HEADER LIGASE/DNA-BINDING PROTEIN/DNA 09-SEP-11 4A0L
TITLE STRUCTURE OF DDB1-DDB2-CUL4B-RBX1 BOUND TO A 12 BP ABASIC SITE
TITLE 2 CONTAINING DNA-DUPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: DDB P127 SUBUNIT, DNA DAMAGE-BINDING PROTEIN A, DDBA,
COMPND 5 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1, HBV X-ASSOCIATED PROTEIN 1,
COMPND 6 XAP-1, UV-DAMAGED DNA-BINDING FACTOR, UV-DAMAGED DNA-BINDING PROTEIN
COMPND 7 1, UV-DDB 1, XPE-BINDING FACTOR, XPE-BF, XERODERMA PIGMENTOSUM GROUP
COMPND 8 E-COMPLEMENTING PROTEIN, XPCE;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DNA DAMAGE-BINDING PROTEIN 2;
COMPND 12 CHAIN: B, D;
COMPND 13 FRAGMENT: RESIDUES 60-423;
COMPND 14 SYNONYM: DAMAGE-SPECIFIC DNA-BINDING PROTEIN 2;
COMPND 15 ENGINEERED: YES;
COMPND 16 OTHER_DETAILS: VARIANT WITH GLN AT POSITION 180 AND ARG AT POSITION
COMPND 17 214 SIMILAR TO PDB ENTRY 3EI2;
COMPND 18 MOL_ID: 3;
COMPND 19 MOLECULE: CULLIN-4B;
COMPND 20 CHAIN: E, H;
COMPND 21 FRAGMENT: RESIDUES 193-913;
COMPND 22 SYNONYM: CULLIN HOMOLOG 4B, CUL-4B;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 4;
COMPND 25 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;
COMPND 26 CHAIN: F, I;
COMPND 27 FRAGMENT: RESIDUES 12-108;
COMPND 28 SYNONYM: RING FINGER PROTEIN 75, RING-BOX PROTEIN 1, RBX1;
COMPND 29 ENGINEERED: YES;
COMPND 30 MOL_ID: 5;
COMPND 31 MOLECULE: 12 BP THF CONTAINING DNA DUPLEX;
COMPND 32 CHAIN: R, T;
COMPND 33 ENGINEERED: YES;
COMPND 34 MOL_ID: 6;
COMPND 35 MOLECULE: 12 BP DNA DUPLEX;
COMPND 36 CHAIN: S, U;
COMPND 37 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: DANIO RERIO;
SOURCE 13 ORGANISM_COMMON: ZEBRAFISH;
SOURCE 14 ORGANISM_TAXID: 7955;
SOURCE 15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 26 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 33 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 34 ORGANISM_TAXID: 10090;
SOURCE 35 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 36 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 38 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DERIVED;
SOURCE 41 MOL_ID: 5;
SOURCE 42 SYNTHETIC: YES;
SOURCE 43 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 44 ORGANISM_TAXID: 32630;
SOURCE 45 MOL_ID: 6;
SOURCE 46 SYNTHETIC: YES;
SOURCE 47 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 48 ORGANISM_TAXID: 32630
KEYWDS LIGASE-DNA-BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.S.FISCHER,A.SCRIMA,H.GUT,N.H.THOMA
REVDAT 4 03-APR-19 4A0L 1 REMARK
REVDAT 3 27-MAR-19 4A0L 1 SOURCE LINK
REVDAT 2 07-NOV-12 4A0L 1 DBREF
REVDAT 1 14-DEC-11 4A0L 0
JRNL AUTH E.S.FISCHER,A.SCRIMA,K.BOHM,S.MATSUMOTO,G.M.LINGARAJU,
JRNL AUTH 2 M.FATY,T.YASUDA,S.CAVADINI,M.WAKASUGI,F.HANAOKA,S.IWAI,
JRNL AUTH 3 H.GUT,K.SUGASAWA,N.H.THOMA
JRNL TITL THE MOLECULAR BASIS OF CRL4(DDB2/CSA) UBIQUITIN LIGASE
JRNL TITL 2 ARCHITECTURE, TARGETING, AND ACTIVATION.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 147 1024 2011
JRNL REFN ISSN 0092-8674
JRNL PMID 22118460
JRNL DOI 10.1016/J.CELL.2011.10.035
REMARK 2
REMARK 2 RESOLUTION. 7.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 7.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 13523
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.318
REMARK 3 R VALUE (WORKING SET) : 0.318
REMARK 3 FREE R VALUE : 0.320
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1352
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.8623 - 15.2754 0.99 1255 140 0.3705 0.3597
REMARK 3 2 15.2754 - 12.4073 0.99 1234 137 0.2662 0.3022
REMARK 3 3 12.4073 - 10.9265 0.99 1205 134 0.2557 0.2379
REMARK 3 4 10.9265 - 9.9683 0.99 1219 136 0.2706 0.3009
REMARK 3 5 9.9683 - 9.2768 0.99 1206 134 0.3106 0.2798
REMARK 3 6 9.2768 - 8.7444 0.99 1205 134 0.3482 0.3367
REMARK 3 7 8.7444 - 8.3164 0.99 1241 137 0.3615 0.3354
REMARK 3 8 8.3164 - 7.9615 0.99 1198 132 0.3661 0.4203
REMARK 3 9 7.9615 - 7.6603 0.99 1206 134 0.3938 0.3798
REMARK 3 10 7.6603 - 7.4001 0.99 1202 134 0.3847 0.3925
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 143.7
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 2.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 344.0
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 36315
REMARK 3 ANGLE : 1.233 49309
REMARK 3 CHIRALITY : 0.083 5617
REMARK 3 PLANARITY : 0.006 6162
REMARK 3 DIHEDRAL : 18.545 13521
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0148 -1.7414 27.6910
REMARK 3 T TENSOR
REMARK 3 T11: 1.6432 T22: 2.3331
REMARK 3 T33: 1.6466 T12: 0.0956
REMARK 3 T13: 0.6729 T23: -0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 2.1609 L22: 4.0697
REMARK 3 L33: 3.0624 L12: 2.7587
REMARK 3 L13: 2.2158 L23: 0.8725
REMARK 3 S TENSOR
REMARK 3 S11: 0.4051 S12: 0.1255 S13: -0.3400
REMARK 3 S21: 0.6988 S22: 0.1412 S23: 0.0398
REMARK 3 S31: -0.1921 S32: -0.4892 S33: -0.4197
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B OR CHAIN R OR CHAIN S
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2836 2.0881 78.0278
REMARK 3 T TENSOR
REMARK 3 T11: 4.5984 T22: 3.7371
REMARK 3 T33: 3.1938 T12: -0.8239
REMARK 3 T13: -0.7651 T23: 0.4963
REMARK 3 L TENSOR
REMARK 3 L11: 3.8964 L22: 0.6248
REMARK 3 L33: 4.6669 L12: 1.0343
REMARK 3 L13: -0.4768 L23: 0.0095
REMARK 3 S TENSOR
REMARK 3 S11: -0.8249 S12: -1.3288 S13: -0.7139
REMARK 3 S21: -0.1346 S22: -0.6149 S23: 0.9720
REMARK 3 S31: -0.3922 S32: 0.0608 S33: 1.1021
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7837 58.3090 22.5275
REMARK 3 T TENSOR
REMARK 3 T11: 1.7110 T22: 2.5306
REMARK 3 T33: 1.3205 T12: -0.0695
REMARK 3 T13: 0.8212 T23: 0.0916
REMARK 3 L TENSOR
REMARK 3 L11: 2.1667 L22: 3.6670
REMARK 3 L33: 1.8266 L12: 1.0470
REMARK 3 L13: 1.7369 L23: 0.9735
REMARK 3 S TENSOR
REMARK 3 S11: 0.1094 S12: 0.4382 S13: -0.5733
REMARK 3 S21: 0.1055 S22: 0.0722 S23: 0.5298
REMARK 3 S31: -0.1616 S32: -0.3858 S33: -0.0735
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D OR CHAIN T OR CHAIN U
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3555 62.8684 69.1982
REMARK 3 T TENSOR
REMARK 3 T11: 2.3320 T22: 2.2801
REMARK 3 T33: 1.9873 T12: -0.5710
REMARK 3 T13: 0.0855 T23: 0.4647
REMARK 3 L TENSOR
REMARK 3 L11: 2.0569 L22: 5.7683
REMARK 3 L33: 3.5564 L12: -1.3109
REMARK 3 L13: 1.4749 L23: 2.7493
REMARK 3 S TENSOR
REMARK 3 S11: 1.1303 S12: -1.1532 S13: -0.6923
REMARK 3 S21: 0.7035 S22: 0.3116 S23: 0.5368
REMARK 3 S31: 1.9510 S32: -1.1286 S33: -1.2954
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN E OR CHAIN F
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1137 -53.0881 75.5630
REMARK 3 T TENSOR
REMARK 3 T11: 3.7293 T22: 3.7199
REMARK 3 T33: 2.1247 T12: 0.4348
REMARK 3 T13: 0.2504 T23: -0.4777
REMARK 3 L TENSOR
REMARK 3 L11: 0.0915 L22: 1.4119
REMARK 3 L33: -0.0962 L12: 0.8887
REMARK 3 L13: -0.1422 L23: -0.2719
REMARK 3 S TENSOR
REMARK 3 S11: -0.8920 S12: -1.5618 S13: 0.2388
REMARK 3 S21: 2.2109 S22: 0.5971 S23: -0.4475
REMARK 3 S31: -1.3757 S32: -0.7753 S33: -0.2562
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN H OR CHAIN I
REMARK 3 ORIGIN FOR THE GROUP (A): -71.9759 31.4826 77.2020
REMARK 3 T TENSOR
REMARK 3 T11: 4.4176 T22: 3.2456
REMARK 3 T33: 2.9480 T12: -0.4538
REMARK 3 T13: -0.4172 T23: -0.1055
REMARK 3 L TENSOR
REMARK 3 L11: 1.8139 L22: 1.0881
REMARK 3 L33: 0.1116 L12: 0.4156
REMARK 3 L13: -0.3379 L23: -0.8166
REMARK 3 S TENSOR
REMARK 3 S11: 0.1779 S12: -0.9941 S13: 0.2729
REMARK 3 S21: 1.1918 S22: -0.1075 S23: -0.0393
REMARK 3 S31: -0.4284 S32: -0.2648 S33: -0.1488
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE MOLECULAR REPLACEMENT SOLUTION HAS
REMARK 3 BEEN RIGID BODY REFINED TO OBTAIN THE OVERALL ASSEMBLY OF THE
REMARK 3 COMPLEX. NO REBUILDING HAS BEEN PERFORMED DUE TO LIMITED
REMARK 3 RESOLUTION. RBX1 RESIDUES 40-108 AND CUL4B RESIDUES 208-209 HAVE
REMARK 3 BEEN REMOVED DUE TO UNCERTAINTY OF CONFORMATIONS.
REMARK 3 STEREOCHEMISTRY IS BASED ON THE SEARCH MODELS 3EI2 AND 4A0C.
REMARK 4
REMARK 4 4A0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1290049591.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0015
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13547
REMARK 200 RESOLUTION RANGE HIGH (A) : 7.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 7.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 7.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRIES 3EI2, 4A0C
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH 6.2, 3.1% PEG 6000, 4%
REMARK 280 ETHYLENEGLYCOL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 77.92000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 123470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, R, S
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 121070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, I, T, U
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 GLY A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 0
REMARK 465 MET A 291
REMARK 465 ASP A 292
REMARK 465 GLY A 293
REMARK 465 THR A 294
REMARK 465 SER A 772
REMARK 465 SER A 773
REMARK 465 SER A 774
REMARK 465 THR A 775
REMARK 465 ALA A 776
REMARK 465 PRO A 777
REMARK 465 HIS A 778
REMARK 465 GLU A 779
REMARK 465 THR A 780
REMARK 465 SER A 781
REMARK 465 PHE A 782
REMARK 465 GLY A 783
REMARK 465 ASN A 1016
REMARK 465 LEU A 1017
REMARK 465 GLY A 1018
REMARK 465 GLU A 1019
REMARK 465 THR A 1020
REMARK 465 SER A 1021
REMARK 465 THR A 1022
REMARK 465 LEU A 1112
REMARK 465 GLN A 1113
REMARK 465 TYR A 1114
REMARK 465 ASP A 1115
REMARK 465 ASP A 1116
REMARK 465 GLY A 1117
REMARK 465 SER A 1118
REMARK 465 GLY A 1119
REMARK 465 MET A 1120
REMARK 465 LYS A 1121
REMARK 465 ARG A 1122
REMARK 465 GLU A 1123
REMARK 465 MET B 76
REMARK 465 HIS B 77
REMARK 465 HIS B 78
REMARK 465 HIS B 79
REMARK 465 HIS B 80
REMARK 465 HIS B 81
REMARK 465 HIS B 82
REMARK 465 ARG B 83
REMARK 465 ARG B 84
REMARK 465 LEU B 85
REMARK 465 VAL B 86
REMARK 465 PRO B 87
REMARK 465 ARG B 88
REMARK 465 GLY B 89
REMARK 465 SER B 90
REMARK 465 GLY B 91
REMARK 465 GLY B 92
REMARK 465 ARG B 93
REMARK 465 THR B 94
REMARK 465 GLY B 95
REMARK 465 GLY B 96
REMARK 465 GLN B 97
REMARK 465 LYS B 98
REMARK 465 LYS B 99
REMARK 465 VAL B 100
REMARK 465 ASP B 456
REMARK 465 THR B 457
REMARK 465 GLY C -3
REMARK 465 GLY C -2
REMARK 465 GLY C -1
REMARK 465 ARG C 0
REMARK 465 MET C 291
REMARK 465 ASP C 292
REMARK 465 GLY C 293
REMARK 465 THR C 294
REMARK 465 SER C 772
REMARK 465 SER C 773
REMARK 465 SER C 774
REMARK 465 THR C 775
REMARK 465 ALA C 776
REMARK 465 PRO C 777
REMARK 465 HIS C 778
REMARK 465 GLU C 779
REMARK 465 THR C 780
REMARK 465 SER C 781
REMARK 465 PHE C 782
REMARK 465 GLY C 783
REMARK 465 ASN C 1016
REMARK 465 LEU C 1017
REMARK 465 GLY C 1018
REMARK 465 GLU C 1019
REMARK 465 THR C 1020
REMARK 465 SER C 1021
REMARK 465 THR C 1022
REMARK 465 LEU C 1112
REMARK 465 GLN C 1113
REMARK 465 TYR C 1114
REMARK 465 ASP C 1115
REMARK 465 ASP C 1116
REMARK 465 GLY C 1117
REMARK 465 SER C 1118
REMARK 465 GLY C 1119
REMARK 465 MET C 1120
REMARK 465 LYS C 1121
REMARK 465 ARG C 1122
REMARK 465 GLU C 1123
REMARK 465 MET D 76
REMARK 465 HIS D 77
REMARK 465 HIS D 78
REMARK 465 HIS D 79
REMARK 465 HIS D 80
REMARK 465 HIS D 81
REMARK 465 HIS D 82
REMARK 465 ARG D 83
REMARK 465 ARG D 84
REMARK 465 LEU D 85
REMARK 465 VAL D 86
REMARK 465 PRO D 87
REMARK 465 ARG D 88
REMARK 465 GLY D 89
REMARK 465 SER D 90
REMARK 465 GLY D 91
REMARK 465 GLY D 92
REMARK 465 ARG D 93
REMARK 465 THR D 94
REMARK 465 GLY D 95
REMARK 465 GLY D 96
REMARK 465 GLN D 97
REMARK 465 LYS D 98
REMARK 465 LYS D 99
REMARK 465 VAL D 100
REMARK 465 ASP D 456
REMARK 465 THR D 457
REMARK 465 GLY E 189
REMARK 465 GLY E 190
REMARK 465 GLY E 191
REMARK 465 ARG E 192
REMARK 465 GLY E 193
REMARK 465 SER E 194
REMARK 465 ALA E 195
REMARK 465 LYS E 208
REMARK 465 LEU E 209
REMARK 465 PRO E 209A
REMARK 465 GLY E 574
REMARK 465 ASN E 575
REMARK 465 LYS E 576
REMARK 465 VAL E 671
REMARK 465 PRO E 672
REMARK 465 GLY E 673
REMARK 465 ASN E 674
REMARK 465 MET F 11
REMARK 465 GLY F 12
REMARK 465 THR F 13
REMARK 465 ASN F 14
REMARK 465 SER F 15
REMARK 465 GLY F 16
REMARK 465 ALA F 17
REMARK 465 GLY F 18
REMARK 465 ASP F 40
REMARK 465 ASN F 41
REMARK 465 CYS F 42
REMARK 465 ALA F 43
REMARK 465 ILE F 44
REMARK 465 CYS F 45
REMARK 465 ARG F 46
REMARK 465 ASN F 47
REMARK 465 HIS F 48
REMARK 465 ILE F 49
REMARK 465 MET F 50
REMARK 465 ASP F 51
REMARK 465 LEU F 52
REMARK 465 CYS F 53
REMARK 465 ILE F 54
REMARK 465 GLU F 55
REMARK 465 CYS F 56
REMARK 465 GLN F 57
REMARK 465 ALA F 58
REMARK 465 ASN F 59
REMARK 465 GLN F 60
REMARK 465 ALA F 61
REMARK 465 SER F 62
REMARK 465 ALA F 63
REMARK 465 THR F 64
REMARK 465 SER F 65
REMARK 465 GLU F 66
REMARK 465 GLU F 67
REMARK 465 CYS F 68
REMARK 465 THR F 69
REMARK 465 VAL F 70
REMARK 465 ALA F 71
REMARK 465 TRP F 72
REMARK 465 GLY F 73
REMARK 465 VAL F 74
REMARK 465 CYS F 75
REMARK 465 ASN F 76
REMARK 465 HIS F 77
REMARK 465 ALA F 78
REMARK 465 PHE F 79
REMARK 465 HIS F 80
REMARK 465 PHE F 81
REMARK 465 HIS F 82
REMARK 465 CYS F 83
REMARK 465 ILE F 84
REMARK 465 SER F 85
REMARK 465 ARG F 86
REMARK 465 TRP F 87
REMARK 465 LEU F 88
REMARK 465 LYS F 89
REMARK 465 THR F 90
REMARK 465 ARG F 91
REMARK 465 GLN F 92
REMARK 465 VAL F 93
REMARK 465 CYS F 94
REMARK 465 PRO F 95
REMARK 465 LEU F 96
REMARK 465 ASP F 97
REMARK 465 ASN F 98
REMARK 465 ARG F 99
REMARK 465 GLU F 100
REMARK 465 TRP F 101
REMARK 465 GLU F 102
REMARK 465 PHE F 103
REMARK 465 GLN F 104
REMARK 465 LYS F 105
REMARK 465 TYR F 106
REMARK 465 GLY F 107
REMARK 465 HIS F 108
REMARK 465 GLY H 189
REMARK 465 GLY H 190
REMARK 465 GLY H 191
REMARK 465 ARG H 192
REMARK 465 GLY H 193
REMARK 465 SER H 194
REMARK 465 ALA H 195
REMARK 465 LYS H 208
REMARK 465 LEU H 209
REMARK 465 PRO H 209A
REMARK 465 GLY H 574
REMARK 465 ASN H 575
REMARK 465 LYS H 576
REMARK 465 VAL H 671
REMARK 465 PRO H 672
REMARK 465 GLY H 673
REMARK 465 ASN H 674
REMARK 465 MET I 11
REMARK 465 GLY I 12
REMARK 465 THR I 13
REMARK 465 ASN I 14
REMARK 465 SER I 15
REMARK 465 GLY I 16
REMARK 465 ALA I 17
REMARK 465 GLY I 18
REMARK 465 ASP I 40
REMARK 465 ASN I 41
REMARK 465 CYS I 42
REMARK 465 ALA I 43
REMARK 465 ILE I 44
REMARK 465 CYS I 45
REMARK 465 ARG I 46
REMARK 465 ASN I 47
REMARK 465 HIS I 48
REMARK 465 ILE I 49
REMARK 465 MET I 50
REMARK 465 ASP I 51
REMARK 465 LEU I 52
REMARK 465 CYS I 53
REMARK 465 ILE I 54
REMARK 465 GLU I 55
REMARK 465 CYS I 56
REMARK 465 GLN I 57
REMARK 465 ALA I 58
REMARK 465 ASN I 59
REMARK 465 GLN I 60
REMARK 465 ALA I 61
REMARK 465 SER I 62
REMARK 465 ALA I 63
REMARK 465 THR I 64
REMARK 465 SER I 65
REMARK 465 GLU I 66
REMARK 465 GLU I 67
REMARK 465 CYS I 68
REMARK 465 THR I 69
REMARK 465 VAL I 70
REMARK 465 ALA I 71
REMARK 465 TRP I 72
REMARK 465 GLY I 73
REMARK 465 VAL I 74
REMARK 465 CYS I 75
REMARK 465 ASN I 76
REMARK 465 HIS I 77
REMARK 465 ALA I 78
REMARK 465 PHE I 79
REMARK 465 HIS I 80
REMARK 465 PHE I 81
REMARK 465 HIS I 82
REMARK 465 CYS I 83
REMARK 465 ILE I 84
REMARK 465 SER I 85
REMARK 465 ARG I 86
REMARK 465 TRP I 87
REMARK 465 LEU I 88
REMARK 465 LYS I 89
REMARK 465 THR I 90
REMARK 465 ARG I 91
REMARK 465 GLN I 92
REMARK 465 VAL I 93
REMARK 465 CYS I 94
REMARK 465 PRO I 95
REMARK 465 LEU I 96
REMARK 465 ASP I 97
REMARK 465 ASN I 98
REMARK 465 ARG I 99
REMARK 465 GLU I 100
REMARK 465 TRP I 101
REMARK 465 GLU I 102
REMARK 465 PHE I 103
REMARK 465 GLN I 104
REMARK 465 LYS I 105
REMARK 465 TYR I 106
REMARK 465 GLY I 107
REMARK 465 HIS I 108
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 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 PHE A 323 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 369 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 388 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 389 CG1 CG2 CD1
REMARK 470 ILE A 390 CG1 CG2 CD1
REMARK 470 ARG A 391 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 392 CG OD1 ND2
REMARK 470 LYS A 408 CG CD CE NZ
REMARK 470 TRP A 561 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 561 CZ3 CH2
REMARK 470 ARG A 655 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 663 CG OD1 ND2
REMARK 470 ASN A 670 CG OD1 ND2
REMARK 470 ASN A 672 CG OD1 ND2
REMARK 470 GLU A 706 CG CD OE1 OE2
REMARK 470 GLN A 708 CG CD OE1 NE2
REMARK 470 ARG A 722 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 769 CB CG CD CE NZ
REMARK 470 VAL A 836 CG1 CG2
REMARK 470 PRO A 843 CG CD
REMARK 470 TYR A 871 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 910 CG SD CE
REMARK 470 ARG A 989 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 991 CG ND1 CD2 CE1 NE2
REMARK 470 MET A1014 CG SD CE
REMARK 470 GLN A1025 CG CD OE1 NE2
REMARK 470 LYS A1063 CG CD CE NZ
REMARK 470 ARG A1080 CD NE CZ NH1 NH2
REMARK 470 ARG A1102 CD NE CZ NH1 NH2
REMARK 470 GLU A1134 CG CD OE1 OE2
REMARK 470 ARG A1138 CD NE CZ NH1 NH2
REMARK 470 THR B 103 OG1 CG2
REMARK 470 SER B 104 OG
REMARK 470 LEU B 106 CG CD1 CD2
REMARK 470 HIS B 107 CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 119 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 158 OG1 CG2
REMARK 470 ARG B 289 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 112 CG1 CG2 CD1
REMARK 470 ARG C 198 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 208 CG CD CE NZ
REMARK 470 GLU C 368 CG CD OE1 OE2
REMARK 470 ARG C 369 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 391 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 408 CG CD CE NZ
REMARK 470 TRP C 561 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 561 CZ3 CH2
REMARK 470 PHE C 668 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 769 CB CG CD CE NZ
REMARK 470 GLN C 859 CG CD OE1 NE2
REMARK 470 TYR C 871 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE C 949 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 989 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 991 CG ND1 CD2 CE1 NE2
REMARK 470 MET C1014 CG SD CE
REMARK 470 GLN C1025 CG CD OE1 NE2
REMARK 470 LEU C1051 CG CD1 CD2
REMARK 470 MET C1054 CG SD CE
REMARK 470 LYS C1063 CG CD CE NZ
REMARK 470 LYS C1067 CG CD CE NZ
REMARK 470 ARG C1080 CD NE CZ NH1 NH2
REMARK 470 ARG C1102 CD NE CZ NH1 NH2
REMARK 470 GLN C1106 CG CD OE1 NE2
REMARK 470 GLU C1107 CG CD OE1 OE2
REMARK 470 ARG C1138 CD NE CZ NH1 NH2
REMARK 470 LYS E 204 CG CD CE NZ
REMARK 470 LYS E 206 CG CD CE NZ
REMARK 470 GLU E 238 CG CD OE1 OE2
REMARK 470 ASP E 290 CG OD1 OD2
REMARK 470 TRP E 293 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP E 293 CZ3 CH2
REMARK 470 ARG E 298 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 312 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 333 CG CD NE CZ NH1 NH2
REMARK 470 VAL E 342 CG1 CG2
REMARK 470 LEU E 353 CG CD1 CD2
REMARK 470 GLU E 357 CG CD OE1 OE2
REMARK 470 ILE E 363 CG1 CG2 CD1
REMARK 470 ARG E 365 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 367 CG CD1 CD2
REMARK 470 GLU E 386 CG CD OE1 OE2
REMARK 470 TYR E 413 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR E 431 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU E 445 CG CD OE1 OE2
REMARK 470 LYS E 446 CG CD CE NZ
REMARK 470 ASN E 553 CG OD1 ND2
REMARK 470 MET E 591 CG SD CE
REMARK 470 PHE E 594 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU E 636 CG CD OE1 OE2
REMARK 470 LYS E 800 CG CD CE NZ
REMARK 470 LEU E 818 CG CD1 CD2
REMARK 470 TRP F 33 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP F 33 CZ3 CH2
REMARK 470 LYS H 204 CG CD CE NZ
REMARK 470 LYS H 206 CG CD CE NZ
REMARK 470 ILE H 233 CG1 CG2 CD1
REMARK 470 GLU H 238 CG CD OE1 OE2
REMARK 470 ARG H 276 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 312 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 333 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 345 CG CD CE NZ
REMARK 470 GLU H 357 CG CD OE1 OE2
REMARK 470 ARG H 365 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 378 CG CD1 CD2
REMARK 470 GLU H 423 CG CD OE1 OE2
REMARK 470 ARG H 427 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 428 CG CD1 CD2
REMARK 470 TYR H 431 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU H 432 CG CD1 CD2
REMARK 470 VAL H 483 CG1 CG2
REMARK 470 LYS H 525 CG CD CE NZ
REMARK 470 LEU H 818 CG CD1 CD2
REMARK 470 VAL I 38 CG1 CG2
REMARK 470 VAL I 39 CG1 CG2
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 PRO A 412 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 SER A 624 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 PRO A 656 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO A 688 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 ASP A 689 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500 PRO A 716 C - N - CD ANGL. DEV. = -15.3 DEGREES
REMARK 500 PRO C 412 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 SER C 624 N - CA - C ANGL. DEV. = 18.9 DEGREES
REMARK 500 PRO C 656 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO C 688 CA - N - CD ANGL. DEV. = -8.4 DEGREES
REMARK 500 PRO C 688 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 ASP C 689 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 PRO E 556 C - N - CD ANGL. DEV. = -17.4 DEGREES
REMARK 500 DC R 13 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG S 4 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DG S 4 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC S 5 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT S 7 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA S 12 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG S 13 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC S 14 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC T 13 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG U 4 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG U 4 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC U 5 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT U 7 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA U 12 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG U 13 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC U 14 O4' - C1' - N1 ANGL. DEV. = 2.9 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 LYS A 35 76.33 -116.08
REMARK 500 ASN A 36 -91.14 61.33
REMARK 500 GLU A 47 55.36 34.03
REMARK 500 LEU A 145 63.09 -101.14
REMARK 500 HIS A 163 78.06 -119.98
REMARK 500 ASN A 241 86.20 -160.18
REMARK 500 LEU A 317 -72.51 -111.30
REMARK 500 ASP A 318 149.82 -177.40
REMARK 500 LEU A 367 -93.40 -64.82
REMARK 500 ARG A 369 -138.11 -108.79
REMARK 500 GLN A 372 -93.31 -75.78
REMARK 500 PHE A 382 -144.36 54.23
REMARK 500 ILE A 389 -118.46 -150.62
REMARK 500 ILE A 390 169.24 139.05
REMARK 500 ARG A 391 117.57 -179.51
REMARK 500 ASN A 392 69.37 -61.20
REMARK 500 ASP A 403 61.95 -107.67
REMARK 500 LEU A 413 -164.59 -102.73
REMARK 500 ARG A 414 84.86 -157.64
REMARK 500 ASN A 418 -82.86 -63.74
REMARK 500 ASP A 423 4.24 -155.17
REMARK 500 VAL A 430 -108.93 -43.35
REMARK 500 GLN A 432 175.08 173.94
REMARK 500 THR A 446 -146.61 -87.29
REMARK 500 MET A 449 -78.02 -38.26
REMARK 500 ASP A 453 -4.10 -144.00
REMARK 500 CYS A 460 142.20 174.52
REMARK 500 GLN A 481 -96.72 -76.68
REMARK 500 SER A 488 140.56 171.19
REMARK 500 TRP A 490 -179.13 -66.29
REMARK 500 PRO A 493 -42.96 -28.11
REMARK 500 CYS A 503 167.26 168.02
REMARK 500 SER A 505 -59.18 -28.70
REMARK 500 ASP A 542 118.21 -162.34
REMARK 500 LEU A 546 -163.49 -129.97
REMARK 500 SER A 549 159.97 -37.79
REMARK 500 ASN A 550 77.73 -110.47
REMARK 500 TRP A 561 -67.21 -105.52
REMARK 500 THR A 562 -87.37 -64.18
REMARK 500 ASP A 563 -24.34 -34.59
REMARK 500 ALA A 566 89.65 -163.74
REMARK 500 LEU A 571 -72.31 -55.57
REMARK 500 LEU A 582 -105.68 -145.75
REMARK 500 GLU A 585 -10.16 -141.36
REMARK 500 ARG A 589 -14.38 -142.36
REMARK 500 LEU A 592 125.32 177.58
REMARK 500 PHE A 596 -71.37 -98.76
REMARK 500 SER A 598 -3.13 158.99
REMARK 500 ALA A 605 114.94 -161.39
REMARK 500 LEU A 606 -178.68 -66.35
REMARK 500
REMARK 500 THIS ENTRY HAS 318 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B5M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DDB1
REMARK 900 RELATED ID: 2B5L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF DDB1 IN COMPLEX WITH SIMIAN VIRUS 5 VPROTEIN
REMARK 900 RELATED ID: 2HYE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DDB1-CUL4A-RBX1-SV5V COMPLEX
REMARK 900 RELATED ID: 2B5N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DDB1 BPB DOMAIN
REMARK 900 RELATED ID: 4A0A RELATED DB: PDB
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 16 BP CPD- DUPLEX (PYRIMIDINE
REMARK 900 AT D-1 POSITION) AT 3.6 A RESOLUTION (CPD 3)
REMARK 900 RELATED ID: 4A0B RELATED DB: PDB
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 16 BP CPD- DUPLEX (PYRIMIDINE
REMARK 900 AT D-1 POSITION) AT 3.8 A RESOLUTION (CPD 4)
REMARK 900 RELATED ID: 4A08 RELATED DB: PDB
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 13 BP CPD- DUPLEX (PURINE AT
REMARK 900 D-1 POSITION) AT 3.0 A RESOLUTION (CPD 1)
REMARK 900 RELATED ID: 4A09 RELATED DB: PDB
REMARK 900 STRUCTURE OF HSDDB1-DRDDB2 BOUND TO A 15 BP CPD- DUPLEX (PURINE AT
REMARK 900 D-1 POSITION) AT 3.1 A RESOLUTION (CPD 2)
REMARK 900 RELATED ID: 4A0C RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX
REMARK 900 RELATED ID: 4A0K RELATED DB: PDB
REMARK 900 RELATED ID: 3EI1 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI2 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI3 RELATED DB: PDB
REMARK 900 RELATED ID: 3EI4 RELATED DB: PDB
DBREF 4A0L C 1 1140 UNP Q16531 DDB1_HUMAN 1 1140
DBREF 4A0L A 1 1140 UNP Q16531 DDB1_HUMAN 1 1140
DBREF 4A0L B 94 457 UNP Q2YDS1 DDB2_DANRE 60 423
DBREF 4A0L D 94 457 UNP Q2YDS1 DDB2_DANRE 60 423
DBREF 4A0L E 193 913 UNP Q13620 CUL4B_HUMAN 192 913
DBREF 4A0L H 193 913 UNP Q13620 CUL4B_HUMAN 192 913
DBREF 4A0L F 12 108 UNP P62878 RBX1_MOUSE 12 108
DBREF 4A0L I 12 108 UNP P62878 RBX1_MOUSE 12 108
DBREF 4A0L R 3 14 PDB 4A0L 4A0L 3 14
DBREF 4A0L S 3 14 PDB 4A0L 4A0L 3 14
DBREF 4A0L T 3 14 PDB 4A0L 4A0L 3 14
DBREF 4A0L U 3 14 PDB 4A0L 4A0L 3 14
SEQADV 4A0L GLY A -3 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L GLY A -2 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L GLY A -1 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L ARG A 0 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L MET B 76 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS B 77 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS B 78 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS B 79 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS B 80 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS B 81 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS B 82 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG B 83 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG B 84 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L LEU B 85 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L VAL B 86 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L PRO B 87 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG B 88 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLY B 89 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L SER B 90 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLY B 91 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLY B 92 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG B 93 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLN B 180 UNP Q2YDS1 LEU 146 VARIANT
SEQADV 4A0L ARG B 214 UNP Q2YDS1 TRP 180 VARIANT
SEQADV 4A0L GLY C -3 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L GLY C -2 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L GLY C -1 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L ARG C 0 UNP Q16531 EXPRESSION TAG
SEQADV 4A0L MET D 76 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS D 77 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS D 78 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS D 79 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS D 80 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS D 81 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L HIS D 82 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG D 83 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG D 84 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L LEU D 85 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L VAL D 86 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L PRO D 87 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG D 88 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLY D 89 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L SER D 90 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLY D 91 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLY D 92 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L ARG D 93 UNP Q2YDS1 EXPRESSION TAG
SEQADV 4A0L GLN D 180 UNP Q2YDS1 LEU 146 VARIANT
SEQADV 4A0L ARG D 214 UNP Q2YDS1 TRP 180 VARIANT
SEQADV 4A0L GLY E 189 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L GLY E 190 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L GLY E 191 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L ARG E 192 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L MET F 11 UNP P62878 EXPRESSION TAG
SEQADV 4A0L GLY H 189 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L GLY H 190 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L GLY H 191 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L ARG H 192 UNP Q13620 EXPRESSION TAG
SEQADV 4A0L MET I 11 UNP P62878 EXPRESSION TAG
SEQRES 1 A 1144 GLY GLY GLY ARG MET SER TYR ASN TYR VAL VAL THR ALA
SEQRES 2 A 1144 GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR GLY HIS
SEQRES 3 A 1144 PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE ALA LYS
SEQRES 4 A 1144 ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA GLU GLY
SEQRES 5 A 1144 LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY LYS ILE
SEQRES 6 A 1144 ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU SER LYS
SEQRES 7 A 1144 ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN ALA CYS
SEQRES 8 A 1144 ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE ASP ILE
SEQRES 9 A 1144 ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE GLY
SEQRES 10 A 1144 ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE ASP PRO
SEQRES 11 A 1144 GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP GLY LEU
SEQRES 12 A 1144 PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU LEU
SEQRES 13 A 1144 LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL ILE
SEQRES 14 A 1144 ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO THR ILE
SEQRES 15 A 1144 CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL LYS
SEQRES 16 A 1144 THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE ASN LYS
SEQRES 17 A 1144 GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA SER
SEQRES 18 A 1144 MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA ILE
SEQRES 19 A 1144 ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN GLY ASP
SEQRES 20 A 1144 LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN SER
SEQRES 21 A 1144 THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY SER
SEQRES 22 A 1144 ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU PHE MET
SEQRES 23 A 1144 LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY THR VAL
SEQRES 24 A 1144 THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU THR
SEQRES 25 A 1144 SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN GLY VAL
SEQRES 26 A 1144 VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN LEU VAL
SEQRES 27 A 1144 LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER TYR VAL
SEQRES 28 A 1144 VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO ILE VAL
SEQRES 29 A 1144 ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN GLY
SEQRES 30 A 1144 GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU GLY SER
SEQRES 31 A 1144 LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS GLU HIS
SEQRES 32 A 1144 ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU TRP PRO
SEQRES 33 A 1144 LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP THR LEU
SEQRES 34 A 1144 VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU MET LEU
SEQRES 35 A 1144 ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET GLY PHE
SEQRES 36 A 1144 VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN VAL ALA
SEQRES 37 A 1144 HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER VAL ARG
SEQRES 38 A 1144 LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER GLU TRP
SEQRES 39 A 1144 LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA SER CYS
SEQRES 40 A 1144 ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG ALA LEU
SEQRES 41 A 1144 TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG GLN ILE
SEQRES 42 A 1144 SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS LEU ASP
SEQRES 43 A 1144 ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER PRO LEU
SEQRES 44 A 1144 CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA ARG ILE
SEQRES 45 A 1144 LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS GLU MET
SEQRES 46 A 1144 LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU MET THR
SEQRES 47 A 1144 THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA LEU GLY
SEQRES 48 A 1144 ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE GLU THR
SEQRES 49 A 1144 GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU GLY THR
SEQRES 50 A 1144 GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU SER THR
SEQRES 51 A 1144 THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR VAL ILE
SEQRES 52 A 1144 TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN VAL ASN
SEQRES 53 A 1144 LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN SER ASP
SEQRES 54 A 1144 GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN SER THR
SEQRES 55 A 1144 LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS LEU HIS
SEQRES 56 A 1144 ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG LYS ILE
SEQRES 57 A 1144 CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL LEU SER
SEQRES 58 A 1144 SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY THR THR
SEQRES 59 A 1144 ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU SER SER
SEQRES 60 A 1144 SER VAL SER SER SER LYS LEU PHE SER SER SER THR ALA
SEQRES 61 A 1144 PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU VAL HIS
SEQRES 62 A 1144 ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU VAL LEU
SEQRES 63 A 1144 HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA LEU SER
SEQRES 64 A 1144 LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN THR TYR
SEQRES 65 A 1144 PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU GLU ALA
SEQRES 66 A 1144 GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN TYR SER
SEQRES 67 A 1144 ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU VAL LYS
SEQRES 68 A 1144 GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY LYS LEU
SEQRES 69 A 1144 LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR GLU TRP
SEQRES 70 A 1144 THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN HIS TYR
SEQRES 71 A 1144 ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS GLY ASP
SEQRES 72 A 1144 PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL LEU LEU
SEQRES 73 A 1144 LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU GLU ILE
SEQRES 74 A 1144 ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA VAL GLU
SEQRES 75 A 1144 ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU ASN ALA
SEQRES 76 A 1144 PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA ALA THR
SEQRES 77 A 1144 THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL GLY LEU
SEQRES 78 A 1144 PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS HIS GLY
SEQRES 79 A 1144 SER LEU VAL MET GLN ASN LEU GLY GLU THR SER THR PRO
SEQRES 80 A 1144 THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN GLY MET
SEQRES 81 A 1144 ILE GLY LEU VAL THR SER LEU SER GLU SER TRP TYR ASN
SEQRES 82 A 1144 LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS VAL ILE
SEQRES 83 A 1144 LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP ARG SER
SEQRES 84 A 1144 PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR GLY PHE
SEQRES 85 A 1144 ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP ILE SER
SEQRES 86 A 1144 ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU GLN TYR
SEQRES 87 A 1144 ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR ALA ASP
SEQRES 88 A 1144 ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG ILE HIS
SEQRES 1 B 382 MET HIS HIS HIS HIS HIS HIS ARG ARG LEU VAL PRO ARG
SEQRES 2 B 382 GLY SER GLY GLY ARG THR GLY GLY GLN LYS LYS VAL GLY
SEQRES 3 B 382 GLN THR SER ILE LEU HIS TYR ILE TYR LYS SER SER LEU
SEQRES 4 B 382 GLY GLN SER ILE HIS ALA GLN LEU ARG GLN CYS LEU GLN
SEQRES 5 B 382 GLU PRO PHE ILE ARG SER LEU LYS SER TYR LYS LEU HIS
SEQRES 6 B 382 ARG THR ALA SER PRO PHE ASP ARG ARG VAL THR SER LEU
SEQRES 7 B 382 GLU TRP HIS PRO THR HIS PRO THR THR VAL ALA VAL GLY
SEQRES 8 B 382 SER LYS GLY GLY ASP ILE ILE LEU TRP ASP TYR ASP VAL
SEQRES 9 B 382 GLN ASN LYS THR SER PHE ILE GLN GLY MET GLY PRO GLY
SEQRES 10 B 382 ASP ALA ILE THR GLY MET LYS PHE ASN GLN PHE ASN THR
SEQRES 11 B 382 ASN GLN LEU PHE VAL SER SER ILE ARG GLY ALA THR THR
SEQRES 12 B 382 LEU ARG ASP PHE SER GLY SER VAL ILE GLN VAL PHE ALA
SEQRES 13 B 382 LYS THR ASP SER TRP ASP TYR TRP TYR CYS CYS VAL ASP
SEQRES 14 B 382 VAL SER VAL SER ARG GLN MET LEU ALA THR GLY ASP SER
SEQRES 15 B 382 THR GLY ARG LEU LEU LEU LEU GLY LEU ASP GLY HIS GLU
SEQRES 16 B 382 ILE PHE LYS GLU LYS LEU HIS LYS ALA LYS VAL THR HIS
SEQRES 17 B 382 ALA GLU PHE ASN PRO ARG CYS ASP TRP LEU MET ALA THR
SEQRES 18 B 382 SER SER VAL ASP ALA THR VAL LYS LEU TRP ASP LEU ARG
SEQRES 19 B 382 ASN ILE LYS ASP LYS ASN SER TYR ILE ALA GLU MET PRO
SEQRES 20 B 382 HIS GLU LYS PRO VAL ASN ALA ALA TYR PHE ASN PRO THR
SEQRES 21 B 382 ASP SER THR LYS LEU LEU THR THR ASP GLN ARG ASN GLU
SEQRES 22 B 382 ILE ARG VAL TYR SER SER TYR ASP TRP SER LYS PRO ASP
SEQRES 23 B 382 GLN ILE ILE ILE HIS PRO HIS ARG GLN PHE GLN HIS LEU
SEQRES 24 B 382 THR PRO ILE LYS ALA THR TRP HIS PRO MET TYR ASP LEU
SEQRES 25 B 382 ILE VAL ALA GLY ARG TYR PRO ASP ASP GLN LEU LEU LEU
SEQRES 26 B 382 ASN ASP LYS ARG THR ILE ASP ILE TYR ASP ALA ASN SER
SEQRES 27 B 382 GLY GLY LEU VAL HIS GLN LEU ARG ASP PRO ASN ALA ALA
SEQRES 28 B 382 GLY ILE ILE SER LEU ASN LYS PHE SER PRO THR GLY ASP
SEQRES 29 B 382 VAL LEU ALA SER GLY MET GLY PHE ASN ILE LEU ILE TRP
SEQRES 30 B 382 ASN ARG GLU ASP THR
SEQRES 1 C 1144 GLY GLY GLY ARG MET SER TYR ASN TYR VAL VAL THR ALA
SEQRES 2 C 1144 GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR GLY HIS
SEQRES 3 C 1144 PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE ALA LYS
SEQRES 4 C 1144 ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA GLU GLY
SEQRES 5 C 1144 LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY LYS ILE
SEQRES 6 C 1144 ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU SER LYS
SEQRES 7 C 1144 ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN ALA CYS
SEQRES 8 C 1144 ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE ASP ILE
SEQRES 9 C 1144 ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE GLY
SEQRES 10 C 1144 ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE ASP PRO
SEQRES 11 C 1144 GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP GLY LEU
SEQRES 12 C 1144 PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU LEU
SEQRES 13 C 1144 LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL ILE
SEQRES 14 C 1144 ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO THR ILE
SEQRES 15 C 1144 CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL LYS
SEQRES 16 C 1144 THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE ASN LYS
SEQRES 17 C 1144 GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA SER
SEQRES 18 C 1144 MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA ILE
SEQRES 19 C 1144 ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN GLY ASP
SEQRES 20 C 1144 LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN SER
SEQRES 21 C 1144 THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY SER
SEQRES 22 C 1144 ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU PHE MET
SEQRES 23 C 1144 LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY THR VAL
SEQRES 24 C 1144 THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU THR
SEQRES 25 C 1144 SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN GLY VAL
SEQRES 26 C 1144 VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN LEU VAL
SEQRES 27 C 1144 LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER TYR VAL
SEQRES 28 C 1144 VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO ILE VAL
SEQRES 29 C 1144 ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN GLY
SEQRES 30 C 1144 GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU GLY SER
SEQRES 31 C 1144 LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS GLU HIS
SEQRES 32 C 1144 ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU TRP PRO
SEQRES 33 C 1144 LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP THR LEU
SEQRES 34 C 1144 VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU MET LEU
SEQRES 35 C 1144 ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET GLY PHE
SEQRES 36 C 1144 VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN VAL ALA
SEQRES 37 C 1144 HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER VAL ARG
SEQRES 38 C 1144 LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER GLU TRP
SEQRES 39 C 1144 LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA SER CYS
SEQRES 40 C 1144 ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG ALA LEU
SEQRES 41 C 1144 TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG GLN ILE
SEQRES 42 C 1144 SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS LEU ASP
SEQRES 43 C 1144 ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER PRO LEU
SEQRES 44 C 1144 CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA ARG ILE
SEQRES 45 C 1144 LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS GLU MET
SEQRES 46 C 1144 LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU MET THR
SEQRES 47 C 1144 THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA LEU GLY
SEQRES 48 C 1144 ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE GLU THR
SEQRES 49 C 1144 GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU GLY THR
SEQRES 50 C 1144 GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU SER THR
SEQRES 51 C 1144 THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR VAL ILE
SEQRES 52 C 1144 TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN VAL ASN
SEQRES 53 C 1144 LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN SER ASP
SEQRES 54 C 1144 GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN SER THR
SEQRES 55 C 1144 LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS LEU HIS
SEQRES 56 C 1144 ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG LYS ILE
SEQRES 57 C 1144 CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL LEU SER
SEQRES 58 C 1144 SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY THR THR
SEQRES 59 C 1144 ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU SER SER
SEQRES 60 C 1144 SER VAL SER SER SER LYS LEU PHE SER SER SER THR ALA
SEQRES 61 C 1144 PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU VAL HIS
SEQRES 62 C 1144 ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU VAL LEU
SEQRES 63 C 1144 HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA LEU SER
SEQRES 64 C 1144 LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN THR TYR
SEQRES 65 C 1144 PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU GLU ALA
SEQRES 66 C 1144 GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN TYR SER
SEQRES 67 C 1144 ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU VAL LYS
SEQRES 68 C 1144 GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY LYS LEU
SEQRES 69 C 1144 LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR GLU TRP
SEQRES 70 C 1144 THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN HIS TYR
SEQRES 71 C 1144 ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS GLY ASP
SEQRES 72 C 1144 PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL LEU LEU
SEQRES 73 C 1144 LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU GLU ILE
SEQRES 74 C 1144 ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA VAL GLU
SEQRES 75 C 1144 ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU ASN ALA
SEQRES 76 C 1144 PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA ALA THR
SEQRES 77 C 1144 THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL GLY LEU
SEQRES 78 C 1144 PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS HIS GLY
SEQRES 79 C 1144 SER LEU VAL MET GLN ASN LEU GLY GLU THR SER THR PRO
SEQRES 80 C 1144 THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN GLY MET
SEQRES 81 C 1144 ILE GLY LEU VAL THR SER LEU SER GLU SER TRP TYR ASN
SEQRES 82 C 1144 LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS VAL ILE
SEQRES 83 C 1144 LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP ARG SER
SEQRES 84 C 1144 PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR GLY PHE
SEQRES 85 C 1144 ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP ILE SER
SEQRES 86 C 1144 ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU GLN TYR
SEQRES 87 C 1144 ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR ALA ASP
SEQRES 88 C 1144 ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG ILE HIS
SEQRES 1 D 382 MET HIS HIS HIS HIS HIS HIS ARG ARG LEU VAL PRO ARG
SEQRES 2 D 382 GLY SER GLY GLY ARG THR GLY GLY GLN LYS LYS VAL GLY
SEQRES 3 D 382 GLN THR SER ILE LEU HIS TYR ILE TYR LYS SER SER LEU
SEQRES 4 D 382 GLY GLN SER ILE HIS ALA GLN LEU ARG GLN CYS LEU GLN
SEQRES 5 D 382 GLU PRO PHE ILE ARG SER LEU LYS SER TYR LYS LEU HIS
SEQRES 6 D 382 ARG THR ALA SER PRO PHE ASP ARG ARG VAL THR SER LEU
SEQRES 7 D 382 GLU TRP HIS PRO THR HIS PRO THR THR VAL ALA VAL GLY
SEQRES 8 D 382 SER LYS GLY GLY ASP ILE ILE LEU TRP ASP TYR ASP VAL
SEQRES 9 D 382 GLN ASN LYS THR SER PHE ILE GLN GLY MET GLY PRO GLY
SEQRES 10 D 382 ASP ALA ILE THR GLY MET LYS PHE ASN GLN PHE ASN THR
SEQRES 11 D 382 ASN GLN LEU PHE VAL SER SER ILE ARG GLY ALA THR THR
SEQRES 12 D 382 LEU ARG ASP PHE SER GLY SER VAL ILE GLN VAL PHE ALA
SEQRES 13 D 382 LYS THR ASP SER TRP ASP TYR TRP TYR CYS CYS VAL ASP
SEQRES 14 D 382 VAL SER VAL SER ARG GLN MET LEU ALA THR GLY ASP SER
SEQRES 15 D 382 THR GLY ARG LEU LEU LEU LEU GLY LEU ASP GLY HIS GLU
SEQRES 16 D 382 ILE PHE LYS GLU LYS LEU HIS LYS ALA LYS VAL THR HIS
SEQRES 17 D 382 ALA GLU PHE ASN PRO ARG CYS ASP TRP LEU MET ALA THR
SEQRES 18 D 382 SER SER VAL ASP ALA THR VAL LYS LEU TRP ASP LEU ARG
SEQRES 19 D 382 ASN ILE LYS ASP LYS ASN SER TYR ILE ALA GLU MET PRO
SEQRES 20 D 382 HIS GLU LYS PRO VAL ASN ALA ALA TYR PHE ASN PRO THR
SEQRES 21 D 382 ASP SER THR LYS LEU LEU THR THR ASP GLN ARG ASN GLU
SEQRES 22 D 382 ILE ARG VAL TYR SER SER TYR ASP TRP SER LYS PRO ASP
SEQRES 23 D 382 GLN ILE ILE ILE HIS PRO HIS ARG GLN PHE GLN HIS LEU
SEQRES 24 D 382 THR PRO ILE LYS ALA THR TRP HIS PRO MET TYR ASP LEU
SEQRES 25 D 382 ILE VAL ALA GLY ARG TYR PRO ASP ASP GLN LEU LEU LEU
SEQRES 26 D 382 ASN ASP LYS ARG THR ILE ASP ILE TYR ASP ALA ASN SER
SEQRES 27 D 382 GLY GLY LEU VAL HIS GLN LEU ARG ASP PRO ASN ALA ALA
SEQRES 28 D 382 GLY ILE ILE SER LEU ASN LYS PHE SER PRO THR GLY ASP
SEQRES 29 D 382 VAL LEU ALA SER GLY MET GLY PHE ASN ILE LEU ILE TRP
SEQRES 30 D 382 ASN ARG GLU ASP THR
SEQRES 1 E 726 GLY GLY GLY ARG GLY SER ALA LYS LYS LEU VAL ILE LYS
SEQRES 2 E 726 ASN PHE LYS ASP LYS PRO LYS LEU PRO GLU ASN TYR THR
SEQRES 3 E 726 ASP GLU THR TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA
SEQRES 4 E 726 ILE GLN ASN SER THR SER ILE LYS TYR ASN LEU GLU GLU
SEQRES 5 E 726 LEU TYR GLN ALA VAL GLU ASN LEU CYS SER TYR LYS ILE
SEQRES 6 E 726 SER ALA ASN LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU
SEQRES 7 E 726 ASP HIS ILE LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP
SEQRES 8 E 726 SER LEU ASP SER VAL LEU PHE LEU LYS LYS ILE ASP ARG
SEQRES 9 E 726 CYS TRP GLN ASN HIS CYS ARG GLN MET ILE MET ILE ARG
SEQRES 10 E 726 SER ILE PHE LEU PHE LEU ASP ARG THR TYR VAL LEU GLN
SEQRES 11 E 726 ASN SER MET LEU PRO SER ILE TRP ASP MET GLY LEU GLU
SEQRES 12 E 726 LEU PHE ARG ALA HIS ILE ILE SER ASP GLN LYS VAL GLN
SEQRES 13 E 726 ASN LYS THR ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG
SEQRES 14 E 726 GLU ARG ASN GLY GLU ALA ILE ASP ARG SER LEU LEU ARG
SEQRES 15 E 726 SER LEU LEU SER MET LEU SER ASP LEU GLN ILE TYR GLN
SEQRES 16 E 726 ASP SER PHE GLU GLN ARG PHE LEU GLU GLU THR ASN ARG
SEQRES 17 E 726 LEU TYR ALA ALA GLU GLY GLN LYS LEU MET GLN GLU ARG
SEQRES 18 E 726 GLU VAL PRO GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU
SEQRES 19 E 726 GLU GLU GLU ALA ASP ARG LEU ILE THR TYR LEU ASP GLN
SEQRES 20 E 726 THR THR GLN LYS SER LEU ILE ALA THR VAL GLU LYS GLN
SEQRES 21 E 726 LEU LEU GLY GLU HIS LEU THR ALA ILE LEU GLN LYS GLY
SEQRES 22 E 726 LEU ASN ASN LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU
SEQRES 23 E 726 SER LEU LEU TYR GLN LEU PHE SER ARG VAL ARG GLY GLY
SEQRES 24 E 726 VAL GLN VAL LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS
SEQRES 25 E 726 ALA PHE GLY SER THR ILE VAL ILE ASN PRO GLU LYS ASP
SEQRES 26 E 726 LYS THR MET VAL GLN GLU LEU LEU ASP PHE LYS ASP LYS
SEQRES 27 E 726 VAL ASP HIS ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU
SEQRES 28 E 726 LYS PHE ILE ASN ALA MET LYS GLU ALA PHE GLU THR PHE
SEQRES 29 E 726 ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU LEU ILE ALA
SEQRES 30 E 726 LYS TYR VAL ASP SER LYS LEU ARG ALA GLY ASN LYS GLU
SEQRES 31 E 726 ALA THR ASP GLU GLU LEU GLU LYS MET LEU ASP LYS ILE
SEQRES 32 E 726 MET ILE ILE PHE ARG PHE ILE TYR GLY LYS ASP VAL PHE
SEQRES 33 E 726 GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS ARG LEU LEU
SEQRES 34 E 726 VAL GLY LYS SER ALA SER VAL ASP ALA GLU LYS SER MET
SEQRES 35 E 726 LEU SER LYS LEU LYS HIS GLU CYS GLY ALA ALA PHE THR
SEQRES 36 E 726 SER LYS LEU GLU GLY MET PHE LYS ASP MET GLU LEU SER
SEQRES 37 E 726 LYS ASP ILE MET ILE GLN PHE LYS GLN TYR MET GLN ASN
SEQRES 38 E 726 GLN ASN VAL PRO GLY ASN ILE GLU LEU THR VAL ASN ILE
SEQRES 39 E 726 LEU THR MET GLY TYR TRP PRO THR TYR VAL PRO MET GLU
SEQRES 40 E 726 VAL HIS LEU PRO PRO GLU MET VAL LYS LEU GLN GLU ILE
SEQRES 41 E 726 PHE LYS THR PHE TYR LEU GLY LYS HIS SER GLY ARG LYS
SEQRES 42 E 726 LEU GLN TRP GLN SER THR LEU GLY HIS CYS VAL LEU LYS
SEQRES 43 E 726 ALA GLU PHE LYS GLU GLY LYS LYS GLU LEU GLN VAL SER
SEQRES 44 E 726 LEU PHE GLN THR LEU VAL LEU LEU MET PHE ASN GLU GLY
SEQRES 45 E 726 GLU GLU PHE SER LEU GLU GLU ILE LYS GLN ALA THR GLY
SEQRES 46 E 726 ILE GLU ASP GLY GLU LEU ARG ARG THR LEU GLN SER LEU
SEQRES 47 E 726 ALA CYS GLY LYS ALA ARG VAL LEU ALA LYS ASN PRO LYS
SEQRES 48 E 726 GLY LYS ASP ILE GLU ASP GLY ASP LYS PHE ILE CYS ASN
SEQRES 49 E 726 ASP ASP PHE LYS HIS LYS LEU PHE ARG ILE LYS ILE ASN
SEQRES 50 E 726 GLN ILE GLN MET LYS GLU THR VAL GLU GLU GLN ALA SER
SEQRES 51 E 726 THR THR GLU ARG VAL PHE GLN ASP ARG GLN TYR GLN ILE
SEQRES 52 E 726 ASP ALA ALA ILE VAL ARG ILE MET LYS MET ARG LYS THR
SEQRES 53 E 726 LEU SER HIS ASN LEU LEU VAL SER GLU VAL TYR ASN GLN
SEQRES 54 E 726 LEU LYS PHE PRO VAL LYS PRO ALA ASP LEU LYS LYS ARG
SEQRES 55 E 726 ILE GLU SER LEU ILE ASP ARG ASP TYR MET GLU ARG ASP
SEQRES 56 E 726 LYS GLU ASN PRO ASN GLN TYR ASN TYR ILE ALA
SEQRES 1 F 98 MET GLY THR ASN SER GLY ALA GLY LYS LYS ARG PHE GLU
SEQRES 2 F 98 VAL LYS LYS TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP
SEQRES 3 F 98 ILE VAL VAL ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE
SEQRES 4 F 98 MET ASP LEU CYS ILE GLU CYS GLN ALA ASN GLN ALA SER
SEQRES 5 F 98 ALA THR SER GLU GLU CYS THR VAL ALA TRP GLY VAL CYS
SEQRES 6 F 98 ASN HIS ALA PHE HIS PHE HIS CYS ILE SER ARG TRP LEU
SEQRES 7 F 98 LYS THR ARG GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP
SEQRES 8 F 98 GLU PHE GLN LYS TYR GLY HIS
SEQRES 1 H 726 GLY GLY GLY ARG GLY SER ALA LYS LYS LEU VAL ILE LYS
SEQRES 2 H 726 ASN PHE LYS ASP LYS PRO LYS LEU PRO GLU ASN TYR THR
SEQRES 3 H 726 ASP GLU THR TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA
SEQRES 4 H 726 ILE GLN ASN SER THR SER ILE LYS TYR ASN LEU GLU GLU
SEQRES 5 H 726 LEU TYR GLN ALA VAL GLU ASN LEU CYS SER TYR LYS ILE
SEQRES 6 H 726 SER ALA ASN LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU
SEQRES 7 H 726 ASP HIS ILE LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP
SEQRES 8 H 726 SER LEU ASP SER VAL LEU PHE LEU LYS LYS ILE ASP ARG
SEQRES 9 H 726 CYS TRP GLN ASN HIS CYS ARG GLN MET ILE MET ILE ARG
SEQRES 10 H 726 SER ILE PHE LEU PHE LEU ASP ARG THR TYR VAL LEU GLN
SEQRES 11 H 726 ASN SER MET LEU PRO SER ILE TRP ASP MET GLY LEU GLU
SEQRES 12 H 726 LEU PHE ARG ALA HIS ILE ILE SER ASP GLN LYS VAL GLN
SEQRES 13 H 726 ASN LYS THR ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG
SEQRES 14 H 726 GLU ARG ASN GLY GLU ALA ILE ASP ARG SER LEU LEU ARG
SEQRES 15 H 726 SER LEU LEU SER MET LEU SER ASP LEU GLN ILE TYR GLN
SEQRES 16 H 726 ASP SER PHE GLU GLN ARG PHE LEU GLU GLU THR ASN ARG
SEQRES 17 H 726 LEU TYR ALA ALA GLU GLY GLN LYS LEU MET GLN GLU ARG
SEQRES 18 H 726 GLU VAL PRO GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU
SEQRES 19 H 726 GLU GLU GLU ALA ASP ARG LEU ILE THR TYR LEU ASP GLN
SEQRES 20 H 726 THR THR GLN LYS SER LEU ILE ALA THR VAL GLU LYS GLN
SEQRES 21 H 726 LEU LEU GLY GLU HIS LEU THR ALA ILE LEU GLN LYS GLY
SEQRES 22 H 726 LEU ASN ASN LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU
SEQRES 23 H 726 SER LEU LEU TYR GLN LEU PHE SER ARG VAL ARG GLY GLY
SEQRES 24 H 726 VAL GLN VAL LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS
SEQRES 25 H 726 ALA PHE GLY SER THR ILE VAL ILE ASN PRO GLU LYS ASP
SEQRES 26 H 726 LYS THR MET VAL GLN GLU LEU LEU ASP PHE LYS ASP LYS
SEQRES 27 H 726 VAL ASP HIS ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU
SEQRES 28 H 726 LYS PHE ILE ASN ALA MET LYS GLU ALA PHE GLU THR PHE
SEQRES 29 H 726 ILE ASN LYS ARG PRO ASN LYS PRO ALA GLU LEU ILE ALA
SEQRES 30 H 726 LYS TYR VAL ASP SER LYS LEU ARG ALA GLY ASN LYS GLU
SEQRES 31 H 726 ALA THR ASP GLU GLU LEU GLU LYS MET LEU ASP LYS ILE
SEQRES 32 H 726 MET ILE ILE PHE ARG PHE ILE TYR GLY LYS ASP VAL PHE
SEQRES 33 H 726 GLU ALA PHE TYR LYS LYS ASP LEU ALA LYS ARG LEU LEU
SEQRES 34 H 726 VAL GLY LYS SER ALA SER VAL ASP ALA GLU LYS SER MET
SEQRES 35 H 726 LEU SER LYS LEU LYS HIS GLU CYS GLY ALA ALA PHE THR
SEQRES 36 H 726 SER LYS LEU GLU GLY MET PHE LYS ASP MET GLU LEU SER
SEQRES 37 H 726 LYS ASP ILE MET ILE GLN PHE LYS GLN TYR MET GLN ASN
SEQRES 38 H 726 GLN ASN VAL PRO GLY ASN ILE GLU LEU THR VAL ASN ILE
SEQRES 39 H 726 LEU THR MET GLY TYR TRP PRO THR TYR VAL PRO MET GLU
SEQRES 40 H 726 VAL HIS LEU PRO PRO GLU MET VAL LYS LEU GLN GLU ILE
SEQRES 41 H 726 PHE LYS THR PHE TYR LEU GLY LYS HIS SER GLY ARG LYS
SEQRES 42 H 726 LEU GLN TRP GLN SER THR LEU GLY HIS CYS VAL LEU LYS
SEQRES 43 H 726 ALA GLU PHE LYS GLU GLY LYS LYS GLU LEU GLN VAL SER
SEQRES 44 H 726 LEU PHE GLN THR LEU VAL LEU LEU MET PHE ASN GLU GLY
SEQRES 45 H 726 GLU GLU PHE SER LEU GLU GLU ILE LYS GLN ALA THR GLY
SEQRES 46 H 726 ILE GLU ASP GLY GLU LEU ARG ARG THR LEU GLN SER LEU
SEQRES 47 H 726 ALA CYS GLY LYS ALA ARG VAL LEU ALA LYS ASN PRO LYS
SEQRES 48 H 726 GLY LYS ASP ILE GLU ASP GLY ASP LYS PHE ILE CYS ASN
SEQRES 49 H 726 ASP ASP PHE LYS HIS LYS LEU PHE ARG ILE LYS ILE ASN
SEQRES 50 H 726 GLN ILE GLN MET LYS GLU THR VAL GLU GLU GLN ALA SER
SEQRES 51 H 726 THR THR GLU ARG VAL PHE GLN ASP ARG GLN TYR GLN ILE
SEQRES 52 H 726 ASP ALA ALA ILE VAL ARG ILE MET LYS MET ARG LYS THR
SEQRES 53 H 726 LEU SER HIS ASN LEU LEU VAL SER GLU VAL TYR ASN GLN
SEQRES 54 H 726 LEU LYS PHE PRO VAL LYS PRO ALA ASP LEU LYS LYS ARG
SEQRES 55 H 726 ILE GLU SER LEU ILE ASP ARG ASP TYR MET GLU ARG ASP
SEQRES 56 H 726 LYS GLU ASN PRO ASN GLN TYR ASN TYR ILE ALA
SEQRES 1 I 98 MET GLY THR ASN SER GLY ALA GLY LYS LYS ARG PHE GLU
SEQRES 2 I 98 VAL LYS LYS TRP ASN ALA VAL ALA LEU TRP ALA TRP ASP
SEQRES 3 I 98 ILE VAL VAL ASP ASN CYS ALA ILE CYS ARG ASN HIS ILE
SEQRES 4 I 98 MET ASP LEU CYS ILE GLU CYS GLN ALA ASN GLN ALA SER
SEQRES 5 I 98 ALA THR SER GLU GLU CYS THR VAL ALA TRP GLY VAL CYS
SEQRES 6 I 98 ASN HIS ALA PHE HIS PHE HIS CYS ILE SER ARG TRP LEU
SEQRES 7 I 98 LYS THR ARG GLN VAL CYS PRO LEU ASP ASN ARG GLU TRP
SEQRES 8 I 98 GLU PHE GLN LYS TYR GLY HIS
SEQRES 1 R 12 DG DC DT DA DC DT 3DR DA DC DG DC DA
SEQRES 1 S 12 DT DG DC DG DT DA DA DG DT DA DG DC
SEQRES 1 T 12 DG DC DT DA DC DT 3DR DA DC DG DC DA
SEQRES 1 U 12 DT DG DC DG DT DA DA DG DT DA DG DC
HET 3DR R 9 11
HET 3DR T 9 11
HETNAM 3DR 1',2'-DIDEOXYRIBOFURANOSE-5'-PHOSPHATE
HETSYN 3DR ABASIC DIDEOXYRIBOSE
FORMUL 9 3DR 2(C5 H11 O6 P)
HELIX 1 1 PRO A 250 GLN A 255 1 6
HELIX 2 2 ALA A 381 GLY A 385 5 5
HELIX 3 3 GLU A 728 SER A 730 5 3
HELIX 4 4 THR A 985 GLN A 990 1 6
HELIX 5 5 SER A 1044 ILE A 1062 1 19
HELIX 6 6 GLU A 1069 ARG A 1074 1 6
HELIX 7 7 GLY A 1091 SER A 1096 1 6
HELIX 8 8 PHE A 1097 ILE A 1100 5 4
HELIX 9 9 SER A 1101 ALA A 1110 1 10
HELIX 10 10 THR A 1125 ARG A 1138 1 14
HELIX 11 11 SER B 104 LEU B 114 1 11
HELIX 12 12 ILE B 118 LYS B 135 1 18
HELIX 13 13 PRO C 250 GLN C 255 1 6
HELIX 14 14 ALA C 381 GLU C 384 5 4
HELIX 15 15 GLU C 728 SER C 730 5 3
HELIX 16 16 THR C 985 GLN C 990 1 6
HELIX 17 17 SER C 1044 ILE C 1062 1 19
HELIX 18 18 GLU C 1069 ARG C 1074 1 6
HELIX 19 19 GLY C 1091 SER C 1096 1 6
HELIX 20 20 PHE C 1097 ILE C 1100 5 4
HELIX 21 21 SER C 1101 ALA C 1110 1 10
HELIX 22 22 THR C 1125 ARG C 1138 1 14
HELIX 23 23 SER D 104 LEU D 114 1 11
HELIX 24 24 ILE D 118 LYS D 135 1 18
HELIX 25 25 GLU E 215 LYS E 219 5 5
HELIX 26 26 ALA E 223 GLN E 228 1 6
HELIX 27 27 GLU E 239 GLU E 245 1 7
HELIX 28 28 SER E 253 LYS E 269 1 17
HELIX 29 29 GLN E 271 ARG E 276 1 6
HELIX 30 30 ASP E 281 PHE E 307 1 27
HELIX 31 31 PHE E 307 THR E 313 1 7
HELIX 32 32 THR E 313 ASN E 318 1 6
HELIX 33 33 SER E 323 ARG E 333 1 11
HELIX 34 34 GLN E 340 ARG E 358 1 19
HELIX 35 35 SER E 366 LEU E 378 1 13
HELIX 36 36 ILE E 380 PHE E 385 1 6
HELIX 37 37 PHE E 385 LEU E 404 1 20
HELIX 38 38 GLU E 409 LEU E 428 1 20
HELIX 39 39 ILE E 429 TYR E 431 5 3
HELIX 40 40 GLN E 437 LEU E 449 1 13
HELIX 41 41 HIS E 452 GLY E 460 1 9
HELIX 42 42 GLY E 460 GLU E 467 1 8
HELIX 43 43 ARG E 469 SER E 481 1 13
HELIX 44 44 GLY E 485 VAL E 506 1 22
HELIX 45 45 ASN E 508 ASP E 512 5 5
HELIX 46 46 MET E 515 CYS E 533 1 19
HELIX 47 47 ASN E 537 ASN E 553 1 17
HELIX 48 48 ASN E 557 LYS E 570 1 14
HELIX 49 49 LEU E 583 ARG E 595 1 13
HELIX 50 50 GLY E 599 VAL E 617 1 19
HELIX 51 51 ASP E 624 LYS E 632 1 9
HELIX 52 52 ALA E 639 LYS E 644 1 6
HELIX 53 53 GLU E 646 ASN E 670 1 25
HELIX 54 54 GLU E 700 GLN E 705 1 6
HELIX 55 55 GLN E 705 LEU E 713 1 9
HELIX 56 56 LEU E 747 MET E 755 1 9
HELIX 57 57 PHE E 756 GLU E 758 5 3
HELIX 58 58 LEU E 764 GLY E 772 1 9
HELIX 59 59 GLU E 774 LEU E 782 1 9
HELIX 60 60 GLN E 825 LYS E 829 5 5
HELIX 61 61 THR E 831 ARG E 861 1 31
HELIX 62 62 LEU E 869 LEU E 877 1 9
HELIX 63 63 LYS E 882 ASP E 895 1 14
HELIX 64 64 GLU H 215 LYS H 219 5 5
HELIX 65 65 ALA H 223 ASN H 229 1 7
HELIX 66 66 GLU H 239 GLU H 245 1 7
HELIX 67 67 SER H 253 LYS H 269 1 17
HELIX 68 68 GLN H 271 ARG H 276 1 6
HELIX 69 69 ASP H 281 PHE H 307 1 27
HELIX 70 70 PHE H 307 THR H 313 1 7
HELIX 71 71 THR H 313 ASN H 318 1 6
HELIX 72 72 SER H 323 ILE H 336 1 14
HELIX 73 73 GLN H 340 ARG H 358 1 19
HELIX 74 74 ARG H 365 ASP H 377 1 13
HELIX 75 75 ILE H 380 PHE H 385 1 6
HELIX 76 76 PHE H 385 LEU H 404 1 20
HELIX 77 77 GLU H 409 LEU H 428 1 20
HELIX 78 78 THR H 436 LEU H 449 1 14
HELIX 79 79 HIS H 452 GLY H 460 1 9
HELIX 80 80 GLY H 460 ASN H 468 1 9
HELIX 81 81 ARG H 469 SER H 481 1 13
HELIX 82 82 GLY H 485 VAL H 506 1 22
HELIX 83 83 ASN H 508 ASP H 512 5 5
HELIX 84 84 MET H 515 CYS H 533 1 19
HELIX 85 85 ASN H 537 ASN H 553 1 17
HELIX 86 86 ASN H 557 LYS H 570 1 14
HELIX 87 87 LEU H 583 ARG H 595 1 13
HELIX 88 88 LYS H 600 VAL H 617 1 18
HELIX 89 89 ASP H 624 LYS H 632 1 9
HELIX 90 90 ALA H 639 LYS H 644 1 6
HELIX 91 91 GLU H 646 ASN H 670 1 25
HELIX 92 92 GLU H 700 GLN H 705 1 6
HELIX 93 93 GLN H 705 LEU H 713 1 9
HELIX 94 94 LEU H 747 MET H 755 1 9
HELIX 95 95 PHE H 756 GLU H 758 5 3
HELIX 96 96 LEU H 764 GLY H 772 1 9
HELIX 97 97 GLU H 774 LEU H 782 1 9
HELIX 98 98 GLN H 825 LYS H 829 5 5
HELIX 99 99 THR H 831 ARG H 861 1 31
HELIX 100 100 LEU H 869 LEU H 877 1 9
HELIX 101 101 LYS H 882 ASP H 895 1 14
SHEET 1 AA 5 VAL A1004 HIS A1009 0
SHEET 2 AA 5 GLN A1025 THR A1032 -1 O LEU A1029 N CYS A1008
SHEET 3 AA 5 ILE A1037 SER A1042 -1 O GLY A1038 N PHE A1030
SHEET 4 AA 5 ASN A 4 GLN A 10 -1 O TYR A 5 N THR A1041
SHEET 5 AA 5 PHE A1088 ASP A1090 1 O ILE A1089 N VAL A 6
SHEET 1 AB 4 GLY A 17 GLY A 21 0
SHEET 2 AB 4 ASN A 30 LYS A 35 -1 O ASN A 30 N GLY A 21
SHEET 3 AB 4 ARG A 38 THR A 45 -1 O ARG A 38 N LYS A 35
SHEET 4 AB 4 GLY A 48 GLY A 56 -1 O GLY A 48 N THR A 45
SHEET 1 AC 4 ILE A 61 PHE A 67 0
SHEET 2 AC 4 LEU A 76 THR A 81 -1 O LEU A 76 N PHE A 67
SHEET 3 AC 4 ASN A 85 SER A 94 -1 O ASN A 85 N THR A 81
SHEET 4 AC 4 SER A 97 ASN A 107 -1 O SER A 97 N SER A 94
SHEET 1 AD 4 ILE A 121 ILE A 124 0
SHEET 2 AD 4 MET A 130 ARG A 134 -1 O GLY A 132 N ILE A 123
SHEET 3 AD 4 LEU A 139 PRO A 144 -1 O LYS A 141 N LEU A 133
SHEET 4 AD 4 PHE A 155 ARG A 158 -1 O PHE A 155 N VAL A 142
SHEET 1 AE 4 VAL A 164 PHE A 169 0
SHEET 2 AE 4 THR A 177 ASP A 184 -1 O CYS A 179 N LYS A 168
SHEET 3 AE 4 GLY A 187 SER A 196 -1 O GLY A 187 N ASP A 184
SHEET 4 AE 4 GLU A 201 LYS A 204 1 O GLU A 201 N SER A 196
SHEET 1 AF 4 VAL A 164 PHE A 169 0
SHEET 2 AF 4 THR A 177 ASP A 184 -1 O CYS A 179 N LYS A 168
SHEET 3 AF 4 GLY A 187 SER A 196 -1 O GLY A 187 N ASP A 184
SHEET 4 AF 4 GLU A 210 VAL A 212 -1 O GLU A 210 N VAL A 190
SHEET 1 AG 2 GLU A 201 LYS A 204 0
SHEET 2 AG 2 GLY A 187 SER A 196 1 O GLU A 194 N ASN A 203
SHEET 1 AH 4 MET A 218 ALA A 221 0
SHEET 2 AH 4 ALA A 229 ILE A 232 -1 O ILE A 230 N ILE A 220
SHEET 3 AH 4 ILE A 237 ASN A 241 -1 O THR A 238 N ILE A 231
SHEET 4 AH 4 LYS A 244 ILE A 248 -1 O LYS A 244 N ASN A 241
SHEET 1 AI 4 ILE A 258 ARG A 263 0
SHEET 2 AI 4 ARG A 270 ASP A 275 -1 O LEU A 272 N ASN A 262
SHEET 3 AI 4 ARG A 279 GLU A 288 -1 O ARG A 279 N ASP A 275
SHEET 4 AI 4 THR A 296 GLU A 307 -1 O THR A 296 N GLU A 288
SHEET 1 AJ 4 CYS A 313 ASP A 318 0
SHEET 2 AJ 4 VAL A 321 GLY A 325 -1 O VAL A 321 N LEU A 317
SHEET 3 AJ 4 SER A 331 LEU A 336 -1 O GLN A 332 N VAL A 324
SHEET 4 AJ 4 VAL A 347 PHE A 353 -1 O VAL A 348 N LYS A 335
SHEET 1 AK 2 ILE A 359 VAL A 365 0
SHEET 2 AK 2 GLN A 374 SER A 379 -1 O GLN A 374 N VAL A 365
SHEET 1 AL 4 ALA A 400 SER A 401 0
SHEET 2 AL 4 LEU A 699 GLY A 702 -1 O ILE A 701 N ALA A 400
SHEET 3 AL 4 SER A 690 ALA A 694 -1 O LEU A 691 N GLY A 702
SHEET 4 AL 4 TYR A 678 LEU A 682 -1 O TYR A 678 N ALA A 694
SHEET 1 AM 4 LEU A 410 LEU A 413 0
SHEET 2 AM 4 THR A 424 LEU A 427 -1 O THR A 424 N LEU A 413
SHEET 3 AM 4 VAL A 435 ASN A 439 -1 O LEU A 436 N LEU A 425
SHEET 4 AM 4 GLU A 442 GLU A 445 -1 O GLU A 442 N ASN A 439
SHEET 1 AN 4 THR A 457 VAL A 463 0
SHEET 2 AN 4 GLN A 467 THR A 472 -1 O GLN A 467 N VAL A 463
SHEET 3 AN 4 VAL A 476 SER A 480 -1 O ARG A 477 N GLN A 470
SHEET 4 AN 4 LEU A 486 SER A 488 -1 N VAL A 487 O LEU A 478
SHEET 1 AO 4 VAL A 500 ALA A 501 0
SHEET 2 AO 4 GLN A 507 VAL A 512 -1 N ALA A 511 O VAL A 500
SHEET 3 AO 4 ALA A 515 HIS A 522 -1 O ALA A 515 N VAL A 512
SHEET 4 AO 4 GLU A 525 GLU A 533 -1 O GLU A 525 N HIS A 522
SHEET 1 AP 4 VAL A 538 ASP A 542 0
SHEET 2 AP 4 LEU A 555 LEU A 560 -1 O ALA A 557 N ASP A 542
SHEET 3 AP 4 ILE A 568 LYS A 570 -1 O LEU A 569 N CYS A 556
SHEET 4 AP 4 GLU A 575 HIS A 578 -1 O GLU A 575 N LYS A 570
SHEET 1 AQ 2 PRO A 588 SER A 590 0
SHEET 2 AQ 2 ALA A 605 LEU A 606 -1 O ALA A 605 N ARG A 589
SHEET 1 AR 4 MET A 593 THR A 595 0
SHEET 2 AR 4 HIS A 600 LEU A 603 -1 O TYR A 601 N THR A 594
SHEET 3 AR 4 ALA A 610 PHE A 614 -1 O PHE A 614 N LEU A 602
SHEET 4 AR 4 LYS A 627 THR A 630 -1 O LYS A 627 N TYR A 613
SHEET 1 AS 2 PHE A 641 ARG A 642 0
SHEET 2 AS 2 THR A 647 ASN A 648 -1 O ASN A 648 N PHE A 641
SHEET 1 AT 2 TYR A 660 SER A 661 0
SHEET 2 AT 2 LEU A 666 VAL A 667 -1 O VAL A 667 N TYR A 660
SHEET 1 AU 2 SER A 720 GLN A 727 0
SHEET 2 AU 2 CYS A 732 GLN A 743 -1 O CYS A 732 N GLN A 727
SHEET 1 AV 2 THR A 749 ALA A 751 0
SHEET 2 AV 2 CYS A 732 GLN A 743 1 O VAL A 742 N THR A 750
SHEET 1 AW 5 SER A 762 VAL A 765 0
SHEET 2 AW 5 VAL A 801 GLN A 806 1 O LEU A 802 N SER A 762
SHEET 3 AW 5 GLU A 785 ASP A 795 -1 O LEU A 791 N HIS A 805
SHEET 4 AW 5 CYS A 732 GLN A 743 -1 O PHE A 733 N ILE A 794
SHEET 5 AW 5 THR A 749 ALA A 751 1 O THR A 750 N VAL A 742
SHEET 1 AX 5 SER A 762 VAL A 765 0
SHEET 2 AX 5 VAL A 801 GLN A 806 1 O LEU A 802 N SER A 762
SHEET 3 AX 5 GLU A 785 ASP A 795 -1 O LEU A 791 N HIS A 805
SHEET 4 AX 5 CYS A 732 GLN A 743 -1 O PHE A 733 N ILE A 794
SHEET 5 AX 5 SER A 720 GLN A 727 -1 O SER A 720 N SER A 738
SHEET 1 AY 4 GLU A 811 CYS A 819 0
SHEET 2 AY 4 TYR A 828 MET A 835 -1 O TYR A 828 N CYS A 819
SHEET 3 AY 4 GLY A 846 TYR A 853 -1 O ARG A 847 N THR A 833
SHEET 4 AY 4 LEU A 858 VAL A 866 -1 O GLN A 859 N GLN A 852
SHEET 1 AZ 4 VAL A 870 PHE A 876 0
SHEET 2 AZ 4 LYS A 879 ILE A 884 -1 O LYS A 879 N PHE A 876
SHEET 3 AZ 4 THR A 887 TRP A 893 -1 O THR A 887 N ILE A 884
SHEET 4 AZ 4 LEU A 899 HIS A 905 -1 O ARG A 900 N GLU A 892
SHEET 1 A0 4 ALA A 911 LYS A 917 0
SHEET 2 A0 4 PHE A 920 ASP A 925 -1 O PHE A 920 N LYS A 917
SHEET 3 A0 4 VAL A 930 LYS A 936 -1 O LEU A 931 N VAL A 923
SHEET 4 A0 4 ASN A 941 ARG A 947 -1 O ASN A 941 N LYS A 936
SHEET 1 A1 4 MET A 954 ILE A 959 0
SHEET 2 A1 4 ASN A 964 GLU A 969 -1 O LEU A 966 N GLU A 958
SHEET 3 A1 4 ASN A 973 LYS A 979 -1 O ASN A 973 N GLU A 969
SHEET 4 A1 4 LEU A 992 HIS A 999 -1 O GLN A 993 N GLN A 978
SHEET 1 A2 2 PHE A1076 HIS A1077 0
SHEET 2 A2 2 THR A1082 GLU A1083 -1 O GLU A1083 N PHE A1076
SHEET 1 BA 4 LYS B 138 ALA B 143 0
SHEET 2 BA 4 ASN B 448 ASN B 453 -1 O ILE B 449 N ALA B 143
SHEET 3 BA 4 LEU B 441 MET B 445 -1 O LEU B 441 N TRP B 452
SHEET 4 BA 4 ILE B 429 PHE B 434 -1 N SER B 430 O GLY B 444
SHEET 1 BB 4 VAL B 150 TRP B 155 0
SHEET 2 BB 4 THR B 162 SER B 167 -1 O ALA B 164 N GLU B 154
SHEET 3 BB 4 ILE B 172 ASP B 176 -1 O ILE B 173 N VAL B 165
SHEET 4 BB 4 THR B 183 ILE B 186 -1 O SER B 184 N LEU B 174
SHEET 1 BC 4 ILE B 195 PHE B 200 0
SHEET 2 BC 4 GLN B 207 SER B 212 -1 O PHE B 209 N LYS B 199
SHEET 3 BC 4 ALA B 216 ASP B 221 -1 O ALA B 216 N SER B 212
SHEET 4 BC 4 VAL B 226 VAL B 229 -1 N ILE B 227 O LEU B 219
SHEET 1 BD 4 TYR B 240 SER B 246 0
SHEET 2 BD 4 MET B 251 ASP B 256 -1 O MET B 251 N SER B 246
SHEET 3 BD 4 ARG B 260 GLY B 265 -1 O ARG B 260 N ASP B 256
SHEET 4 BD 4 GLU B 270 LYS B 275 -1 N ILE B 271 O LEU B 263
SHEET 1 BE 4 VAL B 281 ASN B 287 0
SHEET 2 BE 4 CYS B 290 SER B 298 -1 N CYS B 290 O ASN B 287
SHEET 3 BE 4 THR B 302 ASP B 307 -1 O THR B 302 N SER B 298
SHEET 4 BE 4 ALA B 319 PRO B 322 -1 O ALA B 319 N LEU B 305
SHEET 1 BF 4 VAL B 327 PHE B 332 0
SHEET 2 BF 4 LYS B 339 ASP B 344 -1 O LEU B 341 N TYR B 331
SHEET 3 BF 4 GLU B 348 SER B 353 -1 O GLU B 348 N ASP B 344
SHEET 4 BF 4 GLN B 362 ILE B 365 -1 O GLN B 362 N VAL B 351
SHEET 1 BG 4 THR B 380 TRP B 381 0
SHEET 2 BG 4 LEU B 387 GLY B 391 -1 O VAL B 389 N THR B 380
SHEET 3 BG 4 ILE B 406 ASP B 410 -1 O ASP B 407 N ALA B 390
SHEET 4 BG 4 LEU B 416 LEU B 420 -1 N VAL B 417 O ILE B 408
SHEET 1 CA 5 VAL C1004 HIS C1009 0
SHEET 2 CA 5 GLN C1025 THR C1032 -1 O LEU C1029 N CYS C1008
SHEET 3 CA 5 ILE C1037 SER C1042 -1 O GLY C1038 N PHE C1030
SHEET 4 CA 5 ASN C 4 GLN C 10 -1 O TYR C 5 N THR C1041
SHEET 5 CA 5 PHE C1088 ASP C1090 1 O ILE C1089 N VAL C 6
SHEET 1 CB 4 GLY C 17 GLY C 21 0
SHEET 2 CB 4 ASN C 30 LYS C 35 -1 O ASN C 30 N GLY C 21
SHEET 3 CB 4 ARG C 38 THR C 45 -1 O ARG C 38 N LYS C 35
SHEET 4 CB 4 GLY C 48 GLY C 56 -1 O GLY C 48 N THR C 45
SHEET 1 CC 4 ILE C 61 PHE C 67 0
SHEET 2 CC 4 LEU C 76 THR C 81 -1 O LEU C 76 N PHE C 67
SHEET 3 CC 4 ASN C 85 SER C 94 -1 O ASN C 85 N THR C 81
SHEET 4 CC 4 SER C 97 ASN C 107 -1 O SER C 97 N SER C 94
SHEET 1 CD 4 ILE C 121 ILE C 124 0
SHEET 2 CD 4 MET C 130 ARG C 134 -1 O GLY C 132 N ILE C 123
SHEET 3 CD 4 LEU C 139 PRO C 144 -1 O LYS C 141 N LEU C 133
SHEET 4 CD 4 PHE C 155 ARG C 158 -1 O PHE C 155 N VAL C 142
SHEET 1 CE 4 VAL C 164 PHE C 169 0
SHEET 2 CE 4 THR C 177 ASP C 184 -1 O CYS C 179 N LYS C 168
SHEET 3 CE 4 GLY C 187 SER C 196 -1 O GLY C 187 N ASP C 184
SHEET 4 CE 4 GLU C 201 LYS C 204 1 O GLU C 201 N SER C 196
SHEET 1 CF 4 VAL C 164 PHE C 169 0
SHEET 2 CF 4 THR C 177 ASP C 184 -1 O CYS C 179 N LYS C 168
SHEET 3 CF 4 GLY C 187 SER C 196 -1 O GLY C 187 N ASP C 184
SHEET 4 CF 4 GLU C 210 VAL C 212 -1 O GLU C 210 N VAL C 190
SHEET 1 CG 2 GLU C 201 LYS C 204 0
SHEET 2 CG 2 GLY C 187 SER C 196 1 O GLU C 194 N ASN C 203
SHEET 1 CH 4 MET C 218 ALA C 221 0
SHEET 2 CH 4 ALA C 229 ILE C 232 -1 O ILE C 230 N ILE C 220
SHEET 3 CH 4 ILE C 237 ASN C 241 -1 O THR C 238 N ILE C 231
SHEET 4 CH 4 LYS C 244 ILE C 248 -1 O LYS C 244 N ASN C 241
SHEET 1 CI 4 ILE C 258 ARG C 263 0
SHEET 2 CI 4 ARG C 270 ASP C 275 -1 O LEU C 272 N ASN C 262
SHEET 3 CI 4 ARG C 279 GLU C 288 -1 O ARG C 279 N ASP C 275
SHEET 4 CI 4 THR C 296 GLU C 307 -1 O THR C 296 N GLU C 288
SHEET 1 CJ 4 CYS C 313 ASP C 318 0
SHEET 2 CJ 4 VAL C 321 GLY C 325 -1 O VAL C 321 N LEU C 317
SHEET 3 CJ 4 SER C 331 LEU C 336 -1 O GLN C 332 N VAL C 324
SHEET 4 CJ 4 VAL C 347 PHE C 353 -1 O VAL C 348 N LYS C 335
SHEET 1 CK 4 ILE C 359 VAL C 365 0
SHEET 2 CK 4 GLN C 374 SER C 379 -1 O GLN C 374 N VAL C 365
SHEET 3 CK 4 SER C 386 GLY C 393 -1 O SER C 386 N SER C 379
SHEET 4 CK 4 LYS C 709 PRO C 716 -1 O LYS C 709 N GLY C 393
SHEET 1 CL 4 ILE C 396 SER C 401 0
SHEET 2 CL 4 LEU C 699 ILE C 704 -1 O ILE C 701 N ALA C 400
SHEET 3 CL 4 SER C 690 ALA C 694 -1 O LEU C 691 N GLY C 702
SHEET 4 CL 4 TYR C 678 LEU C 682 -1 O TYR C 678 N ALA C 694
SHEET 1 CM 4 LEU C 410 LEU C 413 0
SHEET 2 CM 4 THR C 424 LEU C 427 -1 O THR C 424 N LEU C 413
SHEET 3 CM 4 VAL C 435 ASN C 439 -1 O LEU C 436 N LEU C 425
SHEET 4 CM 4 GLU C 442 GLU C 445 -1 O GLU C 442 N ASN C 439
SHEET 1 CN 4 THR C 457 VAL C 463 0
SHEET 2 CN 4 GLN C 467 THR C 472 -1 O GLN C 467 N VAL C 463
SHEET 3 CN 4 VAL C 476 SER C 480 -1 O ARG C 477 N GLN C 470
SHEET 4 CN 4 LEU C 486 SER C 488 -1 N VAL C 487 O LEU C 478
SHEET 1 CO 4 VAL C 500 ALA C 501 0
SHEET 2 CO 4 GLN C 507 VAL C 512 -1 N ALA C 511 O VAL C 500
SHEET 3 CO 4 ALA C 515 HIS C 522 -1 O ALA C 515 N VAL C 512
SHEET 4 CO 4 GLU C 525 GLU C 533 -1 O GLU C 525 N HIS C 522
SHEET 1 CP 4 VAL C 538 ASP C 542 0
SHEET 2 CP 4 LEU C 555 LEU C 560 -1 O ALA C 557 N ASP C 542
SHEET 3 CP 4 ILE C 568 LYS C 570 -1 O LEU C 569 N CYS C 556
SHEET 4 CP 4 GLU C 575 HIS C 578 -1 O GLU C 575 N LYS C 570
SHEET 1 CQ 2 PRO C 588 SER C 590 0
SHEET 2 CQ 2 ALA C 605 LEU C 606 -1 O ALA C 605 N ARG C 589
SHEET 1 CR 4 MET C 593 THR C 595 0
SHEET 2 CR 4 HIS C 600 LEU C 603 -1 O TYR C 601 N THR C 594
SHEET 3 CR 4 ALA C 610 PHE C 614 -1 O PHE C 614 N LEU C 602
SHEET 4 CR 4 LYS C 627 THR C 630 -1 O LYS C 627 N TYR C 613
SHEET 1 CS 2 PHE C 641 ARG C 642 0
SHEET 2 CS 2 THR C 647 ASN C 648 -1 O ASN C 648 N PHE C 641
SHEET 1 CT 2 TYR C 660 SER C 661 0
SHEET 2 CT 2 LEU C 666 VAL C 667 -1 O VAL C 667 N TYR C 660
SHEET 1 CU 2 SER C 720 GLN C 727 0
SHEET 2 CU 2 CYS C 732 GLN C 743 -1 O CYS C 732 N GLN C 727
SHEET 1 CV 2 THR C 749 ALA C 751 0
SHEET 2 CV 2 CYS C 732 GLN C 743 1 O VAL C 742 N THR C 750
SHEET 1 CW 5 SER C 762 VAL C 765 0
SHEET 2 CW 5 VAL C 801 GLN C 806 1 O LEU C 802 N SER C 762
SHEET 3 CW 5 GLU C 785 ASP C 795 -1 O LEU C 791 N HIS C 805
SHEET 4 CW 5 CYS C 732 GLN C 743 -1 O PHE C 733 N ILE C 794
SHEET 5 CW 5 THR C 749 ALA C 751 1 O THR C 750 N VAL C 742
SHEET 1 CX 5 SER C 762 VAL C 765 0
SHEET 2 CX 5 VAL C 801 GLN C 806 1 O LEU C 802 N SER C 762
SHEET 3 CX 5 GLU C 785 ASP C 795 -1 O LEU C 791 N HIS C 805
SHEET 4 CX 5 CYS C 732 GLN C 743 -1 O PHE C 733 N ILE C 794
SHEET 5 CX 5 SER C 720 GLN C 727 -1 O SER C 720 N SER C 738
SHEET 1 CY 4 GLU C 811 CYS C 819 0
SHEET 2 CY 4 TYR C 828 MET C 835 -1 O TYR C 828 N CYS C 819
SHEET 3 CY 4 GLY C 846 TYR C 853 -1 O ARG C 847 N THR C 833
SHEET 4 CY 4 LEU C 858 VAL C 866 -1 O GLN C 859 N GLN C 852
SHEET 1 CZ 4 VAL C 870 PHE C 876 0
SHEET 2 CZ 4 LYS C 879 ILE C 884 -1 O LYS C 879 N PHE C 876
SHEET 3 CZ 4 THR C 887 TRP C 893 -1 O THR C 887 N ILE C 884
SHEET 4 CZ 4 LEU C 899 HIS C 905 -1 O ARG C 900 N GLU C 892
SHEET 1 C0 4 ALA C 911 LYS C 917 0
SHEET 2 C0 4 PHE C 920 ASP C 925 -1 O PHE C 920 N LYS C 917
SHEET 3 C0 4 VAL C 930 LYS C 936 -1 O LEU C 931 N VAL C 923
SHEET 4 C0 4 ASN C 941 ARG C 947 -1 O ASN C 941 N LYS C 936
SHEET 1 C1 4 MET C 954 ILE C 959 0
SHEET 2 C1 4 ASN C 964 GLU C 969 -1 O LEU C 966 N GLU C 958
SHEET 3 C1 4 ASN C 973 LYS C 979 -1 O ASN C 973 N GLU C 969
SHEET 4 C1 4 LEU C 992 HIS C 999 -1 O GLN C 993 N GLN C 978
SHEET 1 C2 2 PHE C1076 HIS C1077 0
SHEET 2 C2 2 THR C1082 GLU C1083 -1 O GLU C1083 N PHE C1076
SHEET 1 DA 4 LYS D 138 ALA D 143 0
SHEET 2 DA 4 ASN D 448 ASN D 453 -1 O ILE D 449 N ALA D 143
SHEET 3 DA 4 LEU D 441 MET D 445 -1 O LEU D 441 N TRP D 452
SHEET 4 DA 4 ILE D 429 PHE D 434 -1 N SER D 430 O GLY D 444
SHEET 1 DB 4 VAL D 150 TRP D 155 0
SHEET 2 DB 4 THR D 162 SER D 167 -1 O ALA D 164 N GLU D 154
SHEET 3 DB 4 ILE D 172 ASP D 176 -1 O ILE D 173 N VAL D 165
SHEET 4 DB 4 THR D 183 ILE D 186 -1 O SER D 184 N LEU D 174
SHEET 1 DC 4 ILE D 195 PHE D 200 0
SHEET 2 DC 4 GLN D 207 SER D 212 -1 O PHE D 209 N LYS D 199
SHEET 3 DC 4 ALA D 216 ASP D 221 -1 O ALA D 216 N SER D 212
SHEET 4 DC 4 VAL D 226 VAL D 229 -1 N ILE D 227 O LEU D 219
SHEET 1 DD 4 TYR D 240 SER D 246 0
SHEET 2 DD 4 MET D 251 ASP D 256 -1 O MET D 251 N SER D 246
SHEET 3 DD 4 ARG D 260 GLY D 265 -1 O ARG D 260 N ASP D 256
SHEET 4 DD 4 GLU D 270 LYS D 275 -1 N ILE D 271 O LEU D 263
SHEET 1 DE 4 VAL D 281 ASN D 287 0
SHEET 2 DE 4 CYS D 290 SER D 298 -1 N CYS D 290 O ASN D 287
SHEET 3 DE 4 THR D 302 ASP D 307 -1 O THR D 302 N SER D 298
SHEET 4 DE 4 ALA D 319 PRO D 322 -1 O ALA D 319 N LEU D 305
SHEET 1 DF 4 VAL D 327 PHE D 332 0
SHEET 2 DF 4 LYS D 339 ASP D 344 -1 O LEU D 341 N TYR D 331
SHEET 3 DF 4 GLU D 348 SER D 353 -1 O GLU D 348 N ASP D 344
SHEET 4 DF 4 GLN D 362 ILE D 365 -1 O GLN D 362 N VAL D 351
SHEET 1 DG 4 THR D 380 TRP D 381 0
SHEET 2 DG 4 LEU D 387 GLY D 391 -1 O VAL D 389 N THR D 380
SHEET 3 DG 4 ILE D 406 ASP D 410 -1 O ASP D 407 N ALA D 390
SHEET 4 DG 4 LEU D 416 LEU D 420 -1 N VAL D 417 O ILE D 408
SHEET 1 EA 2 GLU E 676 LEU E 677 0
SHEET 2 EA 2 LYS F 26 TRP F 33 -1 N TRP F 27 O GLU E 676
SHEET 1 EB 2 ASN E 680 THR E 683 0
SHEET 2 EB 2 LYS F 26 TRP F 33 1 O ALA F 29 N ASN E 680
SHEET 1 EC 4 ILE E 821 LYS E 822 0
SHEET 2 EC 4 GLU E 742 SER E 746 1 O GLU E 742 N ILE E 821
SHEET 3 EC 4 LEU E 721 ALA E 734 -1 O CYS E 730 N VAL E 745
SHEET 4 EC 4 PHE F 22 VAL F 24 1 O GLU F 23 N LYS E 733
SHEET 1 ED 5 ILE E 821 LYS E 822 0
SHEET 2 ED 5 GLU E 742 SER E 746 1 O GLU E 742 N ILE E 821
SHEET 3 ED 5 LEU E 721 ALA E 734 -1 O CYS E 730 N VAL E 745
SHEET 4 ED 5 LYS F 26 TRP F 33 -1 N LYS F 26 O VAL E 731
SHEET 5 ED 5 ASN E 680 THR E 683 1 O ASN E 680 N ALA F 31
SHEET 1 FA 2 PHE F 22 VAL F 24 0
SHEET 2 FA 2 LEU E 721 ALA E 734 1 O LYS E 733 N GLU F 23
SHEET 1 EE 5 ILE E 821 LYS E 822 0
SHEET 2 EE 5 GLU E 742 SER E 746 1 O GLU E 742 N ILE E 821
SHEET 3 EE 5 LEU E 721 ALA E 734 -1 O CYS E 730 N VAL E 745
SHEET 4 EE 5 LYS F 26 TRP F 33 -1 N LYS F 26 O VAL E 731
SHEET 5 EE 5 GLU E 676 LEU E 677 -1 O GLU E 676 N TRP F 27
SHEET 1 EF 3 PHE E 762 SER E 763 0
SHEET 2 EF 3 LYS E 807 CYS E 810 -1 O PHE E 808 N PHE E 762
SHEET 3 EF 3 LEU E 793 LYS E 795 -1 O ALA E 794 N ILE E 809
SHEET 1 EG 3 THR E 863 SER E 865 0
SHEET 2 EG 3 GLN E 908 ASN E 910 -1 O TYR E 909 N LEU E 864
SHEET 3 EG 3 GLU E 900 ARG E 901 -1 O GLU E 900 N ASN E 910
SHEET 1 HA 2 GLU H 676 LEU H 677 0
SHEET 2 HA 2 LYS I 26 TRP I 35 -1 N TRP I 27 O GLU H 676
SHEET 1 HB 2 ASN H 680 THR H 683 0
SHEET 2 HB 2 LYS I 26 TRP I 35 1 O ALA I 29 N ASN H 680
SHEET 1 HC 4 ILE H 821 LYS H 822 0
SHEET 2 HC 4 GLU H 742 SER H 746 1 O GLU H 742 N ILE H 821
SHEET 3 HC 4 ARG H 719 ALA H 734 -1 O CYS H 730 N VAL H 745
SHEET 4 HC 4 PHE I 22 VAL I 24 1 O GLU I 23 N LYS H 733
SHEET 1 HD 5 ILE H 821 LYS H 822 0
SHEET 2 HD 5 GLU H 742 SER H 746 1 O GLU H 742 N ILE H 821
SHEET 3 HD 5 ARG H 719 ALA H 734 -1 O CYS H 730 N VAL H 745
SHEET 4 HD 5 LYS I 26 TRP I 35 -1 N LYS I 26 O VAL H 731
SHEET 5 HD 5 ASN H 680 THR H 683 1 O ASN H 680 N ALA I 31
SHEET 1 IA 2 PHE I 22 VAL I 24 0
SHEET 2 IA 2 ARG H 719 ALA H 734 1 O LYS H 733 N GLU I 23
SHEET 1 HE 5 ILE H 821 LYS H 822 0
SHEET 2 HE 5 GLU H 742 SER H 746 1 O GLU H 742 N ILE H 821
SHEET 3 HE 5 ARG H 719 ALA H 734 -1 O CYS H 730 N VAL H 745
SHEET 4 HE 5 LYS I 26 TRP I 35 -1 N LYS I 26 O VAL H 731
SHEET 5 HE 5 GLU H 676 LEU H 677 -1 O GLU H 676 N TRP I 27
SHEET 1 HF 3 PHE H 762 SER H 763 0
SHEET 2 HF 3 LYS H 807 CYS H 810 -1 O PHE H 808 N PHE H 762
SHEET 3 HF 3 LEU H 793 LYS H 795 -1 O ALA H 794 N ILE H 809
SHEET 1 HG 3 THR H 863 SER H 865 0
SHEET 2 HG 3 GLN H 908 ASN H 910 -1 O TYR H 909 N LEU H 864
SHEET 3 HG 3 GLU H 900 ARG H 901 -1 O GLU H 900 N ASN H 910
LINK O3' DT R 8 P 3DR R 9 1555 1555 1.60
LINK O3' 3DR R 9 P DA R 10 1555 1555 1.61
LINK O3' DT T 8 P 3DR T 9 1555 1555 1.60
LINK O3' 3DR T 9 P DA T 10 1555 1555 1.61
CISPEP 1 GLU A 224 PRO A 225 0 11.76
CISPEP 2 GLY A 357 PRO A 358 0 -5.20
CISPEP 3 GLU C 224 PRO C 225 0 11.89
CISPEP 4 GLY C 357 PRO C 358 0 -5.26
CRYST1 130.800 155.840 255.390 90.00 94.17 90.00 P 1 21 1 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 0.007645 0.000000 0.000557 0.00000
SCALE2 0.000000 0.006417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
