300 1555 1555 2.49
LINK SG CYS A 68 ZN ZN A1300 1555 1555 2.33
LINK NE2 HIS A 71 ZN ZN A1300 1555 1555 2.06
LINK SG CYS A 98 ZN ZN A1350 1555 1555 2.26
LINK OD1 ASP A 456 MG MG A1400 1555 1555 2.36
LINK OD1 ASP A 458 MG MG A1400 1555 1555 2.46
LINK OD1 ASP A 460 MG MG A1400 1555 1555 2.61
LINK ZN ZN A1360 OE2 GLU C 80 1555 1555 1.96
LINK ND1 HIS B 570 ZN ZN B1400 1555 1555 2.25
LINK SG CYS B1064 ZN ZN B1300 1555 1555 2.11
LINK SG CYS B1067 ZN ZN B1300 1555 1555 2.44
LINK NE2 HIS C 353 ZN ZN C1000 1555 1555 1.89
LINK SG CYS D 203 FE3 F3S D1001 1555 1555 2.32
LINK SG CYS D 206 FE4 F3S D1001 1555 1555 2.65
LINK SG CYS D 209 FE1 F3S D1001 1555 1555 2.22
LINK SG CYS N 7 ZN ZN N 100 1555 1555 2.35
LINK SG CYS N 10 ZN ZN N 100 1555 1555 2.08
LINK SG CYS N 45 ZN ZN N 100 1555 1555 2.36
LINK SG CYS P 9 ZN ZN P 50 1555 1555 2.37
LINK OG1 THR P 12 ZN ZN P 50 1555 1555 2.51
LINK SG CYS P 29 ZN ZN P 50 1555 1555 1.63
CISPEP 1 LYS A 155 ILE A 156 0 3.97
CISPEP 2 PRO A 285 PRO A 286 0 -13.32
CISPEP 3 GLN A 422 PRO A 423 0 5.49
CISPEP 4 SER B 76 ASP B 77 0 5.11
CISPEP 5 ILE B 110 GLU B 111 0 -6.87
CISPEP 6 GLU B 113 PRO B 114 0 -3.59
CISPEP 7 GLY B 734 TYR B 735 0 -7.10
CISPEP 8 VAL B 783 ARG B 784 0 -1.23
CISPEP 9 TYR B 1069 ILE B 1070 0 -3.89
CISPEP 10 ASP B 1074 LYS B 1075 0 1.12
CISPEP 11 LYS B 1077 ASN B 1078 0 3.08
CISPEP 12 MET C 163 SER C 164 0 4.13
CISPEP 13 LYS C 244 LYS C 245 0 -7.26
CISPEP 14 LEU P 21 PRO P 22 0 -0.76
SITE 1 AC1 4 CYS A 58 CYS A 61 CYS A 68 HIS A 71
SITE 1 AC2 4 CYS A 98 CYS A 101 VAL A 145 CYS A 146
SITE 1 AC3 2 HIS A 426 GLU C 80
SITE 1 AC4 3 ASP A 456 ASP A 458 ASP A 460
SITE 1 AC5 3 CYS B1064 CYS B1067 CYS B1082
SITE 1 AC6 3 ARG B 174 HIS B 570 GLU B 622
SITE 1 AC7 3 ARG B 694 HIS B 696 HIS B 997
SITE 1 AC8 2 GLU C 348 HIS C 353
SITE 1 AC9 8 CYS D 183 PHE D 188 CYS D 203 LEU D 205
SITE 2 AC9 8 CYS D 206 GLU D 207 CYS D 209 ILE D 219
SITE 1 BC1 4 CYS N 7 CYS N 10 CYS N 44 CYS N 45
SITE 1 BC2 4 CYS P 9 THR P 12 CYS P 26 CYS P 29
CRYST1 193.501 212.620 128.998 90.00 90.00 90.00 P 21 21 2 4
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 0.005168 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007752 0.00000
(ATOM LINES ARE NOT SHOWN.)
END