HEADER TRANSFERASE/RNA 12-SEP-07 2R93
TITLE ELONGATION COMPLEX OF RNA POLYMERASE II WITH A HEPATITIS DELTA VIRUS-
TITLE 2 DERIVED RNA STEM LOOP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA (5'-
COMPND 3 R(*UP*GP*AP*UP*UP*CP*UP*CP*UP*AP*UP*CP*GP*GP*AP*AP*UP*C)-3');
COMPND 4 CHAIN: R;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;
COMPND 8 CHAIN: A;
COMPND 9 SYNONYM: RNA POLYMERASE II SUBUNIT B1, RNA POLYMERASE II SUBUNIT 1,
COMPND 10 DNA-DIRECTED RNA POLYMERASE III LARGEST SUBUNIT, B220;
COMPND 11 EC: 2.7.7.6;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;
COMPND 14 CHAIN: B;
COMPND 15 SYNONYM: RNA POLYMERASE II SUBUNIT 2, DNA-DIRECTED RNA POLYMERASE II
COMPND 16 140 KDA POLYPEPTIDE, B150;
COMPND 17 EC: 2.7.7.6;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;
COMPND 20 CHAIN: C;
COMPND 21 SYNONYM: RNA POLYMERASE II SUBUNIT B3, RNA POLYMERASE II SUBUNIT 3,
COMPND 22 DNA-DIRECTED RNA POLYMERASE II 45 KDA POLYPEPTIDE, B44.5;
COMPND 23 EC: 2.7.7.6;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4;
COMPND 26 CHAIN: D;
COMPND 27 SYNONYM: RNA POLYMERASE II SUBUNIT B4, DNA-DIRECTED RNA POLYMERASE II
COMPND 28 32 KDA POLYPEPTIDE, B32;
COMPND 29 EC: 2.7.7.6;
COMPND 30 MOL_ID: 6;
COMPND 31 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1;
COMPND 32 CHAIN: E;
COMPND 33 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC1, DNA-DIRECTED
COMPND 34 RNA POLYMERASES I, II, AND III 27 KDA POLYPEPTIDE, ABC27;
COMPND 35 EC: 2.7.7.6;
COMPND 36 MOL_ID: 7;
COMPND 37 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2;
COMPND 38 CHAIN: F;
COMPND 39 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC2, DNA-DIRECTED
COMPND 40 RNA POLYMERASES I, II, AND III 23 KDA POLYPEPTIDE, ABC23;
COMPND 41 EC: 2.7.7.6;
COMPND 42 MOL_ID: 8;
COMPND 43 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7;
COMPND 44 CHAIN: G;
COMPND 45 SYNONYM: RNA POLYMERASE II SUBUNIT B7, B16;
COMPND 46 EC: 2.7.7.6;
COMPND 47 MOL_ID: 9;
COMPND 48 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND 49 CHAIN: H;
COMPND 50 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC3, DNA-DIRECTED
COMPND 51 RNA POLYMERASES I, II, AND III 14.5 KDA POLYPEPTIDE, ABC14.4,
COMPND 52 ABC14.5;
COMPND 53 EC: 2.7.7.6;
COMPND 54 MOL_ID: 10;
COMPND 55 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;
COMPND 56 CHAIN: I;
COMPND 57 SYNONYM: RNA POLYMERASE II SUBUNIT B9, DNA-DIRECTED RNA POLYMERASE II
COMPND 58 SUBUNIT 9, DNA-DIRECTED RNA POLYMERASE II 14.2 KDA POLYPEPTIDE,
COMPND 59 B12.6;
COMPND 60 EC: 2.7.7.6;
COMPND 61 MOL_ID: 11;
COMPND 62 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5;
COMPND 63 CHAIN: J;
COMPND 64 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC5, DNA-DIRECTED
COMPND 65 RNA POLYMERASES I, II, AND III 8.3 KDA POLYPEPTIDE, ABC10-BETA, ABC8;
COMPND 66 EC: 2.7.7.6;
COMPND 67 MOL_ID: 12;
COMPND 68 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11;
COMPND 69 CHAIN: K;
COMPND 70 SYNONYM: RNA POLYMERASE II SUBUNIT B11, DNA-DIRECTED RNA POLYMERASE
COMPND 71 II 13.6 KDA POLYPEPTIDE, B13.6;
COMPND 72 EC: 2.7.7.6;
COMPND 73 MOL_ID: 13;
COMPND 74 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4;
COMPND 75 CHAIN: L;
COMPND 76 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC4, ABC10-ALPHA;
COMPND 77 EC: 2.7.7.6
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HEPATITIS DELTA
SOURCE 4 VIRUS.;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 16 ORGANISM_TAXID: 4932;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 4932;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 28 ORGANISM_TAXID: 4932;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 32 ORGANISM_TAXID: 4932;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 36 ORGANISM_TAXID: 4932;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 40 ORGANISM_TAXID: 4932;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 47 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 48 ORGANISM_TAXID: 4932;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 51 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 52 ORGANISM_TAXID: 4932
KEYWDS TRANSFERASE/DNA/RNA, DNA-BINDING, PHOSPHORYLATION, RNA POLYMERASE II,
KEYWDS 2 METAL-BINDING, NUCLEAR PROTEIN, TRANSCRIPTION BUBBLE, ELONGATION
KEYWDS 3 COMPLEX, TRANSFERASE, TRANSCRIPTION, RNA-DEPENDENT, RNA-DEPENDENT
KEYWDS 4 RNA SYNTHESIS, RDRP, DDRP, RNA-BINDING, HEPATITIS DELTA VIRUS, HDV,
KEYWDS 5 DNA-DIRECTED RNA POLYMERASE, MAGNESIUM, NUCLEOTIDYLTRANSFERASE,
KEYWDS 6 NUCLEUS, UBL CONJUGATION, ZINC, ZINC-FINGER, POLYMORPHISM,
KEYWDS 7 CYTOPLASM, DNA DAMAGE, DNA REPAIR, MRNA PROCESSING, TRANSFERASE-RNA
KEYWDS 8 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.LEHMANN,F.BRUECKNER,P.CRAMER
REVDAT 4 21-FEB-24 2R93 1 LINK
REVDAT 3 25-OCT-17 2R93 1 REMARK
REVDAT 2 24-FEB-09 2R93 1 VERSN
REVDAT 1 27-NOV-07 2R93 0
JRNL AUTH E.LEHMANN,F.BRUECKNER,P.CRAMER
JRNL TITL MOLECULAR BASIS OF RNA-DEPENDENT RNA POLYMERASE II ACTIVITY.
JRNL REF NATURE V. 450 445 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 18004386
JRNL DOI 10.1038/NATURE06290
REMARK 2
REMARK 2 RESOLUTION. 4.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 102707
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : THE SAME SET OF REFLECTIONS
REMARK 3 THAT HAS BEEN EXCLUDED FROM
REMARK 3 PREVIOUS POL II STRUCTURE
REMARK 3 DETERMINATIONS HAVE BEEN
REMARK 3 USED. KETTENBERGER ET AL.
REMARK 3 MOL. CELL 16, 955-965 (2004)
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2068
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 31202
REMARK 3 NUCLEIC ACID ATOMS : 289
REMARK 3 HETEROGEN ATOMS : 9
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) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.473
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000044578.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104533
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.14900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.47900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% (W/V) PEG 6000, 200 MM AMMONIUM
REMARK 280 ACETATE, 150 MM MAGNESIUM ACETATE, 50 MM HEPES PH 7.0, 5 MM TCEP,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 142.06050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 142.06050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 111.66800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 197.44200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 111.66800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 197.44200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 142.06050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 111.66800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 197.44200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 142.06050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 111.66800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 197.44200
REMARK 290 SMTRY3 8 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 APPLY THE FOLLOWING TO CHAINS: R, A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, 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 C R 8
REMARK 465 U R 9
REMARK 465 A R 10
REMARK 465 U R 11
REMARK 465 MET A 1
REMARK 465 ALA A 190
REMARK 465 THR A 191
REMARK 465 GLY A 192
REMARK 465 ASP A 193
REMARK 465 ALA A 194
REMARK 465 ASN A 1082
REMARK 465 THR A 1083
REMARK 465 PHE A 1084
REMARK 465 HIS A 1085
REMARK 465 PHE A 1086
REMARK 465 ALA A 1087
REMARK 465 GLY A 1088
REMARK 465 VAL A 1089
REMARK 465 ALA A 1090
REMARK 465 SER A 1091
REMARK 465 ASP A 1178
REMARK 465 GLU A 1179
REMARK 465 GLU A 1180
REMARK 465 ALA A 1181
REMARK 465 GLU A 1182
REMARK 465 GLN A 1183
REMARK 465 SER A 1184
REMARK 465 PHE A 1185
REMARK 465 ASP A 1186
REMARK 465 LYS A 1246
REMARK 465 SER A 1247
REMARK 465 LEU A 1248
REMARK 465 ASP A 1249
REMARK 465 ALA A 1250
REMARK 465 GLU A 1251
REMARK 465 THR A 1252
REMARK 465 GLU A 1253
REMARK 465 GLU A 1456
REMARK 465 GLN A 1457
REMARK 465 LYS A 1458
REMARK 465 ILE A 1459
REMARK 465 THR A 1460
REMARK 465 GLU A 1461
REMARK 465 ILE A 1462
REMARK 465 GLU A 1463
REMARK 465 ASP A 1464
REMARK 465 GLY A 1465
REMARK 465 GLN A 1466
REMARK 465 ASP A 1467
REMARK 465 GLY A 1468
REMARK 465 GLY A 1469
REMARK 465 VAL A 1470
REMARK 465 THR A 1471
REMARK 465 PRO A 1472
REMARK 465 TYR A 1473
REMARK 465 SER A 1474
REMARK 465 ASN A 1475
REMARK 465 GLU A 1476
REMARK 465 SER A 1477
REMARK 465 GLY A 1478
REMARK 465 LEU A 1479
REMARK 465 VAL A 1480
REMARK 465 ASN A 1481
REMARK 465 ALA A 1482
REMARK 465 ASP A 1483
REMARK 465 LEU A 1484
REMARK 465 ASP A 1485
REMARK 465 VAL A 1486
REMARK 465 LYS A 1487
REMARK 465 ASP A 1488
REMARK 465 GLU A 1489
REMARK 465 LEU A 1490
REMARK 465 MET A 1491
REMARK 465 PHE A 1492
REMARK 465 SER A 1493
REMARK 465 PRO A 1494
REMARK 465 LEU A 1495
REMARK 465 VAL A 1496
REMARK 465 ASP A 1497
REMARK 465 SER A 1498
REMARK 465 GLY A 1499
REMARK 465 SER A 1500
REMARK 465 ASN A 1501
REMARK 465 ASP A 1502
REMARK 465 ALA A 1503
REMARK 465 MET A 1504
REMARK 465 ALA A 1505
REMARK 465 GLY A 1506
REMARK 465 GLY A 1507
REMARK 465 PHE A 1508
REMARK 465 THR A 1509
REMARK 465 ALA A 1510
REMARK 465 TYR A 1511
REMARK 465 GLY A 1512
REMARK 465 GLY A 1513
REMARK 465 ALA A 1514
REMARK 465 ASP A 1515
REMARK 465 TYR A 1516
REMARK 465 GLY A 1517
REMARK 465 GLU A 1518
REMARK 465 ALA A 1519
REMARK 465 THR A 1520
REMARK 465 SER A 1521
REMARK 465 PRO A 1522
REMARK 465 PHE A 1523
REMARK 465 GLY A 1524
REMARK 465 ALA A 1525
REMARK 465 TYR A 1526
REMARK 465 GLY A 1527
REMARK 465 GLU A 1528
REMARK 465 ALA A 1529
REMARK 465 PRO A 1530
REMARK 465 THR A 1531
REMARK 465 SER A 1532
REMARK 465 PRO A 1533
REMARK 465 GLY A 1534
REMARK 465 PHE A 1535
REMARK 465 GLY A 1536
REMARK 465 VAL A 1537
REMARK 465 SER A 1538
REMARK 465 SER A 1539
REMARK 465 PRO A 1540
REMARK 465 GLY A 1541
REMARK 465 PHE A 1542
REMARK 465 SER A 1543
REMARK 465 PRO A 1544
REMARK 465 THR A 1545
REMARK 465 SER A 1546
REMARK 465 PRO A 1547
REMARK 465 THR A 1548
REMARK 465 TYR A 1549
REMARK 465 SER A 1550
REMARK 465 PRO A 1551
REMARK 465 THR A 1552
REMARK 465 SER A 1553
REMARK 465 PRO A 1554
REMARK 465 ALA A 1555
REMARK 465 TYR A 1556
REMARK 465 SER A 1557
REMARK 465 PRO A 1558
REMARK 465 THR A 1559
REMARK 465 SER A 1560
REMARK 465 PRO A 1561
REMARK 465 SER A 1562
REMARK 465 TYR A 1563
REMARK 465 SER A 1564
REMARK 465 PRO A 1565
REMARK 465 THR A 1566
REMARK 465 SER A 1567
REMARK 465 PRO A 1568
REMARK 465 SER A 1569
REMARK 465 TYR A 1570
REMARK 465 SER A 1571
REMARK 465 PRO A 1572
REMARK 465 THR A 1573
REMARK 465 SER A 1574
REMARK 465 PRO A 1575
REMARK 465 SER A 1576
REMARK 465 TYR A 1577
REMARK 465 SER A 1578
REMARK 465 PRO A 1579
REMARK 465 THR A 1580
REMARK 465 SER A 1581
REMARK 465 PRO A 1582
REMARK 465 SER A 1583
REMARK 465 TYR A 1584
REMARK 465 SER A 1585
REMARK 465 PRO A 1586
REMARK 465 THR A 1587
REMARK 465 SER A 1588
REMARK 465 PRO A 1589
REMARK 465 SER A 1590
REMARK 465 TYR A 1591
REMARK 465 SER A 1592
REMARK 465 PRO A 1593
REMARK 465 THR A 1594
REMARK 465 SER A 1595
REMARK 465 PRO A 1596
REMARK 465 SER A 1597
REMARK 465 TYR A 1598
REMARK 465 SER A 1599
REMARK 465 PRO A 1600
REMARK 465 THR A 1601
REMARK 465 SER A 1602
REMARK 465 PRO A 1603
REMARK 465 SER A 1604
REMARK 465 TYR A 1605
REMARK 465 SER A 1606
REMARK 465 PRO A 1607
REMARK 465 THR A 1608
REMARK 465 SER A 1609
REMARK 465 PRO A 1610
REMARK 465 SER A 1611
REMARK 465 TYR A 1612
REMARK 465 SER A 1613
REMARK 465 PRO A 1614
REMARK 465 THR A 1615
REMARK 465 SER A 1616
REMARK 465 PRO A 1617
REMARK 465 SER A 1618
REMARK 465 TYR A 1619
REMARK 465 SER A 1620
REMARK 465 PRO A 1621
REMARK 465 THR A 1622
REMARK 465 SER A 1623
REMARK 465 PRO A 1624
REMARK 465 SER A 1625
REMARK 465 TYR A 1626
REMARK 465 SER A 1627
REMARK 465 PRO A 1628
REMARK 465 THR A 1629
REMARK 465 SER A 1630
REMARK 465 PRO A 1631
REMARK 465 SER A 1632
REMARK 465 TYR A 1633
REMARK 465 SER A 1634
REMARK 465 PRO A 1635
REMARK 465 THR A 1636
REMARK 465 SER A 1637
REMARK 465 PRO A 1638
REMARK 465 SER A 1639
REMARK 465 TYR A 1640
REMARK 465 SER A 1641
REMARK 465 PRO A 1642
REMARK 465 THR A 1643
REMARK 465 SER A 1644
REMARK 465 PRO A 1645
REMARK 465 SER A 1646
REMARK 465 TYR A 1647
REMARK 465 SER A 1648
REMARK 465 PRO A 1649
REMARK 465 THR A 1650
REMARK 465 SER A 1651
REMARK 465 PRO A 1652
REMARK 465 SER A 1653
REMARK 465 TYR A 1654
REMARK 465 SER A 1655
REMARK 465 PRO A 1656
REMARK 465 THR A 1657
REMARK 465 SER A 1658
REMARK 465 PRO A 1659
REMARK 465 ALA A 1660
REMARK 465 TYR A 1661
REMARK 465 SER A 1662
REMARK 465 PRO A 1663
REMARK 465 THR A 1664
REMARK 465 SER A 1665
REMARK 465 PRO A 1666
REMARK 465 SER A 1667
REMARK 465 TYR A 1668
REMARK 465 SER A 1669
REMARK 465 PRO A 1670
REMARK 465 THR A 1671
REMARK 465 SER A 1672
REMARK 465 PRO A 1673
REMARK 465 SER A 1674
REMARK 465 TYR A 1675
REMARK 465 SER A 1676
REMARK 465 PRO A 1677
REMARK 465 THR A 1678
REMARK 465 SER A 1679
REMARK 465 PRO A 1680
REMARK 465 SER A 1681
REMARK 465 TYR A 1682
REMARK 465 SER A 1683
REMARK 465 PRO A 1684
REMARK 465 THR A 1685
REMARK 465 SER A 1686
REMARK 465 PRO A 1687
REMARK 465 SER A 1688
REMARK 465 TYR A 1689
REMARK 465 SER A 1690
REMARK 465 PRO A 1691
REMARK 465 THR A 1692
REMARK 465 SER A 1693
REMARK 465 PRO A 1694
REMARK 465 ASN A 1695
REMARK 465 TYR A 1696
REMARK 465 SER A 1697
REMARK 465 PRO A 1698
REMARK 465 THR A 1699
REMARK 465 SER A 1700
REMARK 465 PRO A 1701
REMARK 465 SER A 1702
REMARK 465 TYR A 1703
REMARK 465 SER A 1704
REMARK 465 PRO A 1705
REMARK 465 THR A 1706
REMARK 465 SER A 1707
REMARK 465 PRO A 1708
REMARK 465 GLY A 1709
REMARK 465 TYR A 1710
REMARK 465 SER A 1711
REMARK 465 PRO A 1712
REMARK 465 GLY A 1713
REMARK 465 SER A 1714
REMARK 465 PRO A 1715
REMARK 465 ALA A 1716
REMARK 465 TYR A 1717
REMARK 465 SER A 1718
REMARK 465 PRO A 1719
REMARK 465 LYS A 1720
REMARK 465 GLN A 1721
REMARK 465 ASP A 1722
REMARK 465 GLU A 1723
REMARK 465 GLN A 1724
REMARK 465 LYS A 1725
REMARK 465 HIS A 1726
REMARK 465 ASN A 1727
REMARK 465 GLU A 1728
REMARK 465 ASN A 1729
REMARK 465 GLU A 1730
REMARK 465 ASN A 1731
REMARK 465 SER A 1732
REMARK 465 ARG A 1733
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 TYR B 10
REMARK 465 TYR B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 ASP B 14
REMARK 465 PRO B 15
REMARK 465 TYR B 16
REMARK 465 GLY B 17
REMARK 465 PHE B 18
REMARK 465 LEU B 71
REMARK 465 GLU B 72
REMARK 465 GLN B 73
REMARK 465 LEU B 74
REMARK 465 ALA B 75
REMARK 465 GLN B 76
REMARK 465 HIS B 77
REMARK 465 THR B 78
REMARK 465 THR B 79
REMARK 465 GLU B 80
REMARK 465 SER B 81
REMARK 465 ASP B 82
REMARK 465 ASN B 83
REMARK 465 ILE B 84
REMARK 465 SER B 85
REMARK 465 ARG B 86
REMARK 465 LYS B 87
REMARK 465 TYR B 88
REMARK 465 GLU B 89
REMARK 465 LYS B 134
REMARK 465 ARG B 135
REMARK 465 THR B 136
REMARK 465 TYR B 137
REMARK 465 GLU B 138
REMARK 465 ALA B 139
REMARK 465 ILE B 140
REMARK 465 ASP B 141
REMARK 465 VAL B 142
REMARK 465 PRO B 143
REMARK 465 GLY B 144
REMARK 465 ARG B 145
REMARK 465 GLU B 146
REMARK 465 LEU B 147
REMARK 465 LYS B 148
REMARK 465 TYR B 149
REMARK 465 GLU B 150
REMARK 465 LEU B 151
REMARK 465 ILE B 152
REMARK 465 ALA B 153
REMARK 465 GLU B 154
REMARK 465 GLU B 155
REMARK 465 SER B 156
REMARK 465 GLU B 157
REMARK 465 ASP B 158
REMARK 465 ASP B 159
REMARK 465 SER B 160
REMARK 465 GLU B 161
REMARK 465 SER B 162
REMARK 465 GLY B 163
REMARK 465 GLU B 438
REMARK 465 ALA B 439
REMARK 465 HIS B 440
REMARK 465 ASP B 441
REMARK 465 PHE B 442
REMARK 465 ASN B 443
REMARK 465 MET B 444
REMARK 465 LYS B 445
REMARK 465 GLY B 503
REMARK 465 ARG B 504
REMARK 465 ASP B 505
REMARK 465 GLY B 506
REMARK 465 LYS B 507
REMARK 465 LEU B 508
REMARK 465 ALA B 509
REMARK 465 ILE B 669
REMARK 465 GLU B 670
REMARK 465 GLY B 671
REMARK 465 GLY B 672
REMARK 465 PHE B 673
REMARK 465 GLU B 674
REMARK 465 ASP B 675
REMARK 465 VAL B 676
REMARK 465 GLU B 677
REMARK 465 ASN B 716
REMARK 465 GLU B 717
REMARK 465 GLU B 718
REMARK 465 ASN B 719
REMARK 465 ASP B 720
REMARK 465 LEU B 721
REMARK 465 ILE B 918
REMARK 465 SER B 919
REMARK 465 PRO B 920
REMARK 465 ASP B 921
REMARK 465 GLU B 922
REMARK 465 GLU B 923
REMARK 465 GLU B 924
REMARK 465 LEU B 925
REMARK 465 GLY B 926
REMARK 465 GLN B 927
REMARK 465 ARG B 928
REMARK 465 THR B 929
REMARK 465 ALA B 930
REMARK 465 TYR B 931
REMARK 465 HIS B 932
REMARK 465 MET C 1
REMARK 465 LYS C 269
REMARK 465 VAL C 270
REMARK 465 ASN C 271
REMARK 465 PHE C 272
REMARK 465 ALA C 273
REMARK 465 SER C 274
REMARK 465 GLY C 275
REMARK 465 ASP C 276
REMARK 465 ASN C 277
REMARK 465 ASN C 278
REMARK 465 THR C 279
REMARK 465 ALA C 280
REMARK 465 SER C 281
REMARK 465 ASN C 282
REMARK 465 MET C 283
REMARK 465 LEU C 284
REMARK 465 GLY C 285
REMARK 465 SER C 286
REMARK 465 ASN C 287
REMARK 465 GLU C 288
REMARK 465 ASP C 289
REMARK 465 VAL C 290
REMARK 465 MET C 291
REMARK 465 MET C 292
REMARK 465 THR C 293
REMARK 465 GLY C 294
REMARK 465 ALA C 295
REMARK 465 GLU C 296
REMARK 465 GLN C 297
REMARK 465 ASP C 298
REMARK 465 PRO C 299
REMARK 465 TYR C 300
REMARK 465 SER C 301
REMARK 465 ASN C 302
REMARK 465 ALA C 303
REMARK 465 SER C 304
REMARK 465 GLN C 305
REMARK 465 MET C 306
REMARK 465 GLY C 307
REMARK 465 ASN C 308
REMARK 465 THR C 309
REMARK 465 GLY C 310
REMARK 465 SER C 311
REMARK 465 GLY C 312
REMARK 465 GLY C 313
REMARK 465 TYR C 314
REMARK 465 ASP C 315
REMARK 465 ASN C 316
REMARK 465 ALA C 317
REMARK 465 TRP C 318
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 HIS D 77
REMARK 465 LYS D 78
REMARK 465 LYS D 79
REMARK 465 LYS D 80
REMARK 465 HIS D 81
REMARK 465 LEU D 82
REMARK 465 LYS D 83
REMARK 465 HIS D 84
REMARK 465 GLU D 85
REMARK 465 ASN D 86
REMARK 465 ALA D 87
REMARK 465 ASN D 88
REMARK 465 ASP D 89
REMARK 465 GLU D 90
REMARK 465 THR D 91
REMARK 465 THR D 92
REMARK 465 ALA D 93
REMARK 465 VAL D 94
REMARK 465 GLU D 95
REMARK 465 ASP D 96
REMARK 465 GLU D 97
REMARK 465 ASP D 98
REMARK 465 ASP D 99
REMARK 465 ASP D 100
REMARK 465 LEU D 101
REMARK 465 ASP D 102
REMARK 465 GLU D 103
REMARK 465 ASP D 104
REMARK 465 ASP D 105
REMARK 465 VAL D 106
REMARK 465 ASN D 107
REMARK 465 ALA D 108
REMARK 465 ASP D 109
REMARK 465 ASP D 110
REMARK 465 ASP D 111
REMARK 465 ASP D 112
REMARK 465 PHE D 113
REMARK 465 MET D 114
REMARK 465 HIS D 115
REMARK 465 SER D 116
REMARK 465 GLU D 117
REMARK 465 MET E 1
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 TYR F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 ALA F 7
REMARK 465 PHE F 8
REMARK 465 ASN F 9
REMARK 465 ASP F 10
REMARK 465 GLY F 11
REMARK 465 ASN F 12
REMARK 465 GLU F 13
REMARK 465 ASN F 14
REMARK 465 PHE F 15
REMARK 465 GLU F 16
REMARK 465 ASP F 17
REMARK 465 PHE F 18
REMARK 465 ASP F 19
REMARK 465 VAL F 20
REMARK 465 GLU F 21
REMARK 465 HIS F 22
REMARK 465 PHE F 23
REMARK 465 SER F 24
REMARK 465 ASP F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 THR F 28
REMARK 465 TYR F 29
REMARK 465 GLU F 30
REMARK 465 GLU F 31
REMARK 465 LYS F 32
REMARK 465 PRO F 33
REMARK 465 GLN F 34
REMARK 465 PHE F 35
REMARK 465 LYS F 36
REMARK 465 ASP F 37
REMARK 465 GLY F 38
REMARK 465 GLU F 39
REMARK 465 THR F 40
REMARK 465 THR F 41
REMARK 465 ASP F 42
REMARK 465 ALA F 43
REMARK 465 ASN F 44
REMARK 465 GLY F 45
REMARK 465 LYS F 46
REMARK 465 THR F 47
REMARK 465 ILE F 48
REMARK 465 VAL F 49
REMARK 465 THR F 50
REMARK 465 GLY F 51
REMARK 465 GLY F 52
REMARK 465 ASN F 53
REMARK 465 GLY F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 ASP F 57
REMARK 465 PHE F 58
REMARK 465 GLN F 59
REMARK 465 GLN F 60
REMARK 465 HIS F 61
REMARK 465 GLU F 62
REMARK 465 GLN F 63
REMARK 465 ILE F 64
REMARK 465 ARG F 65
REMARK 465 ARG F 66
REMARK 465 LYS F 67
REMARK 465 MET H 1
REMARK 465 GLU H 66
REMARK 465 ASP H 67
REMARK 465 THR H 68
REMARK 465 PRO H 69
REMARK 465 ALA H 70
REMARK 465 ASN H 71
REMARK 465 ASP H 72
REMARK 465 SER H 73
REMARK 465 SER H 74
REMARK 465 ALA H 75
REMARK 465 MET I 1
REMARK 465 ARG I 118
REMARK 465 THR I 119
REMARK 465 GLN I 120
REMARK 465 PHE I 121
REMARK 465 SER I 122
REMARK 465 LEU J 66
REMARK 465 GLU J 67
REMARK 465 LYS J 68
REMARK 465 ARG J 69
REMARK 465 ASP J 70
REMARK 465 THR K 113
REMARK 465 LEU K 114
REMARK 465 ALA K 115
REMARK 465 ALA K 116
REMARK 465 ASP K 117
REMARK 465 ASP K 118
REMARK 465 ALA K 119
REMARK 465 PHE K 120
REMARK 465 MET L 1
REMARK 465 SER L 2
REMARK 465 ARG L 3
REMARK 465 GLU L 4
REMARK 465 GLY L 5
REMARK 465 PHE L 6
REMARK 465 GLN L 7
REMARK 465 ILE L 8
REMARK 465 PRO L 9
REMARK 465 THR L 10
REMARK 465 ASN L 11
REMARK 465 LEU L 12
REMARK 465 ASP L 13
REMARK 465 ALA L 14
REMARK 465 ALA L 15
REMARK 465 ALA L 16
REMARK 465 ALA L 17
REMARK 465 GLY L 18
REMARK 465 THR L 19
REMARK 465 SER L 20
REMARK 465 GLN L 21
REMARK 465 ALA L 22
REMARK 465 ARG L 23
REMARK 465 THR L 24
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 C R 12 P OP1 OP2
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 OP1 U R 7 NH2 ARG B 942 2.13
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 U R 7 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 C R 12 N1 - C1' - C2' ANGL. DEV. = 8.8 DEGREES
REMARK 500 PRO A 243 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU A1176 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 LEU A1176 N - CA - C ANGL. DEV. = 20.1 DEGREES
REMARK 500 LEU F 69 CA - CB - CG ANGL. DEV. = 21.7 DEGREES
REMARK 500 LYS F 70 N - CA - C ANGL. DEV. = -28.9 DEGREES
REMARK 500 PRO G 63 C - N - CA ANGL. DEV. = -9.7 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 4 142.29 59.15
REMARK 500 GLN A 5 123.08 87.82
REMARK 500 SER A 8 2.54 -64.50
REMARK 500 SER A 31 139.15 -36.30
REMARK 500 ILE A 35 78.99 84.05
REMARK 500 THR A 40 -71.78 -82.73
REMARK 500 MET A 41 -107.33 -145.54
REMARK 500 ASP A 42 96.02 38.41
REMARK 500 GLU A 43 49.10 -73.22
REMARK 500 THR A 44 58.82 87.76
REMARK 500 GLN A 45 -29.35 79.59
REMARK 500 THR A 46 95.10 -63.95
REMARK 500 ALA A 48 -126.97 173.69
REMARK 500 LYS A 49 108.08 -162.36
REMARK 500 ASN A 54 109.54 5.71
REMARK 500 ASP A 55 55.51 79.69
REMARK 500 ARG A 57 -31.28 161.71
REMARK 500 LEU A 58 173.21 -49.60
REMARK 500 ILE A 61 -137.87 -127.76
REMARK 500 ASP A 62 24.11 21.27
REMARK 500 LEU A 65 -59.92 -29.49
REMARK 500 LYS A 66 130.38 -25.21
REMARK 500 CYS A 67 51.70 -175.14
REMARK 500 THR A 69 -10.53 49.88
REMARK 500 CYS A 70 -6.91 -51.56
REMARK 500 GLN A 71 -133.32 35.88
REMARK 500 GLU A 72 -35.73 71.34
REMARK 500 MET A 74 -94.69 37.95
REMARK 500 GLU A 76 -32.54 121.76
REMARK 500 ILE A 84 96.96 -160.63
REMARK 500 ASP A 85 104.01 -54.96
REMARK 500 VAL A 93 -44.26 -10.34
REMARK 500 HIS A 109 -56.77 75.09
REMARK 500 LEU A 113 167.79 -47.53
REMARK 500 LEU A 115 105.91 -165.80
REMARK 500 ILE A 128 81.65 -67.05
REMARK 500 ASP A 130 89.23 171.70
REMARK 500 CYS A 148 74.56 -68.22
REMARK 500 SER A 154 -162.05 -57.56
REMARK 500 ASP A 156 -128.88 -123.24
REMARK 500 ARG A 164 -117.42 -152.94
REMARK 500 CYS A 167 82.88 109.07
REMARK 500 ASN A 169 117.57 -29.00
REMARK 500 GLU A 196 143.93 67.15
REMARK 500 ILE A 214 132.13 -38.68
REMARK 500 PHE A 219 -73.70 -41.54
REMARK 500 THR A 220 -70.94 -36.65
REMARK 500 PHE A 224 -168.28 -125.31
REMARK 500 THR A 237 -61.04 -92.91
REMARK 500 PRO A 245 -12.95 -43.16
REMARK 500
REMARK 500 THIS ENTRY HAS 702 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 A1508 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 67 SG
REMARK 620 2 CYS A 70 SG 127.0
REMARK 620 3 CYS A 77 SG 71.1 112.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 110 SG
REMARK 620 2 CYS A 148 SG 114.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1307 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1163 SG
REMARK 620 2 CYS B1166 SG 101.2
REMARK 620 3 CYS B1182 SG 105.7 141.4
REMARK 620 4 CYS B1185 SG 86.0 73.7 134.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 86 SG
REMARK 620 2 CYS C 88 SG 99.1
REMARK 620 3 CYS C 92 SG 86.2 90.1
REMARK 620 4 CYS C 95 SG 126.6 118.7 126.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 7 SG
REMARK 620 2 CYS I 10 SG 134.9
REMARK 620 3 CYS I 29 SG 102.4 104.4
REMARK 620 4 CYS I 32 SG 118.8 100.9 80.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 75 SG
REMARK 620 2 CYS I 106 SG 152.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 7 SG
REMARK 620 2 CYS J 10 SG 99.7
REMARK 620 3 CYS J 45 SG 119.8 131.2
REMARK 620 4 CYS J 46 SG 111.5 97.1 94.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 105 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 31 SG
REMARK 620 2 CYS L 34 SG 79.7
REMARK 620 3 CYS L 48 SG 109.2 99.3
REMARK 620 4 CYS L 51 SG 98.3 82.6 152.3
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R92 RELATED DB: PDB
DBREF 2R93 R 1 18 PDB 2R93 2R93 1 18
DBREF 2R93 A 1 1733 UNP P04050 RPB1_YEAST 1 1733
DBREF 2R93 B 1 1224 UNP P08518 RPB2_YEAST 1 1224
DBREF 2R93 C 1 318 UNP P16370 RPB3_YEAST 1 318
DBREF 2R93 D 1 221 UNP P20433 RPB4_YEAST 1 221
DBREF 2R93 E 1 215 UNP P20434 RPAB1_YEAST 1 215
DBREF 2R93 F 1 155 UNP P20435 RPAB2_YEAST 1 155
DBREF 2R93 G 1 171 UNP P34087 RPB7_YEAST 1 171
DBREF 2R93 H 1 146 UNP P20436 RPAB3_YEAST 1 146
DBREF 2R93 I 1 122 UNP P27999 RPB9_YEAST 1 122
DBREF 2R93 J 1 70 UNP P22139 RPAB5_YEAST 1 70
DBREF 2R93 K 1 120 UNP P38902 RPB11_YEAST 1 120
DBREF 2R93 L 1 70 UNP P40422 RPAB4_YEAST 1 70
SEQRES 1 R 18 U G A U U C U C U A U C G
SEQRES 2 R 18 G A A U C
SEQRES 1 A 1733 MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR
SEQRES 2 A 1733 VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU
SEQRES 3 A 1733 VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU
SEQRES 4 A 1733 THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY
SEQRES 5 A 1733 LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU
SEQRES 6 A 1733 LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO
SEQRES 7 A 1733 GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE
SEQRES 8 A 1733 HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU
SEQRES 9 A 1733 CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES 10 A 1733 HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP
SEQRES 11 A 1733 SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS
SEQRES 12 A 1733 THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP
SEQRES 13 A 1733 ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN
SEQRES 14 A 1733 THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL
SEQRES 15 A 1733 GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP
SEQRES 16 A 1733 GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU
SEQRES 17 A 1733 ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER
SEQRES 18 A 1733 LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET
SEQRES 19 A 1733 ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG
SEQRES 20 A 1733 PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP
SEQRES 21 A 1733 ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN
SEQRES 22 A 1733 ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS
SEQRES 23 A 1733 HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS
SEQRES 24 A 1733 VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO
SEQRES 25 A 1733 GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE
SEQRES 26 A 1733 ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY
SEQRES 27 A 1733 ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR
SEQRES 28 A 1733 VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL
SEQRES 29 A 1733 GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO
SEQRES 30 A 1733 GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN
SEQRES 31 A 1733 LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS
SEQRES 32 A 1733 TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG
SEQRES 33 A 1733 TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY
SEQRES 34 A 1733 TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL
SEQRES 35 A 1733 LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET
SEQRES 36 A 1733 MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE
SEQRES 37 A 1733 ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP
SEQRES 38 A 1733 PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER
SEQRES 39 A 1733 GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL
SEQRES 40 A 1733 PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS
SEQRES 41 A 1733 MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS
SEQRES 42 A 1733 LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL
SEQRES 43 A 1733 LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL
SEQRES 44 A 1733 ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP
SEQRES 45 A 1733 SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY
SEQRES 46 A 1733 ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU
SEQRES 47 A 1733 SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN
SEQRES 48 A 1733 ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER
SEQRES 49 A 1733 SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS
SEQRES 50 A 1733 GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN
SEQRES 51 A 1733 LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER
SEQRES 52 A 1733 THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET
SEQRES 53 A 1733 ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS
SEQRES 54 A 1733 VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU
SEQRES 55 A 1733 THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU
SEQRES 56 A 1733 ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS
SEQRES 57 A 1733 ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN
SEQRES 58 A 1733 ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER
SEQRES 59 A 1733 PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN
SEQRES 60 A 1733 GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL
SEQRES 61 A 1733 ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER
SEQRES 62 A 1733 PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG
SEQRES 63 A 1733 GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY
SEQRES 64 A 1733 GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA
SEQRES 65 A 1733 GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU
SEQRES 66 A 1733 GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN
SEQRES 67 A 1733 SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP
SEQRES 68 A 1733 GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP
SEQRES 69 A 1733 THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR
SEQRES 70 A 1733 ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO
SEQRES 71 A 1733 SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU
SEQRES 72 A 1733 LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU
SEQRES 73 A 1733 VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP
SEQRES 74 A 1733 GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG
SEQRES 75 A 1733 ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS
SEQRES 76 A 1733 THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU
SEQRES 77 A 1733 GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG
SEQRES 78 A 1733 GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA
SEQRES 79 A 1733 VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA
SEQRES 80 A 1733 THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN
SEQRES 81 A 1733 ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE
SEQRES 82 A 1733 LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL
SEQRES 83 A 1733 LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET
SEQRES 84 A 1733 THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS
SEQRES 85 A 1733 LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU
SEQRES 86 A 1733 ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL
SEQRES 87 A 1733 TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA
SEQRES 88 A 1733 LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS
SEQRES 89 A 1733 SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP
SEQRES 90 A 1733 PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE
SEQRES 91 A 1733 GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN
SEQRES 92 A 1733 SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU
SEQRES 93 A 1733 LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET
SEQRES 94 A 1733 GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN
SEQRES 95 A 1733 ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS
SEQRES 96 A 1733 LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU
SEQRES 97 A 1733 ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS
SEQRES 98 A 1733 LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG
SEQRES 99 A 1733 GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR
SEQRES 100 A 1733 ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS
SEQRES 101 A 1733 GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU
SEQRES 102 A 1733 SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG
SEQRES 103 A 1733 ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU
SEQRES 104 A 1733 GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL
SEQRES 105 A 1733 TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR
SEQRES 106 A 1733 ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN
SEQRES 107 A 1733 GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG
SEQRES 108 A 1733 SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU
SEQRES 109 A 1733 THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU
SEQRES 110 A 1733 LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU
SEQRES 111 A 1733 GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL
SEQRES 112 A 1733 MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU
SEQRES 113 A 1733 GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY
SEQRES 114 A 1733 VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA
SEQRES 115 A 1733 ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU
SEQRES 116 A 1733 VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE
SEQRES 117 A 1733 THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER
SEQRES 118 A 1733 PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY
SEQRES 119 A 1733 PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO
SEQRES 120 A 1733 THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 121 A 1733 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 122 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 123 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 124 A 1733 PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 125 A 1733 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 126 A 1733 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 127 A 1733 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 128 A 1733 PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR
SEQRES 129 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 130 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 131 A 1733 PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR
SEQRES 132 A 1733 SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA
SEQRES 133 A 1733 TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN
SEQRES 134 A 1733 GLU ASN SER ARG
SEQRES 1 B 1224 MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU
SEQRES 2 B 1224 ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR
SEQRES 3 B 1224 ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG
SEQRES 4 B 1224 GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN
SEQRES 5 B 1224 GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU
SEQRES 6 B 1224 ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR
SEQRES 7 B 1224 THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER
SEQRES 8 B 1224 PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU
SEQRES 9 B 1224 SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA
SEQRES 10 B 1224 ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL
SEQRES 11 B 1224 ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO
SEQRES 12 B 1224 GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER
SEQRES 13 B 1224 GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG
SEQRES 14 B 1224 LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER
SEQRES 15 B 1224 GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS
SEQRES 16 B 1224 PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER
SEQRES 17 B 1224 GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN
SEQRES 18 B 1224 ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE
SEQRES 19 B 1224 SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY
SEQRES 20 B 1224 SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY
SEQRES 21 B 1224 ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU
SEQRES 22 B 1224 PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE
SEQRES 23 B 1224 ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU
SEQRES 24 B 1224 HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU
SEQRES 25 B 1224 MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN
SEQRES 26 B 1224 ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY
SEQRES 27 B 1224 THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR
SEQRES 28 B 1224 ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE
SEQRES 29 B 1224 THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE
SEQRES 30 B 1224 LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU
SEQRES 31 B 1224 ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS
SEQRES 32 B 1224 LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU
SEQRES 33 B 1224 PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE
SEQRES 34 B 1224 ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE
SEQRES 35 B 1224 ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER
SEQRES 36 B 1224 GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU
SEQRES 37 B 1224 GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN
SEQRES 38 B 1224 VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS
SEQRES 39 B 1224 LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS
SEQRES 40 B 1224 LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY
SEQRES 41 B 1224 LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS
SEQRES 42 B 1224 GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER
SEQRES 43 B 1224 VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER
SEQRES 44 B 1224 GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS
SEQRES 45 B 1224 GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL
SEQRES 46 B 1224 TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU
SEQRES 47 B 1224 THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO
SEQRES 48 B 1224 GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU
SEQRES 49 B 1224 LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU
SEQRES 50 B 1224 PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU
SEQRES 51 B 1224 LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA
SEQRES 52 B 1224 THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL
SEQRES 53 B 1224 GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU
SEQRES 54 B 1224 VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU
SEQRES 55 B 1224 ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA
SEQRES 56 B 1224 ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG
SEQRES 57 B 1224 ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS
SEQRES 58 B 1224 GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES 59 B 1224 ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES 60 B 1224 THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES 61 B 1224 PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES 62 B 1224 ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR
SEQRES 63 B 1224 ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES 64 B 1224 GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES 65 B 1224 TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES 66 B 1224 ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES 67 B 1224 TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR
SEQRES 68 B 1224 GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG
SEQRES 69 B 1224 MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY
SEQRES 70 B 1224 LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL
SEQRES 71 B 1224 ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU
SEQRES 72 B 1224 GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP
SEQRES 73 B 1224 ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES 74 B 1224 ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS
SEQRES 75 B 1224 PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN
SEQRES 76 B 1224 ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES 77 B 1224 THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE
SEQRES 78 B 1224 THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES 79 B 1224 HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES 80 B 1224 GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN
SEQRES 81 B 1224 GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU
SEQRES 82 B 1224 GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER
SEQRES 83 B 1224 ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES 84 B 1224 LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR
SEQRES 85 B 1224 GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES 86 B 1224 ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO
SEQRES 87 B 1224 VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES 88 B 1224 GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES 89 B 1224 SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES 90 B 1224 PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR
SEQRES 91 B 1224 VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS
SEQRES 92 B 1224 GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE
SEQRES 93 B 1224 PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES 94 B 1224 MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG
SEQRES 95 B 1224 ASP PHE
SEQRES 1 C 318 MET SER GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA
SEQRES 2 C 318 SER LYS ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP
SEQRES 3 C 318 LEU ALA MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA
SEQRES 4 C 318 GLU ILE PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU
SEQRES 5 C 318 THR ASN THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS
SEQRES 6 C 318 ARG LEU GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU
SEQRES 7 C 318 GLN LEU GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS
SEQRES 8 C 318 CYS ASP LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE
SEQRES 9 C 318 GLY GLU SER GLU SER THR THR ASN VAL TYR SER LYS ASP
SEQRES 10 C 318 LEU VAL ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY
SEQRES 11 C 318 HIS PRO ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU
SEQRES 12 C 318 ILE CYS LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR
SEQRES 13 C 318 CYS VAL ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS
SEQRES 14 C 318 TRP GLY PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO
SEQRES 15 C 318 TRP ASN LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN
SEQRES 16 C 318 ASP SER ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU
SEQRES 17 C 318 TYR GLU ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR
SEQRES 18 C 318 LYS ALA GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER
SEQRES 19 C 318 VAL GLY SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY
SEQRES 20 C 318 ILE ASP THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU
SEQRES 21 C 318 ALA LEU THR GLN MET ASP GLN ASP LYS VAL ASN PHE ALA
SEQRES 22 C 318 SER GLY ASP ASN ASN THR ALA SER ASN MET LEU GLY SER
SEQRES 23 C 318 ASN GLU ASP VAL MET MET THR GLY ALA GLU GLN ASP PRO
SEQRES 24 C 318 TYR SER ASN ALA SER GLN MET GLY ASN THR GLY SER GLY
SEQRES 25 C 318 GLY TYR ASP ASN ALA TRP
SEQRES 1 D 221 MET ASN VAL SER THR SER THR PHE GLN THR ARG ARG ARG
SEQRES 2 D 221 ARG LEU LYS LYS VAL GLU GLU GLU GLU ASN ALA ALA THR
SEQRES 3 D 221 LEU GLN LEU GLY GLN GLU PHE GLN LEU LYS GLN ILE ASN
SEQRES 4 D 221 HIS GLN GLY GLU GLU GLU GLU LEU ILE ALA LEU ASN LEU
SEQRES 5 D 221 SER GLU ALA ARG LEU VAL ILE LYS GLU ALA LEU VAL GLU
SEQRES 6 D 221 ARG ARG ARG ALA PHE LYS ARG SER GLN LYS LYS HIS LYS
SEQRES 7 D 221 LYS LYS HIS LEU LYS HIS GLU ASN ALA ASN ASP GLU THR
SEQRES 8 D 221 THR ALA VAL GLU ASP GLU ASP ASP ASP LEU ASP GLU ASP
SEQRES 9 D 221 ASP VAL ASN ALA ASP ASP ASP ASP PHE MET HIS SER GLU
SEQRES 10 D 221 THR ARG GLU LYS GLU LEU GLU SER ILE ASP VAL LEU LEU
SEQRES 11 D 221 GLU GLN THR THR GLY GLY ASN ASN LYS ASP LEU LYS ASN
SEQRES 12 D 221 THR MET GLN TYR LEU THR ASN PHE SER ARG PHE ARG ASP
SEQRES 13 D 221 GLN GLU THR VAL GLY ALA VAL ILE GLN LEU LEU LYS SER
SEQRES 14 D 221 THR GLY LEU HIS PRO PHE GLU VAL ALA GLN LEU GLY SER
SEQRES 15 D 221 LEU ALA CYS ASP THR ALA ASP GLU ALA LYS THR LEU ILE
SEQRES 16 D 221 PRO SER LEU ASN ASN LYS ILE SER ASP ASP GLU LEU GLU
SEQRES 17 D 221 ARG ILE LEU LYS GLU LEU SER ASN LEU GLU THR LEU TYR
SEQRES 1 E 215 MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP
SEQRES 2 E 215 ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG
SEQRES 3 E 215 GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU
SEQRES 4 E 215 GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG
SEQRES 5 E 215 PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR
SEQRES 6 E 215 GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU
SEQRES 7 E 215 TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS
SEQRES 8 E 215 THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN
SEQRES 9 E 215 PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR
SEQRES 10 E 215 PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA
SEQRES 11 E 215 THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN
SEQRES 12 E 215 ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU
SEQRES 13 E 215 SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG
SEQRES 14 E 215 LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP
SEQRES 15 E 215 PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL
SEQRES 16 E 215 VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR
SEQRES 17 E 215 ALA SER TYR ARG ILE CYS MET
SEQRES 1 F 155 MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU
SEQRES 2 F 155 ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU
SEQRES 3 F 155 GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU
SEQRES 4 F 155 THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY
SEQRES 5 F 155 ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG
SEQRES 6 F 155 ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN
SEQRES 7 F 155 ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA
SEQRES 8 F 155 ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN
SEQRES 9 F 155 ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO
SEQRES 10 F 155 LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE
SEQRES 11 F 155 PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE
SEQRES 12 F 155 GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES 1 G 171 MET PHE PHE ILE LYS ASP LEU SER LEU ASN ILE THR LEU
SEQRES 2 G 171 HIS PRO SER PHE PHE GLY PRO ARG MET LYS GLN TYR LEU
SEQRES 3 G 171 LYS THR LYS LEU LEU GLU GLU VAL GLU GLY SER CYS THR
SEQRES 4 G 171 GLY LYS PHE GLY TYR ILE LEU CYS VAL LEU ASP TYR ASP
SEQRES 5 G 171 ASN ILE ASP ILE GLN ARG GLY ARG ILE LEU PRO THR ASP
SEQRES 6 G 171 GLY SER ALA GLU PHE ASN VAL LYS TYR ARG ALA VAL VAL
SEQRES 7 G 171 PHE LYS PRO PHE LYS GLY GLU VAL VAL ASP GLY THR VAL
SEQRES 8 G 171 VAL SER CYS SER GLN HIS GLY PHE GLU VAL GLN VAL GLY
SEQRES 9 G 171 PRO MET LYS VAL PHE VAL THR LYS HIS LEU MET PRO GLN
SEQRES 10 G 171 ASP LEU THR PHE ASN ALA GLY SER ASN PRO PRO SER TYR
SEQRES 11 G 171 GLN SER SER GLU ASP VAL ILE THR ILE LYS SER ARG ILE
SEQRES 12 G 171 ARG VAL LYS ILE GLU GLY CYS ILE SER GLN VAL SER SER
SEQRES 13 G 171 ILE HIS ALA ILE GLY SER ILE LYS GLU ASP TYR LEU GLY
SEQRES 14 G 171 ALA ILE
SEQRES 1 H 146 MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER
SEQRES 2 H 146 GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE
SEQRES 3 H 146 GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR
SEQRES 4 H 146 LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN
SEQRES 5 H 146 ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU
SEQRES 6 H 146 GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER
SEQRES 7 H 146 TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP
SEQRES 8 H 146 ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE
SEQRES 9 H 146 GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER
SEQRES 10 H 146 PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG
SEQRES 11 H 146 ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU
SEQRES 12 H 146 ILE ARG ARG
SEQRES 1 I 122 MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET
SEQRES 2 I 122 LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU
SEQRES 3 I 122 PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY
SEQRES 4 I 122 SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES 5 I 122 GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP
SEQRES 6 I 122 PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS
SEQRES 7 I 122 HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG
SEQRES 8 I 122 ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU
SEQRES 9 I 122 SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS
SEQRES 10 I 122 ARG THR GLN PHE SER
SEQRES 1 J 70 MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 70 VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES 3 J 70 GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES 4 J 70 GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES 5 J 70 HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES 6 J 70 LEU GLU LYS ARG ASP
SEQRES 1 K 120 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES 2 K 120 GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES 3 K 120 ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES 4 K 120 HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES 5 K 120 ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES 6 K 120 PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES 7 K 120 GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES 8 K 120 ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES 9 K 120 PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP
SEQRES 10 K 120 ASP ALA PHE
SEQRES 1 L 70 MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP
SEQRES 2 L 70 ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR
SEQRES 3 L 70 LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER
SEQRES 4 L 70 LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY
SEQRES 5 L 70 HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL
SEQRES 6 L 70 GLN PHE GLU ALA ARG
HET ZN A1506 1
HET ZN A1508 1
HET MG A 1 1
HET ZN B1307 1
HET ZN C 302 1
HET ZN I 203 1
HET ZN I 204 1
HET ZN J 101 1
HET ZN L 105 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 14 ZN 8(ZN 2+)
FORMUL 16 MG MG 2+
HELIX 1 1 GLU A 25 SER A 31 1 7
HELIX 2 2 PHE A 95 GLU A 104 1 10
HELIX 3 3 ASN A 119 LEU A 126 1 8
HELIX 4 4 ASP A 130 LYS A 143 1 14
HELIX 5 5 SER A 203 ILE A 214 1 12
HELIX 6 6 SER A 215 LEU A 222 1 8
HELIX 7 7 ARG A 230 MET A 234 5 5
HELIX 8 8 PRO A 243 ARG A 247 5 5
HELIX 9 9 ASP A 261 HIS A 281 1 21
HELIX 10 10 ILE A 289 TYR A 303 1 15
HELIX 11 11 SER A 324 LYS A 330 1 7
HELIX 12 12 GLY A 334 LEU A 340 1 7
HELIX 13 13 LYS A 368 LYS A 372 1 5
HELIX 14 14 ASN A 384 ASN A 394 1 11
HELIX 15 15 VAL A 474 ASN A 479 1 6
HELIX 16 16 SER A 494 CYS A 505 1 12
HELIX 17 17 VAL A 524 LEU A 534 1 11
HELIX 18 18 LEU A 543 VAL A 553 1 11
HELIX 19 19 GLY A 574 ILE A 582 1 9
HELIX 20 20 GLU A 618 GLY A 623 1 6
HELIX 21 21 GLY A 628 GLY A 638 1 11
HELIX 22 22 GLY A 638 GLY A 661 1 24
HELIX 23 23 GLY A 665 ILE A 670 5 6
HELIX 24 24 ASP A 672 GLU A 696 1 25
HELIX 25 25 ARG A 711 VAL A 735 1 25
HELIX 26 26 ASN A 741 GLY A 750 1 10
HELIX 27 27 SER A 754 ALA A 763 1 10
HELIX 28 28 THR A 809 LYS A 830 1 22
HELIX 29 29 THR A 831 GLU A 846 1 16
HELIX 30 30 SER A 889 ARG A 898 1 10
HELIX 31 31 GLY A 916 LEU A 920 5 5
HELIX 32 32 LYS A 924 PHE A 947 1 24
HELIX 33 33 ASN A 959 GLN A 969 1 11
HELIX 34 34 THR A 982 GLN A 994 1 13
HELIX 35 35 ASN A 1004 LEU A 1026 1 23
HELIX 36 36 ALA A 1027 GLU A 1034 1 8
HELIX 37 37 THR A 1038 SER A 1056 1 19
HELIX 38 38 MET A 1063 GLU A 1074 1 12
HELIX 39 39 GLY A 1097 VAL A 1107 1 11
HELIX 40 40 ASP A 1127 SER A 1136 1 10
HELIX 41 41 LEU A 1143 VAL A 1146 1 4
HELIX 42 42 GLU A 1167 LEU A 1172 1 6
HELIX 43 43 ALA A 1200 LYS A 1205 1 6
HELIX 44 44 THR A 1208 LYS A 1221 1 14
HELIX 45 45 LYS A 1261 GLU A 1269 1 9
HELIX 46 46 ASN A 1312 MET A 1317 1 6
HELIX 47 47 SER A 1331 LEU A 1339 1 9
HELIX 48 48 GLY A 1340 SER A 1358 1 19
HELIX 49 49 TYR A 1365 THR A 1377 1 13
HELIX 50 50 GLY A 1388 SER A 1392 5 5
HELIX 51 51 GLY A 1395 CYS A 1400 1 6
HELIX 52 52 GLU A 1404 ALA A 1414 1 11
HELIX 53 53 GLY A 1423 GLY A 1431 1 9
HELIX 54 54 ILE A 1436 ALA A 1440 5 5
HELIX 55 55 GLU A 1448 TYR A 1453 1 6
HELIX 56 56 ASP B 29 GLY B 42 1 14
HELIX 57 57 VAL B 44 TYR B 57 1 14
HELIX 58 58 TYR B 57 CYS B 64 1 8
HELIX 59 59 TYR B 113 ARG B 120 1 8
HELIX 60 60 CYS B 179 GLU B 183 5 5
HELIX 61 61 THR B 185 LYS B 191 1 7
HELIX 62 62 ILE B 282 ALA B 288 1 7
HELIX 63 63 GLY B 295 CYS B 302 1 8
HELIX 64 64 ASP B 307 GLY B 321 1 15
HELIX 65 65 PHE B 322 ILE B 324 5 3
HELIX 66 66 ASP B 326 THR B 339 1 14
HELIX 67 67 LYS B 345 LYS B 358 1 14
HELIX 68 68 PHE B 370 LEU B 390 1 21
HELIX 69 69 HIS B 400 GLY B 402 5 3
HELIX 70 70 LEU B 408 VAL B 436 1 29
HELIX 71 71 ALA B 450 GLY B 464 1 15
HELIX 72 72 THR B 487 ARG B 496 1 10
HELIX 73 73 HIS B 515 TRP B 519 5 5
HELIX 74 74 PRO B 551 GLU B 560 1 10
HELIX 75 75 PRO B 565 TYR B 569 5 5
HELIX 76 76 PRO B 593 ARG B 605 1 13
HELIX 77 77 ARG B 654 LYS B 660 1 7
HELIX 78 78 LEU B 661 GLN B 667 1 7
HELIX 79 79 THR B 680 ASN B 686 1 7
HELIX 80 80 GLU B 696 ILE B 701 5 6
HELIX 81 81 HIS B 744 LEU B 749 5 6
HELIX 82 82 ALA B 752 ILE B 756 5 5
HELIX 83 83 GLN B 763 GLY B 774 1 12
HELIX 84 84 LYS B 775 ALA B 777 5 3
HELIX 85 85 THR B 783 ARG B 788 5 6
HELIX 86 86 THR B 806 LEU B 812 5 7
HELIX 87 87 GLN B 843 ARG B 848 1 6
HELIX 88 88 ASN B 1013 ILE B 1017 5 5
HELIX 89 89 THR B 1022 ALA B 1036 1 15
HELIX 90 90 THR B 1051 GLU B 1061 1 11
HELIX 91 91 MET B 1098 LYS B 1102 5 5
HELIX 92 92 GLY B 1121 ASP B 1125 5 5
HELIX 93 93 GLY B 1131 GLY B 1142 1 12
HELIX 94 94 ALA B 1143 MET B 1152 1 10
HELIX 95 95 PRO B 1197 ALA B 1209 1 13
HELIX 96 96 ASP C 26 GLU C 40 1 15
HELIX 97 97 ALA C 59 ILE C 70 1 12
HELIX 98 98 ASP C 76 LEU C 80 5 5
HELIX 99 99 TYR C 82 CYS C 86 5 5
HELIX 100 100 LYS C 116 LEU C 118 5 3
HELIX 101 101 HIS C 167 GLY C 171 5 5
HELIX 102 102 ASP C 196 TRP C 201 1 6
HELIX 103 103 ASP C 241 MET C 265 1 25
HELIX 104 104 GLY D 30 GLN D 34 5 5
HELIX 105 105 SER D 53 PHE D 70 1 18
HELIX 106 106 THR D 118 GLU D 120 5 3
HELIX 107 107 LYS D 121 GLU D 131 1 11
HELIX 108 108 ASN D 138 PHE D 151 1 14
HELIX 109 109 GLU D 158 LYS D 168 1 11
HELIX 110 110 HIS D 173 LEU D 183 1 11
HELIX 111 111 THR D 187 ILE D 195 1 9
HELIX 112 112 SER D 203 GLU D 218 1 16
HELIX 113 113 ASP E 2 ARG E 26 1 25
HELIX 114 114 PRO E 38 ALA E 44 1 7
HELIX 115 115 GLN E 54 MET E 58 5 5
HELIX 116 116 GLU E 67 PHE E 72 1 6
HELIX 117 117 VAL E 90 ASN E 104 1 15
HELIX 118 118 ASN E 143 HIS E 147 5 5
HELIX 119 119 ASP E 159 TYR E 168 1 10
HELIX 120 120 LYS E 171 LEU E 175 5 5
HELIX 121 121 ASP E 182 GLY E 189 1 8
HELIX 122 122 THR F 86 MET F 103 1 18
HELIX 123 123 ASP F 116 LEU F 125 1 10
HELIX 124 124 HIS G 14 PHE G 18 5 5
HELIX 125 125 ARG G 21 VAL G 34 1 14
HELIX 126 126 ASP G 50 ILE G 54 5 5
HELIX 127 127 ASP J 16 LEU J 22 1 7
HELIX 128 128 LEU J 22 GLU J 27 1 6
HELIX 129 129 ASP J 31 GLY J 40 1 10
HELIX 130 130 ARG J 43 HIS J 53 1 11
HELIX 131 131 LEU J 56 ARG J 62 1 7
HELIX 132 132 ASP K 5 LEU K 9 5 5
HELIX 133 133 ASP K 39 GLU K 49 1 11
HELIX 134 134 LEU K 50 ASN K 52 5 3
HELIX 135 135 ASP K 82 ASN K 110 1 29
SHEET 1 A 3 LEU A1418 ASP A1419 0
SHEET 2 A 3 VAL A 17 LEU A 21 -1 N VAL A 17 O ASP A1419
SHEET 3 A 3 ILE B1212 PRO B1214 -1 O THR B1213 N GLY A 20
SHEET 1 B 2 ASP A 85 VAL A 90 0
SHEET 2 B 2 LEU A 236 CYS A 238 -1 O LEU A 236 N VAL A 90
SHEET 1 C 2 ASP A 151 PRO A 153 0
SHEET 2 C 2 LEU A 161 SER A 163 -1 O VAL A 162 N VAL A 152
SHEET 1 D 3 THR A 173 ASP A 177 0
SHEET 2 D 3 LYS A 180 SER A 184 -1 O VAL A 182 N ARG A 175
SHEET 3 D 3 LEU A 199 VAL A 201 -1 O ARG A 200 N GLY A 183
SHEET 1 E 8 HIS B1104 ARG B1106 0
SHEET 2 E 8 SER A 348 GLY A 355 -1 N SER A 348 O ARG B1106
SHEET 3 E 8 GLU A 486 HIS A 490 -1 O LEU A 489 N ALA A 349
SHEET 4 E 8 VAL A 442 ASN A 445 -1 N LEU A 443 O HIS A 490
SHEET 5 E 8 MET A 455 ILE A 463 -1 O MET A 456 N PHE A 444
SHEET 6 E 8 GLN A 363 PRO A 367 1 N VAL A 366 O LYS A 461
SHEET 7 E 8 THR A 467 LEU A 470 -1 O ARG A 469 N GLY A 365
SHEET 8 E 8 SER A 348 GLY A 355 1 N VAL A 352 O PHE A 468
SHEET 1 F 4 THR A 375 VAL A 379 0
SHEET 2 F 4 LYS A 431 HIS A 435 -1 O VAL A 432 N GLU A 378
SHEET 3 F 4 ALA A 402 ARG A 407 -1 N ILE A 406 O LYS A 431
SHEET 4 F 4 ASP A 411 ASP A 414 -1 O ILE A 413 N VAL A 405
SHEET 1 G 2 VAL A 512 SER A 513 0
SHEET 2 G 2 LYS A 518 PRO A 519 -1 O LYS A 518 N SER A 513
SHEET 1 H 2 PHE A 540 GLU A 542 0
SHEET 2 H 2 LEU A 571 SER A 573 -1 O TRP A 572 N ILE A 541
SHEET 1 I 3 LEU A 588 GLN A 589 0
SHEET 2 I 3 LEU A 606 ILE A 608 -1 O ILE A 607 N LEU A 588
SHEET 3 I 3 GLN A 611 PHE A 614 -1 O GLN A 611 N ILE A 608
SHEET 1 J 2 GLY A 766 GLN A 767 0
SHEET 2 J 2 PHE A 799 VAL A 800 -1 O VAL A 800 N GLY A 766
SHEET 1 K 2 SER A 769 VAL A 770 0
SHEET 2 K 2 LYS A 773 ARG A 774 -1 O LYS A 773 N VAL A 770
SHEET 1 L 3 MET A 849 VAL A 850 0
SHEET 2 L 3 THR A 856 ARG A 857 -1 O ARG A 857 N MET A 849
SHEET 3 L 3 VAL A 863 GLN A 865 -1 O ILE A 864 N THR A 856
SHEET 1 M 2 GLU A 879 SER A 882 0
SHEET 2 M 2 ASN A 953 LEU A 956 -1 O TRP A 954 N GLN A 881
SHEET 1 N 3 THR A1117 TYR A1119 0
SHEET 2 N 3 GLU A1303 GLU A1307 -1 O LEU A1306 N VAL A1118
SHEET 3 N 3 VAL A1283 TYR A1287 -1 N TYR A1287 O GLU A1303
SHEET 1 O 2 THR A1141 THR A1142 0
SHEET 2 O 2 THR A1272 ARG A1274 -1 O LEU A1273 N THR A1141
SHEET 1 P 4 ILE A1237 ILE A1238 0
SHEET 2 P 4 TRP A1191 LEU A1197 -1 N LEU A1195 O ILE A1238
SHEET 3 P 4 THR A1147 TYR A1154 -1 N GLU A1151 O ARG A1194
SHEET 4 P 4 LEU I 42 ARG I 45 -1 O VAL I 43 N ILE A1152
SHEET 1 Q 2 LEU A1224 VAL A1226 0
SHEET 2 Q 2 CYS A1240 VAL A1242 -1 O ARG A1241 N PHE A1225
SHEET 1 R 2 LYS A1290 PRO A1292 0
SHEET 2 R 2 TYR A1298 LYS A1300 -1 O VAL A1299 N VAL A1291
SHEET 1 S 7 SER D 6 THR D 7 0
SHEET 2 S 7 LEU G 7 LEU G 13 -1 O SER G 8 N SER D 6
SHEET 3 S 7 ALA G 68 LYS G 73 -1 O ALA G 68 N LEU G 13
SHEET 4 S 7 GLY G 59 ILE G 61 -1 N ARG G 60 O GLU G 69
SHEET 5 S 7 ASP A1442 ILE A1445 -1 N VAL A1443 O ILE G 61
SHEET 6 S 7 LEU F 132 TYR F 137 -1 O ARG F 135 N ASP A1442
SHEET 7 S 7 PHE F 143 SER F 147 -1 O TRP F 146 N ILE F 134
SHEET 1 T 3 SER B 91 VAL B 97 0
SHEET 2 T 3 GLY B 127 LYS B 133 -1 O PHE B 129 N TYR B 96
SHEET 3 T 3 VAL B 165 ARG B 169 -1 O ILE B 167 N LEU B 128
SHEET 1 U 3 PHE B 203 ILE B 204 0
SHEET 2 U 3 GLU B 209 VAL B 211 -1 O LYS B 210 N PHE B 203
SHEET 3 U 3 GLN B 481 VAL B 482 -1 O GLN B 481 N VAL B 211
SHEET 1 V 4 LYS B 404 ASP B 407 0
SHEET 2 V 4 ALA B 214 SER B 218 -1 N ARG B 217 O ARG B 405
SHEET 3 V 4 ARG B 497 ASN B 499 1 O ASN B 499 N ALA B 214
SHEET 4 V 4 VAL B 536 ASN B 538 -1 O LYS B 537 N THR B 498
SHEET 1 W 5 VAL B 223 LYS B 227 0
SHEET 2 W 5 HIS B 236 SER B 242 -1 O GLU B 239 N GLN B 224
SHEET 3 W 5 SER B 252 VAL B 256 -1 O LEU B 254 N ILE B 240
SHEET 4 W 5 LYS B 270 THR B 272 -1 O THR B 272 N GLN B 255
SHEET 5 W 5 ILE B 280 PRO B 281 -1 O ILE B 280 N ALA B 271
SHEET 1 X 3 CYS B 544 ILE B 545 0
SHEET 2 X 3 VAL B 633 ILE B 639 -1 O TYR B 634 N CYS B 544
SHEET 3 X 3 VAL B 690 ASP B 694 -1 O GLU B 691 N LEU B 637
SHEET 1 Y 4 CYS B 544 ILE B 545 0
SHEET 2 Y 4 VAL B 633 ILE B 639 -1 O TYR B 634 N CYS B 544
SHEET 3 Y 4 HIS B 740 GLU B 742 -1 O CYS B 741 N PHE B 638
SHEET 4 Y 4 ILE B 703 ALA B 704 1 N ALA B 704 O GLU B 742
SHEET 1 Z 5 MET B 563 GLU B 564 0
SHEET 2 Z 5 VAL B 585 HIS B 590 -1 O VAL B 589 N GLU B 564
SHEET 3 Z 5 THR B 578 VAL B 582 -1 N VAL B 580 O GLY B 588
SHEET 4 Z 5 GLU B 623 PHE B 627 1 O LEU B 624 N PHE B 581
SHEET 5 Z 5 SER B 614 ARG B 617 -1 N ILE B 616 O LYS B 625
SHEET 1 AA 4 ALA B 793 LEU B 796 0
SHEET 2 AA 4 SER B 853 ASP B 861 -1 O LEU B 854 N ILE B 795
SHEET 3 AA 4 LEU B 961 LYS B 972 -1 O VAL B 964 N ASP B 861
SHEET 4 AA 4 ILE B 948 ASN B 957 -1 N ILE B 948 O ARG B 969
SHEET 1 AB 2 GLN B 821 ILE B 827 0
SHEET 2 AB 2 PHE B1086 TYR B1092 -1 O THR B1090 N ALA B 823
SHEET 1 AC 3 SER B 838 ASN B 842 0
SHEET 2 AC 3 GLY B 988 TYR B 994 1 O ILE B 992 N MET B 841
SHEET 3 AC 3 LYS B 979 PHE B 980 -1 N PHE B 980 O GLY B 988
SHEET 1 AD 2 THR B 915 THR B 916 0
SHEET 2 AD 2 ARG B 935 ASP B 936 -1 O ARG B 935 N THR B 916
SHEET 1 AE 2 PHE B1001 THR B1002 0
SHEET 2 AE 2 MET B1072 TYR B1073 -1 O TYR B1073 N PHE B1001
SHEET 1 AF 2 PHE B1158 CYS B1163 0
SHEET 2 AF 2 ILE B1191 ILE B1196 -1 O ILE B1194 N VAL B1160
SHEET 1 AG 3 PHE C 20 LEU C 22 0
SHEET 2 AG 3 PHE C 228 VAL C 232 -1 O PHE C 228 N LEU C 22
SHEET 3 AG 3 ILE C 176 GLU C 177 -1 N GLU C 177 O ASN C 231
SHEET 1 AH 5 VAL C 119 ILE C 120 0
SHEET 2 AH 5 VAL C 97 THR C 100 -1 N THR C 100 O VAL C 119
SHEET 3 AH 5 CYS C 157 LYS C 160 -1 O ALA C 159 N VAL C 97
SHEET 4 AH 5 ALA C 45 VAL C 49 -1 N ASP C 47 O VAL C 158
SHEET 5 AH 5 PHE L 67 GLU L 68 -1 O PHE L 67 N VAL C 49
SHEET 1 AI 3 THR C 53 ASN C 54 0
SHEET 2 AI 3 GLU C 152 LYS C 154 -1 O LYS C 154 N THR C 53
SHEET 3 AI 3 GLN C 102 PHE C 104 -1 N ALA C 103 O LEU C 153
SHEET 1 AJ 2 THR C 111 TYR C 114 0
SHEET 2 AJ 2 LEU C 143 LEU C 147 -1 O CYS C 145 N VAL C 113
SHEET 1 AK 2 LYS D 36 ILE D 38 0
SHEET 2 AK 2 GLU D 44 GLU D 46 -1 O GLU D 45 N GLN D 37
SHEET 1 AL 5 ALA D 49 LEU D 50 0
SHEET 2 AL 5 PHE G 2 LYS G 5 -1 O PHE G 2 N LEU D 50
SHEET 3 AL 5 ALA G 76 PHE G 79 -1 O VAL G 78 N PHE G 3
SHEET 4 AL 5 GLY G 43 VAL G 48 -1 N CYS G 47 O VAL G 77
SHEET 5 AL 5 CYS G 38 THR G 39 -1 N THR G 39 O GLY G 43
SHEET 1 AM 4 PHE E 60 ALA E 62 0
SHEET 2 AM 4 LEU E 78 GLU E 81 -1 O LEU E 78 N ALA E 62
SHEET 3 AM 4 THR E 107 TYR E 112 1 O ILE E 109 N TRP E 79
SHEET 4 AM 4 THR E 131 ASN E 136 1 O GLU E 133 N GLY E 108
SHEET 1 AN 3 ARG E 177 ILE E 178 0
SHEET 2 AN 3 ARG E 207 CYS E 214 1 O ILE E 213 N ILE E 178
SHEET 3 AN 3 VAL E 195 LYS E 201 -1 N ILE E 198 O SER E 210
SHEET 1 AO 6 GLU G 85 VAL G 87 0
SHEET 2 AO 6 ILE G 143 GLN G 153 -1 O ILE G 147 N GLU G 85
SHEET 3 AO 6 SER G 156 SER G 162 -1 O HIS G 158 N ILE G 151
SHEET 4 AO 6 LYS G 107 THR G 111 1 N PHE G 109 O ALA G 159
SHEET 5 AO 6 GLY G 98 GLN G 102 -1 N PHE G 99 O VAL G 110
SHEET 6 AO 6 THR G 90 SER G 95 -1 N SER G 95 O GLY G 98
SHEET 1 AP 3 GLU G 85 VAL G 87 0
SHEET 2 AP 3 ILE G 143 GLN G 153 -1 O ILE G 147 N GLU G 85
SHEET 3 AP 3 GLY G 169 ALA G 170 -1 O GLY G 169 N ARG G 144
SHEET 1 AQ 2 TYR G 130 GLN G 131 0
SHEET 2 AQ 2 VAL G 136 ILE G 137 -1 O ILE G 137 N TYR G 130
SHEET 1 AR 7 LEU H 55 THR H 58 0
SHEET 2 AR 7 ASP H 7 ASP H 16 -1 N PHE H 10 O LEU H 55
SHEET 3 AR 7 CYS H 24 SER H 30 -1 O GLU H 27 N SER H 13
SHEET 4 AR 7 LEU H 38 ILE H 42 -1 O ILE H 42 N CYS H 24
SHEET 5 AR 7 LEU H 121 LEU H 125 -1 O ARG H 124 N THR H 39
SHEET 6 AR 7 TYR H 115 PHE H 118 -1 N TYR H 116 O MET H 123
SHEET 7 AR 7 THR H 100 ALA H 101 -1 N THR H 100 O SER H 117
SHEET 1 AS 3 PRO I 16 GLU I 18 0
SHEET 2 AS 3 LEU I 25 GLU I 28 -1 O LEU I 26 N ARG I 17
SHEET 3 AS 3 VAL I 35 GLU I 37 -1 O GLU I 36 N PHE I 27
SHEET 1 AT 3 ARG I 70 SER I 71 0
SHEET 2 AT 3 ASN I 83 PHE I 86 -1 O ASN I 83 N SER I 71
SHEET 3 AT 3 PHE I 100 CYS I 103 -1 O VAL I 102 N VAL I 84
SHEET 1 AU 4 LEU K 19 PRO K 23 0
SHEET 2 AU 4 VAL K 31 GLU K 36 -1 O THR K 34 N LYS K 20
SHEET 3 AU 4 ARG K 70 THR K 77 -1 O LEU K 73 N ILE K 33
SHEET 4 AU 4 VAL K 56 LYS K 62 -1 N ALA K 60 O ARG K 74
LINK MG MG A 1 OD1 ASP A 481 1555 1555 2.49
LINK SG CYS A 67 ZN ZN A1508 1555 1555 2.74
LINK SG CYS A 70 ZN ZN A1508 1555 1555 2.58
LINK SG CYS A 77 ZN ZN A1508 1555 1555 2.70
LINK SG CYS A 110 ZN ZN A1506 1555 1555 2.67
LINK SG CYS A 148 ZN ZN A1506 1555 1555 2.80
LINK SG CYS B1163 ZN ZN B1307 1555 1555 2.49
LINK SG CYS B1166 ZN ZN B1307 1555 1555 2.60
LINK SG CYS B1182 ZN ZN B1307 1555 1555 2.62
LINK SG CYS B1185 ZN ZN B1307 1555 1555 2.63
LINK SG CYS C 86 ZN ZN C 302 1555 1555 2.42
LINK SG CYS C 88 ZN ZN C 302 1555 1555 2.58
LINK SG CYS C 92 ZN ZN C 302 1555 1555 2.74
LINK SG CYS C 95 ZN ZN C 302 1555 1555 2.64
LINK SG CYS I 7 ZN ZN I 203 1555 1555 2.45
LINK SG CYS I 10 ZN ZN I 203 1555 1555 2.55
LINK SG CYS I 29 ZN ZN I 203 1555 1555 2.74
LINK SG CYS I 32 ZN ZN I 203 1555 1555 2.50
LINK SG CYS I 75 ZN ZN I 204 1555 1555 2.65
LINK SG CYS I 106 ZN ZN I 204 1555 1555 2.49
LINK SG CYS J 7 ZN ZN J 101 1555 1555 2.78
LINK SG CYS J 10 ZN ZN J 101 1555 1555 2.40
LINK SG CYS J 45 ZN ZN J 101 1555 1555 2.55
LINK SG CYS J 46 ZN ZN J 101 1555 1555 2.54
LINK SG CYS L 31 ZN ZN L 105 1555 1555 2.96
LINK SG CYS L 34 ZN ZN L 105 1555 1555 2.44
LINK SG CYS L 48 ZN ZN L 105 1555 1555 2.68
LINK SG CYS L 51 ZN ZN L 105 1555 1555 2.60
CISPEP 1 GLN A 447 PRO A 448 0 -0.40
CISPEP 2 PRO E 128 PRO E 129 0 -1.15
CISPEP 3 ASN G 126 PRO G 127 0 0.01
CRYST1 223.336 394.884 284.121 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004478 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003520 0.00000
(ATOM LINES ARE NOT SHOWN.)
END