HEADER TRANSFERASE 05-JUL-13 4LJZ
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE E.COLI HOLOENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B, G, H;
COMPND 4 SYNONYM: RNAP SUBUNIT ALPHA, RNA POLYMERASE SUBUNIT ALPHA,
COMPND 5 TRANSCRIPTASE SUBUNIT ALPHA;
COMPND 6 EC: 2.7.7.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA;
COMPND 10 CHAIN: C, I;
COMPND 11 SYNONYM: RNAP SUBUNIT BETA, RNA POLYMERASE SUBUNIT BETA,
COMPND 12 TRANSCRIPTASE SUBUNIT BETA;
COMPND 13 EC: 2.7.7.6;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA';
COMPND 17 CHAIN: D, J;
COMPND 18 EC: 2.7.7.6;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: DNA-DIRECTED RNA POLYMERASE SUBUNIT OMEGA;
COMPND 22 CHAIN: E, K;
COMPND 23 SYNONYM: RNAP OMEGA SUBUNIT, RNA POLYMERASE OMEGA SUBUNIT,
COMPND 24 TRANSCRIPTASE SUBUNIT OMEGA;
COMPND 25 EC: 2.7.7.6;
COMPND 26 ENGINEERED: YES;
COMPND 27 MOL_ID: 5;
COMPND 28 MOLECULE: RNA POLYMERASE SIGMA FACTOR RPOD;
COMPND 29 CHAIN: F, L;
COMPND 30 SYNONYM: SIGMA-70;
COMPND 31 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 536056;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: RPOA, ECDH1_0418, ECDH1ME8569_3173;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 10 ORGANISM_TAXID: 536056;
SOURCE 11 STRAIN: K12;
SOURCE 12 GENE: RPOB, ECDH1_4008, ECDH1ME8569_3846;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI BW2952;
SOURCE 17 ORGANISM_TAXID: 595496;
SOURCE 18 STRAIN: K12;
SOURCE 19 GENE: RPOC, BWG_3647;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 24 ORGANISM_TAXID: 536056;
SOURCE 25 STRAIN: K12;
SOURCE 26 GENE: RPOZ, ECDH1_0056, ECDH1ME8569_3534;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 29 MOL_ID: 5;
SOURCE 30 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 31 ORGANISM_TAXID: 83333;
SOURCE 32 STRAIN: K12;
SOURCE 33 GENE: RPOD, ALT, B3067, JW3039;
SOURCE 34 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 35 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA DIRECTED RNA POLYMERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BAE,S.A.DARST
REVDAT 4 28-FEB-24 4LJZ 1 REMARK SEQADV LINK
REVDAT 3 18-DEC-13 4LJZ 1 JRNL
REVDAT 2 04-DEC-13 4LJZ 1 JRNL
REVDAT 1 13-NOV-13 4LJZ 0
JRNL AUTH B.BAE,E.DAVIS,D.BROWN,E.A.CAMPBELL,S.WIGNESHWERARAJ,
JRNL AUTH 2 S.A.DARST
JRNL TITL PHAGE T7 GP2 INHIBITION OF ESCHERICHIA COLI RNA POLYMERASE
JRNL TITL 2 INVOLVES MISAPPROPRIATION OF SIGMA 70 DOMAIN 1.1.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 19772 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 24218560
JRNL DOI 10.1073/PNAS.1314576110
REMARK 2
REMARK 2 RESOLUTION. 3.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 3.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 138592
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6970
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 29.8849 - 10.9655 0.99 4639 251 0.2276 0.2302
REMARK 3 2 10.9655 - 8.7762 1.00 4535 247 0.1774 0.1852
REMARK 3 3 8.7762 - 7.6884 1.00 4487 237 0.2045 0.2219
REMARK 3 4 7.6884 - 6.9953 1.00 4491 242 0.2209 0.2563
REMARK 3 5 6.9953 - 6.4994 1.00 4466 221 0.2422 0.2887
REMARK 3 6 6.4994 - 6.1197 1.00 4471 212 0.2416 0.3124
REMARK 3 7 6.1197 - 5.8156 1.00 4431 243 0.2519 0.3068
REMARK 3 8 5.8156 - 5.5641 1.00 4437 229 0.2463 0.2997
REMARK 3 9 5.5641 - 5.3512 1.00 4453 208 0.2438 0.3149
REMARK 3 10 5.3512 - 5.1675 1.00 4385 235 0.2454 0.3034
REMARK 3 11 5.1675 - 5.0067 1.00 4434 241 0.2436 0.2710
REMARK 3 12 5.0067 - 4.8642 1.00 4438 225 0.2510 0.3118
REMARK 3 13 4.8642 - 4.7366 1.00 4373 227 0.2445 0.3064
REMARK 3 14 4.7366 - 4.6215 0.99 4359 246 0.2469 0.3033
REMARK 3 15 4.6215 - 4.5168 0.99 4404 219 0.2477 0.3291
REMARK 3 16 4.5168 - 4.4210 1.00 4369 223 0.2544 0.3200
REMARK 3 17 4.4210 - 4.3328 1.00 4385 251 0.2619 0.3203
REMARK 3 18 4.3328 - 4.2513 1.00 4376 239 0.2580 0.3150
REMARK 3 19 4.2513 - 4.1756 1.00 4356 241 0.2750 0.3428
REMARK 3 20 4.1756 - 4.1050 1.00 4379 237 0.2816 0.3577
REMARK 3 21 4.1050 - 4.0389 1.00 4347 242 0.3000 0.3474
REMARK 3 22 4.0389 - 3.9769 1.00 4359 217 0.3042 0.3797
REMARK 3 23 3.9769 - 3.9186 1.00 4426 226 0.3079 0.4001
REMARK 3 24 3.9186 - 3.8635 1.00 4398 227 0.3137 0.3643
REMARK 3 25 3.8635 - 3.8114 1.00 4315 250 0.3108 0.3744
REMARK 3 26 3.8114 - 3.7620 1.00 4388 227 0.3226 0.3555
REMARK 3 27 3.7620 - 3.7150 1.00 4369 237 0.3198 0.4397
REMARK 3 28 3.7150 - 3.6704 1.00 4388 237 0.3284 0.3907
REMARK 3 29 3.6704 - 3.6278 1.00 4358 246 0.3269 0.3619
REMARK 3 30 3.6278 - 3.5871 0.83 3606 187 0.3404 0.4006
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.10
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.580
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 99.79
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 : 0.005 57200
REMARK 3 ANGLE : 1.187 77204
REMARK 3 CHIRALITY : 0.088 8799
REMARK 3 PLANARITY : 0.006 10125
REMARK 3 DIHEDRAL : 18.421 22064
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 12
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'C' AND (RESSEQ 3:30 OR RESSEQ
REMARK 3 140:150 OR RESSEQ 445:455 OR RESSEQ 513:
REMARK 3 713 OR RESSEQ 786:832 OR RESSEQ 1056:1295)
REMARK 3 ) OR (CHAIN 'D' AND (RESSEQ 343:897 OR
REMARK 3 RESSEQ 899:931 OR RESSEQ 1137:1320 OR
REMARK 3 RESSEQ 1345:1375 OR RESSEQ 1408 OR RESSEQ
REMARK 3 1410)) OR (CHAIN 'E' AND RESSEQ 2:75)
REMARK 3 SELECTION : (CHAIN 'I' AND (RESSEQ 3:30 OR RESSEQ
REMARK 3 140:150 OR RESSEQ 445:455 OR RESSEQ 513:
REMARK 3 713 OR RESSEQ 786:832 OR RESSEQ 1056:1295)
REMARK 3 ) OR (CHAIN 'J' AND (RESSEQ 343:897 OR
REMARK 3 RESSEQ 899:931 OR RESSEQ 1137:1320 OR
REMARK 3 RESSEQ 1345:1375 OR RESSEQ 1408 OR RESSEQ
REMARK 3 1410)) OR (CHAIN 'K' AND RESSEQ 2:75)
REMARK 3 ATOM PAIRS NUMBER : 11014
REMARK 3 RMSD : 0.036
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND (RESSEQ 31:139 OR RESSEQ
REMARK 3 456:512)
REMARK 3 SELECTION : CHAIN 'I' AND (RESSEQ 31:139 OR RESSEQ
REMARK 3 456:512)
REMARK 3 ATOM PAIRS NUMBER : 1310
REMARK 3 RMSD : 0.058
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND (RESSEQ 151:225 OR RESSEQ
REMARK 3 340:444)
REMARK 3 SELECTION : CHAIN 'I' AND (RESSEQ 151:225 OR RESSEQ
REMARK 3 340:444)
REMARK 3 ATOM PAIRS NUMBER : 1470
REMARK 3 RMSD : 0.031
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND RESSEQ 226:339
REMARK 3 SELECTION : CHAIN 'I' AND RESSEQ 226:339
REMARK 3 ATOM PAIRS NUMBER : 912
REMARK 3 RMSD : 0.020
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND RESSEQ 714:785
REMARK 3 SELECTION : CHAIN 'I' AND RESSEQ 714:785
REMARK 3 ATOM PAIRS NUMBER : 549
REMARK 3 RMSD : 0.039
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'C' AND (RESSEQ 833:937 OR RESSEQ
REMARK 3 1040:1055)) OR (CHAIN 'F' AND RESSEQ 551:
REMARK 3 612)
REMARK 3 SELECTION : (CHAIN 'I' AND (RESSEQ 833:937 OR RESSEQ
REMARK 3 1040:1055)) OR (CHAIN 'L' AND RESSEQ 551:
REMARK 3 612)
REMARK 3 ATOM PAIRS NUMBER : 1414
REMARK 3 RMSD : 0.067
REMARK 3 NCS GROUP : 7
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'C' AND RESSEQ 938:1039
REMARK 3 SELECTION : CHAIN 'I' AND RESSEQ 938:1039
REMARK 3 ATOM PAIRS NUMBER : 835
REMARK 3 RMSD : 0.062
REMARK 3 NCS GROUP : 8
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN 'C' AND RESSEQ 1296:1342) OR
REMARK 3 (CHAIN 'D' AND (RESSEQ 17:342 OR RESSEQ
REMARK 3 1321:1344 OR RESSEQ 1409)) OR (CHAIN 'F'
REMARK 3 AND (RESSEQ 95:127 OR RESSEQ 375:444))
REMARK 3 SELECTION : (CHAIN 'I' AND RESSEQ 1296:1342) OR
REMARK 3 (CHAIN 'J' AND (RESSEQ 17:342 OR RESSEQ
REMARK 3 1321:1344 OR RESSEQ 1409)) OR (CHAIN 'L'
REMARK 3 AND (RESSEQ 95:127 OR RESSEQ 375:444))
REMARK 3 ATOM PAIRS NUMBER : 3954
REMARK 3 RMSD : 0.029
REMARK 3 NCS GROUP : 9
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'F' AND (RESSEQ 128:167 OR RESSEQ
REMARK 3 212:236 OR RESSEQ 242:374)
REMARK 3 SELECTION : CHAIN 'L' AND (RESSEQ 128:167 OR RESSEQ
REMARK 3 212:236 OR RESSEQ 242:374)
REMARK 3 ATOM PAIRS NUMBER : 1626
REMARK 3 RMSD : 0.025
REMARK 3 NCS GROUP : 10
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'F' AND RESSEQ 445:550
REMARK 3 SELECTION : CHAIN 'L' AND RESSEQ 445:550
REMARK 3 ATOM PAIRS NUMBER : 836
REMARK 3 RMSD : 0.068
REMARK 3 NCS GROUP : 11
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'A' AND RESSEQ 9:231
REMARK 3 SELECTION : CHAIN 'G' AND RESSEQ 9:231
REMARK 3 ATOM PAIRS NUMBER : 1725
REMARK 3 RMSD : 0.021
REMARK 3 NCS GROUP : 12
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN 'B' AND RESSEQ 9:234
REMARK 3 SELECTION : CHAIN 'H' AND RESSEQ 9:234
REMARK 3 ATOM PAIRS NUMBER : 1632
REMARK 3 RMSD : 0.037
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4LJZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138966
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.587
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : 0.12700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.20
REMARK 200 R MERGE FOR SHELL (I) : 0.95200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 64.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 0.1 M CALCIUM ACETATE, 12
REMARK 280 -15% PEG 400, 5 MM DITHIOTHREITOL, PH 6.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 93.18300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 154.59500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 103.37000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 154.59500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 93.18300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 103.37000
REMARK 290 SMTRY3 4 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: 36290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 155680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 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: 35850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 162360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -176.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, 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 MET A 1
REMARK 465 GLN A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 VAL A 5
REMARK 465 THR A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 232
REMARK 465 ASP A 233
REMARK 465 LEU A 234
REMARK 465 GLU A 235
REMARK 465 VAL A 236
REMARK 465 LEU A 237
REMARK 465 PHE A 238
REMARK 465 GLN A 239
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 VAL B 5
REMARK 465 SER B 161
REMARK 465 GLU B 162
REMARK 465 GLU B 163
REMARK 465 ASP B 164
REMARK 465 GLU B 165
REMARK 465 ARG B 166
REMARK 465 PRO B 167
REMARK 465 ILE B 168
REMARK 465 GLY B 169
REMARK 465 ARG B 170
REMARK 465 LEU B 171
REMARK 465 LEU B 237
REMARK 465 PHE B 238
REMARK 465 GLN B 239
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 ASP D 3
REMARK 465 LEU D 4
REMARK 465 LEU D 5
REMARK 465 LYS D 6
REMARK 465 PHE D 7
REMARK 465 MET D 932
REMARK 465 ARG D 933
REMARK 465 THR D 934
REMARK 465 PHE D 935
REMARK 465 HIS D 936
REMARK 465 ILE D 937
REMARK 465 GLY D 938
REMARK 465 GLY D 939
REMARK 465 ALA D 940
REMARK 465 ALA D 941
REMARK 465 SER D 942
REMARK 465 ARG D 943
REMARK 465 ALA D 944
REMARK 465 ALA D 945
REMARK 465 ALA D 946
REMARK 465 GLU D 947
REMARK 465 SER D 948
REMARK 465 SER D 949
REMARK 465 ILE D 950
REMARK 465 GLN D 951
REMARK 465 VAL D 952
REMARK 465 LYS D 953
REMARK 465 ASN D 954
REMARK 465 LYS D 955
REMARK 465 GLY D 956
REMARK 465 SER D 957
REMARK 465 ILE D 958
REMARK 465 LYS D 959
REMARK 465 LEU D 960
REMARK 465 SER D 961
REMARK 465 ASN D 962
REMARK 465 VAL D 963
REMARK 465 LYS D 964
REMARK 465 SER D 965
REMARK 465 VAL D 966
REMARK 465 VAL D 967
REMARK 465 ASN D 968
REMARK 465 SER D 969
REMARK 465 SER D 970
REMARK 465 GLY D 971
REMARK 465 LYS D 972
REMARK 465 LEU D 973
REMARK 465 VAL D 974
REMARK 465 ILE D 975
REMARK 465 THR D 976
REMARK 465 SER D 977
REMARK 465 ARG D 978
REMARK 465 ASN D 979
REMARK 465 THR D 980
REMARK 465 GLU D 981
REMARK 465 LEU D 982
REMARK 465 LYS D 983
REMARK 465 LEU D 984
REMARK 465 ILE D 985
REMARK 465 ASP D 986
REMARK 465 GLU D 987
REMARK 465 PHE D 988
REMARK 465 GLY D 989
REMARK 465 ARG D 990
REMARK 465 THR D 991
REMARK 465 LYS D 992
REMARK 465 GLU D 993
REMARK 465 SER D 994
REMARK 465 TYR D 995
REMARK 465 LYS D 996
REMARK 465 VAL D 997
REMARK 465 PRO D 998
REMARK 465 TYR D 999
REMARK 465 GLY D 1000
REMARK 465 ALA D 1001
REMARK 465 VAL D 1002
REMARK 465 LEU D 1003
REMARK 465 ALA D 1004
REMARK 465 LYS D 1005
REMARK 465 GLY D 1006
REMARK 465 ASP D 1007
REMARK 465 GLY D 1008
REMARK 465 GLU D 1009
REMARK 465 GLN D 1010
REMARK 465 VAL D 1011
REMARK 465 ALA D 1012
REMARK 465 GLY D 1013
REMARK 465 GLY D 1014
REMARK 465 GLU D 1015
REMARK 465 THR D 1016
REMARK 465 VAL D 1017
REMARK 465 ALA D 1018
REMARK 465 ASN D 1019
REMARK 465 TRP D 1020
REMARK 465 ASP D 1021
REMARK 465 PRO D 1022
REMARK 465 HIS D 1023
REMARK 465 THR D 1024
REMARK 465 MET D 1025
REMARK 465 PRO D 1026
REMARK 465 VAL D 1027
REMARK 465 ILE D 1028
REMARK 465 THR D 1029
REMARK 465 GLU D 1030
REMARK 465 VAL D 1031
REMARK 465 SER D 1032
REMARK 465 GLY D 1033
REMARK 465 PHE D 1034
REMARK 465 VAL D 1035
REMARK 465 ARG D 1036
REMARK 465 PHE D 1037
REMARK 465 THR D 1038
REMARK 465 ASP D 1039
REMARK 465 MET D 1040
REMARK 465 ILE D 1041
REMARK 465 ASP D 1042
REMARK 465 GLY D 1043
REMARK 465 GLN D 1044
REMARK 465 THR D 1045
REMARK 465 ILE D 1046
REMARK 465 THR D 1047
REMARK 465 ARG D 1048
REMARK 465 GLN D 1049
REMARK 465 THR D 1050
REMARK 465 ASP D 1051
REMARK 465 GLU D 1052
REMARK 465 LEU D 1053
REMARK 465 THR D 1054
REMARK 465 GLY D 1055
REMARK 465 LEU D 1056
REMARK 465 SER D 1057
REMARK 465 SER D 1058
REMARK 465 LEU D 1059
REMARK 465 VAL D 1060
REMARK 465 VAL D 1061
REMARK 465 LEU D 1062
REMARK 465 ASP D 1063
REMARK 465 SER D 1064
REMARK 465 ALA D 1065
REMARK 465 GLU D 1066
REMARK 465 ARG D 1067
REMARK 465 THR D 1068
REMARK 465 ALA D 1069
REMARK 465 GLY D 1070
REMARK 465 GLY D 1071
REMARK 465 LYS D 1072
REMARK 465 ASP D 1073
REMARK 465 LEU D 1074
REMARK 465 ARG D 1075
REMARK 465 PRO D 1076
REMARK 465 ALA D 1077
REMARK 465 LEU D 1078
REMARK 465 LYS D 1079
REMARK 465 ILE D 1080
REMARK 465 VAL D 1081
REMARK 465 ASP D 1082
REMARK 465 ALA D 1083
REMARK 465 GLN D 1084
REMARK 465 GLY D 1085
REMARK 465 ASN D 1086
REMARK 465 ASP D 1087
REMARK 465 VAL D 1088
REMARK 465 LEU D 1089
REMARK 465 ILE D 1090
REMARK 465 PRO D 1091
REMARK 465 GLY D 1092
REMARK 465 THR D 1093
REMARK 465 ASP D 1094
REMARK 465 MET D 1095
REMARK 465 PRO D 1096
REMARK 465 ALA D 1097
REMARK 465 GLN D 1098
REMARK 465 TYR D 1099
REMARK 465 PHE D 1100
REMARK 465 LEU D 1101
REMARK 465 PRO D 1102
REMARK 465 GLY D 1103
REMARK 465 LYS D 1104
REMARK 465 ALA D 1105
REMARK 465 ILE D 1106
REMARK 465 VAL D 1107
REMARK 465 GLN D 1108
REMARK 465 LEU D 1109
REMARK 465 GLU D 1110
REMARK 465 ASP D 1111
REMARK 465 GLY D 1112
REMARK 465 VAL D 1113
REMARK 465 GLN D 1114
REMARK 465 ILE D 1115
REMARK 465 SER D 1116
REMARK 465 SER D 1117
REMARK 465 GLY D 1118
REMARK 465 ASP D 1119
REMARK 465 THR D 1120
REMARK 465 LEU D 1121
REMARK 465 ALA D 1122
REMARK 465 ARG D 1123
REMARK 465 ILE D 1124
REMARK 465 PRO D 1125
REMARK 465 GLN D 1126
REMARK 465 GLU D 1127
REMARK 465 SER D 1128
REMARK 465 GLY D 1129
REMARK 465 GLY D 1130
REMARK 465 THR D 1131
REMARK 465 LYS D 1132
REMARK 465 ASP D 1133
REMARK 465 ILE D 1134
REMARK 465 GLU D 1377
REMARK 465 ALA D 1378
REMARK 465 PRO D 1379
REMARK 465 ALA D 1380
REMARK 465 ALA D 1381
REMARK 465 PRO D 1382
REMARK 465 GLN D 1383
REMARK 465 VAL D 1384
REMARK 465 THR D 1385
REMARK 465 ALA D 1386
REMARK 465 GLU D 1387
REMARK 465 ASP D 1388
REMARK 465 ALA D 1389
REMARK 465 SER D 1390
REMARK 465 ALA D 1391
REMARK 465 SER D 1392
REMARK 465 LEU D 1393
REMARK 465 ALA D 1394
REMARK 465 GLU D 1395
REMARK 465 LEU D 1396
REMARK 465 LEU D 1397
REMARK 465 ASN D 1398
REMARK 465 ALA D 1399
REMARK 465 GLY D 1400
REMARK 465 LEU D 1401
REMARK 465 GLY D 1402
REMARK 465 GLY D 1403
REMARK 465 SER D 1404
REMARK 465 ASP D 1405
REMARK 465 ASN D 1406
REMARK 465 GLU D 1407
REMARK 465 MET E 1
REMARK 465 ARG E 91
REMARK 465 PRO F 168
REMARK 465 ASN F 169
REMARK 465 ALA F 170
REMARK 465 GLU F 171
REMARK 465 GLU F 172
REMARK 465 ASP F 173
REMARK 465 LEU F 174
REMARK 465 ALA F 175
REMARK 465 PRO F 176
REMARK 465 THR F 177
REMARK 465 ALA F 178
REMARK 465 THR F 179
REMARK 465 HIS F 180
REMARK 465 VAL F 181
REMARK 465 GLY F 182
REMARK 465 SER F 183
REMARK 465 GLU F 184
REMARK 465 LEU F 185
REMARK 465 SER F 186
REMARK 465 GLN F 187
REMARK 465 GLU F 188
REMARK 465 ASP F 189
REMARK 465 LEU F 190
REMARK 465 ASP F 191
REMARK 465 ASP F 192
REMARK 465 ASP F 193
REMARK 465 GLU F 194
REMARK 465 ASP F 195
REMARK 465 GLU F 196
REMARK 465 ASP F 197
REMARK 465 GLU F 198
REMARK 465 GLU F 199
REMARK 465 ASP F 200
REMARK 465 GLY F 201
REMARK 465 ASP F 202
REMARK 465 ASP F 203
REMARK 465 ASP F 204
REMARK 465 SER F 205
REMARK 465 ALA F 206
REMARK 465 ASP F 207
REMARK 465 ASP F 208
REMARK 465 ASP F 209
REMARK 465 ASN F 210
REMARK 465 SER F 211
REMARK 465 ILE F 212
REMARK 465 ALA F 237
REMARK 465 LYS F 238
REMARK 465 GLY F 239
REMARK 465 ARG F 240
REMARK 465 SER F 241
REMARK 465 HIS F 242
REMARK 465 ASP F 613
REMARK 465 MET G 1
REMARK 465 GLN G 2
REMARK 465 GLY G 3
REMARK 465 SER G 4
REMARK 465 VAL G 5
REMARK 465 THR G 6
REMARK 465 GLU G 7
REMARK 465 VAL G 236
REMARK 465 LEU G 237
REMARK 465 PHE G 238
REMARK 465 GLN G 239
REMARK 465 MET H 1
REMARK 465 GLN H 2
REMARK 465 GLY H 3
REMARK 465 SER H 4
REMARK 465 VAL H 5
REMARK 465 ILE H 159
REMARK 465 HIS H 160
REMARK 465 SER H 161
REMARK 465 GLU H 162
REMARK 465 GLU H 163
REMARK 465 ASP H 164
REMARK 465 GLU H 165
REMARK 465 ARG H 166
REMARK 465 PRO H 167
REMARK 465 ILE H 168
REMARK 465 GLY H 169
REMARK 465 ARG H 170
REMARK 465 GLU H 235
REMARK 465 VAL H 236
REMARK 465 LEU H 237
REMARK 465 PHE H 238
REMARK 465 GLN H 239
REMARK 465 MET I 1
REMARK 465 VAL I 2
REMARK 465 MET J 1
REMARK 465 LYS J 2
REMARK 465 ASP J 3
REMARK 465 LEU J 4
REMARK 465 LEU J 5
REMARK 465 LYS J 6
REMARK 465 PHE J 7
REMARK 465 LEU J 8
REMARK 465 LYS J 9
REMARK 465 ALA J 10
REMARK 465 GLN J 11
REMARK 465 THR J 12
REMARK 465 LYS J 13
REMARK 465 THR J 14
REMARK 465 GLU J 15
REMARK 465 LYS J 334
REMARK 465 GLN J 335
REMARK 465 GLY J 336
REMARK 465 ARG J 337
REMARK 465 PHE J 338
REMARK 465 ARG J 339
REMARK 465 GLN J 340
REMARK 465 ASN J 341
REMARK 465 LEU J 342
REMARK 465 MET J 932
REMARK 465 ARG J 933
REMARK 465 THR J 934
REMARK 465 PHE J 935
REMARK 465 HIS J 936
REMARK 465 ILE J 937
REMARK 465 GLY J 938
REMARK 465 GLY J 939
REMARK 465 ALA J 940
REMARK 465 ALA J 941
REMARK 465 SER J 942
REMARK 465 ARG J 943
REMARK 465 ALA J 944
REMARK 465 ALA J 945
REMARK 465 ALA J 946
REMARK 465 GLU J 947
REMARK 465 GLU J 1127
REMARK 465 SER J 1128
REMARK 465 GLY J 1129
REMARK 465 GLY J 1130
REMARK 465 THR J 1131
REMARK 465 LYS J 1132
REMARK 465 ASP J 1133
REMARK 465 ILE J 1134
REMARK 465 THR J 1135
REMARK 465 GLY J 1136
REMARK 465 GLY J 1376
REMARK 465 GLU J 1377
REMARK 465 ALA J 1378
REMARK 465 PRO J 1379
REMARK 465 ALA J 1380
REMARK 465 ALA J 1381
REMARK 465 PRO J 1382
REMARK 465 GLN J 1383
REMARK 465 VAL J 1384
REMARK 465 THR J 1385
REMARK 465 ALA J 1386
REMARK 465 GLU J 1387
REMARK 465 ASP J 1388
REMARK 465 ALA J 1389
REMARK 465 SER J 1390
REMARK 465 ALA J 1391
REMARK 465 SER J 1392
REMARK 465 LEU J 1393
REMARK 465 ALA J 1394
REMARK 465 GLU J 1395
REMARK 465 LEU J 1396
REMARK 465 LEU J 1397
REMARK 465 ASN J 1398
REMARK 465 ALA J 1399
REMARK 465 GLY J 1400
REMARK 465 LEU J 1401
REMARK 465 GLY J 1402
REMARK 465 GLY J 1403
REMARK 465 SER J 1404
REMARK 465 ASP J 1405
REMARK 465 ASN J 1406
REMARK 465 GLU J 1407
REMARK 465 MET K 1
REMARK 465 GLN K 81
REMARK 465 ALA K 82
REMARK 465 VAL K 83
REMARK 465 THR K 84
REMARK 465 ALA K 85
REMARK 465 ILE K 86
REMARK 465 ALA K 87
REMARK 465 GLU K 88
REMARK 465 GLY K 89
REMARK 465 ARG K 90
REMARK 465 ARG K 91
REMARK 465 GLY L 92
REMARK 465 ARG L 93
REMARK 465 PRO L 168
REMARK 465 ASN L 169
REMARK 465 ALA L 170
REMARK 465 GLU L 171
REMARK 465 GLU L 172
REMARK 465 ASP L 173
REMARK 465 LEU L 174
REMARK 465 ALA L 175
REMARK 465 PRO L 176
REMARK 465 THR L 177
REMARK 465 ALA L 178
REMARK 465 THR L 179
REMARK 465 HIS L 180
REMARK 465 VAL L 181
REMARK 465 GLY L 182
REMARK 465 SER L 183
REMARK 465 GLU L 184
REMARK 465 LEU L 185
REMARK 465 SER L 186
REMARK 465 GLN L 187
REMARK 465 GLU L 188
REMARK 465 ASP L 189
REMARK 465 LEU L 190
REMARK 465 ASP L 191
REMARK 465 ASP L 192
REMARK 465 ASP L 193
REMARK 465 GLU L 194
REMARK 465 ASP L 195
REMARK 465 GLU L 196
REMARK 465 ASP L 197
REMARK 465 GLU L 198
REMARK 465 GLU L 199
REMARK 465 ASP L 200
REMARK 465 GLY L 201
REMARK 465 ASP L 202
REMARK 465 ASP L 203
REMARK 465 ASP L 204
REMARK 465 SER L 205
REMARK 465 ALA L 206
REMARK 465 ASP L 207
REMARK 465 ASP L 208
REMARK 465 ASP L 209
REMARK 465 ASN L 210
REMARK 465 SER L 211
REMARK 465 ILE L 212
REMARK 465 ALA L 237
REMARK 465 LYS L 238
REMARK 465 GLY L 239
REMARK 465 ARG L 240
REMARK 465 SER L 241
REMARK 465 HIS L 242
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 PHE A 8 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B 232 CG1 CG2
REMARK 470 ASP B 233 CG OD1 OD2
REMARK 470 LEU B 234 CG CD1 CD2
REMARK 470 GLU B 235 CG CD OE1 OE2
REMARK 470 VAL B 236 CG1 CG2
REMARK 470 PHE D 338 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG E 90 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 93 CG CD NE CZ NH1 NH2
REMARK 470 PHE G 8 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL G 232 CG1 CG2
REMARK 470 ASP G 233 CG OD1 OD2
REMARK 470 LEU G 234 CG CD1 CD2
REMARK 470 GLU G 235 CG CD OE1 OE2
REMARK 470 VAL H 232 CG1 CG2
REMARK 470 ASP H 233 CG OD1 OD2
REMARK 470 LEU H 234 CG CD1 CD2
REMARK 470 GLN I 120 CG CD OE1 NE2
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 NH1 ARG I 452 O TYR I 584 2.13
REMARK 500 NH1 ARG C 452 O TYR C 584 2.14
REMARK 500 O MET F 474 N ARG F 476 2.14
REMARK 500 O MET L 474 N ARG L 476 2.15
REMARK 500 O GLU C 40 OH TYR C 73 2.16
REMARK 500 O GLY J 613 OG1 THR J 617 2.17
REMARK 500 O GLU I 40 OH TYR I 73 2.17
REMARK 500 OG1 THR D 844 O ARG D 860 2.18
REMARK 500 O GLY D 613 OG1 THR D 617 2.18
REMARK 500 O GLY J 893 NH1 ARG J 1258 2.18
REMARK 500 OG1 THR J 844 O ARG J 860 2.18
REMARK 500 NH1 ARG I 74 OE2 GLU I 121 2.18
REMARK 500 O GLY I 168 N VAL I 170 2.19
REMARK 500 O GLY D 893 NH1 ARG D 1258 2.19
REMARK 500 NH1 ARG C 74 OE2 GLU C 121 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU C 108 NZ LYS I 422 3554 2.19
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 GLN B 75 CA - CB - CG ANGL. DEV. = 13.2 DEGREES
REMARK 500 GLN C 490 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 GLY C 747 N - CA - C ANGL. DEV. = 36.5 DEGREES
REMARK 500 PRO C 897 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500 GLY D 231 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG D 678 CA - CB - CG ANGL. DEV. = 13.4 DEGREES
REMARK 500 PRO D 859 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG D 860 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D1262 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLY I 112 N - CA - C ANGL. DEV. = 17.1 DEGREES
REMARK 500 GLY I 747 N - CA - C ANGL. DEV. = 29.7 DEGREES
REMARK 500 PRO I 897 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG J 678 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 PRO J 859 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG J 860 NE - CZ - NH1 ANGL. DEV. = 3.2 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 VAL A 19 -60.90 -120.58
REMARK 500 GLU A 32 -169.92 -75.58
REMARK 500 SER A 49 -70.67 -81.93
REMARK 500 CYS A 54 79.20 -116.74
REMARK 500 THR A 57 -72.14 -127.42
REMARK 500 ASP A 62 -74.09 -62.24
REMARK 500 GLN A 93 -63.88 -129.76
REMARK 500 HIS A 160 -60.07 -133.83
REMARK 500 GLU A 162 -108.11 55.81
REMARK 500 ASP A 164 67.05 62.23
REMARK 500 ARG A 166 -38.90 -36.16
REMARK 500 SER A 178 132.16 174.41
REMARK 500 GLU A 181 -61.79 -101.37
REMARK 500 THR A 196 -72.65 -70.88
REMARK 500 SER B 20 -122.00 56.95
REMARK 500 SER B 21 -63.16 -125.60
REMARK 500 LEU B 48 -72.24 -81.15
REMARK 500 ALA B 55 -106.23 -130.61
REMARK 500 SER B 69 -178.94 -172.88
REMARK 500 LYS B 104 156.34 174.79
REMARK 500 ASP B 120 75.92 -110.86
REMARK 500 ILE B 130 -63.28 -92.42
REMARK 500 GLU B 136 -144.33 62.43
REMARK 500 ALA B 138 112.90 62.74
REMARK 500 TYR B 177 -60.57 -98.82
REMARK 500 GLU B 193 -121.82 43.94
REMARK 500 PHE B 231 -61.99 -122.40
REMARK 500 LEU B 234 -117.64 65.56
REMARK 500 GLU C 40 161.77 177.10
REMARK 500 GLU C 44 -165.22 148.43
REMARK 500 SER C 63 13.51 51.22
REMARK 500 VAL C 71 -73.75 -91.23
REMARK 500 LYS C 118 41.21 -90.81
REMARK 500 ILE C 138 -63.73 -100.01
REMARK 500 SER C 159 -71.13 -111.78
REMARK 500 HIS C 165 -16.23 76.33
REMARK 500 SER C 166 19.74 57.23
REMARK 500 LYS C 169 -22.18 48.86
REMARK 500 VAL C 170 -153.69 50.58
REMARK 500 ASP C 199 -139.01 56.28
REMARK 500 ARG C 201 -174.86 -68.06
REMARK 500 ASN C 214 65.34 62.81
REMARK 500 ASP C 234 -123.26 56.87
REMARK 500 LYS C 236 73.47 62.70
REMARK 500 LEU C 237 77.04 65.47
REMARK 500 ASN C 357 -64.75 -131.33
REMARK 500 ARG C 371 74.98 -119.88
REMARK 500 LEU C 388 -75.99 -75.48
REMARK 500 SER C 398 -152.67 55.95
REMARK 500 GLU C 412 -60.64 -104.64
REMARK 500
REMARK 500 THIS ENTRY HAS 347 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE B 140 SER B 141 149.67
REMARK 500 ALA C 109 PRO C 110 51.57
REMARK 500 GLU C 111 GLY C 112 -137.39
REMARK 500 GLY C 112 THR C 113 -112.57
REMARK 500 LYS C 236 LEU C 237 144.02
REMARK 500 PRO C 489 GLN C 490 68.18
REMARK 500 ASP C 648 GLN C 649 143.90
REMARK 500 ALA C 746 GLY C 747 -145.15
REMARK 500 GLN C 1134 GLN C 1135 -132.92
REMARK 500 GLY C 1202 ASP C 1203 -146.83
REMARK 500 SER D 230 GLY D 231 57.12
REMARK 500 GLU D 1168 THR D 1169 136.53
REMARK 500 ASP D 1184 PRO D 1185 -138.71
REMARK 500 GLY D 1296 LYS D 1297 147.64
REMARK 500 MET F 474 GLY F 475 -149.67
REMARK 500 PRO F 601 SER F 602 -118.65
REMARK 500 PHE G 231 VAL G 232 -149.73
REMARK 500 ILE H 140 SER H 141 149.45
REMARK 500 ALA I 109 PRO I 110 92.81
REMARK 500 GLU I 111 GLY I 112 -49.22
REMARK 500 GLY I 112 THR I 113 -71.14
REMARK 500 LYS I 236 LEU I 237 144.08
REMARK 500 PRO I 489 GLN I 490 105.58
REMARK 500 ASP I 648 GLN I 649 143.97
REMARK 500 GLN I 1134 GLN I 1135 -54.68
REMARK 500 GLN I 1136 GLU I 1137 -149.88
REMARK 500 ALA I 1153 ASP I 1154 -142.43
REMARK 500 GLY I 1202 ASP I 1203 145.60
REMARK 500 ASN I 1236 HIS I 1237 149.98
REMARK 500 SER J 230 GLY J 231 116.41
REMARK 500 GLU J 1168 THR J 1169 136.44
REMARK 500 ASP J 1184 PRO J 1185 -138.95
REMARK 500 GLY J 1296 LYS J 1297 148.12
REMARK 500 PRO L 601 SER L 602 -80.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO C 43 10.12
REMARK 500 GLY C 168 11.01
REMARK 500 GLU C 985 11.83
REMARK 500 GLY C1152 -10.93
REMARK 500 GLY C1202 -12.92
REMARK 500 PHE D 172 11.37
REMARK 500 MET F 474 -13.19
REMARK 500 SER F 602 -10.88
REMARK 500 PRO I 43 -10.22
REMARK 500 GLY I 168 -11.41
REMARK 500 GLY I1152 12.88
REMARK 500 GLY I1202 12.54
REMARK 500 SER J 230 11.50
REMARK 500 ALA J1359 -12.46
REMARK 500 GLY K 14 11.42
REMARK 500 MET L 474 10.27
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 D1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 70 SG
REMARK 620 2 CYS D 72 SG 103.3
REMARK 620 3 CYS D 85 SG 100.4 106.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 814 SG
REMARK 620 2 CYS D 888 SG 95.7
REMARK 620 3 CYS D 895 SG 89.3 98.5
REMARK 620 4 CYS D 898 SG 94.5 162.2 96.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 70 SG
REMARK 620 2 CYS J 72 SG 102.9
REMARK 620 3 CYS J 85 SG 100.4 106.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J1503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 814 SG
REMARK 620 2 CYS J 888 SG 95.0
REMARK 620 3 CYS J 895 SG 89.5 97.7
REMARK 620 4 CYS J 898 SG 118.2 129.8 117.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 1503
DBREF 4LJZ A 1 234 UNP C9QXI7 C9QXI7_ECOD1 1 234
DBREF 4LJZ B 1 234 UNP C9QXI7 C9QXI7_ECOD1 1 234
DBREF 4LJZ C 1 1342 UNP C9QV90 C9QV90_ECOD1 1 1342
DBREF 4LJZ D 1 1407 UNP C5A0S8 C5A0S8_ECOBW 1 1407
DBREF 4LJZ E 1 91 UNP C9QUL2 C9QUL2_ECOD1 1 91
DBREF 4LJZ F 92 613 UNP P00579 RPOD_ECOLI 92 613
DBREF 4LJZ G 1 234 UNP C9QXI7 C9QXI7_ECOD1 1 234
DBREF 4LJZ H 1 234 UNP C9QXI7 C9QXI7_ECOD1 1 234
DBREF 4LJZ I 1 1342 UNP C9QV90 C9QV90_ECOD1 1 1342
DBREF 4LJZ J 1 1407 UNP C5A0S8 C5A0S8_ECOBW 1 1407
DBREF 4LJZ K 1 91 UNP C9QUL2 C9QUL2_ECOD1 1 91
DBREF 4LJZ L 92 613 UNP P00579 RPOD_ECOLI 92 613
SEQADV 4LJZ GLU A 235 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ VAL A 236 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ LEU A 237 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ PHE A 238 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLN A 239 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLU B 235 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ VAL B 236 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ LEU B 237 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ PHE B 238 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLN B 239 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLU G 235 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ VAL G 236 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ LEU G 237 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ PHE G 238 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLN G 239 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLU H 235 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ VAL H 236 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ LEU H 237 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ PHE H 238 UNP C9QXI7 EXPRESSION TAG
SEQADV 4LJZ GLN H 239 UNP C9QXI7 EXPRESSION TAG
SEQRES 1 A 239 MET GLN GLY SER VAL THR GLU PHE LEU LYS PRO ARG LEU
SEQRES 2 A 239 VAL ASP ILE GLU GLN VAL SER SER THR HIS ALA LYS VAL
SEQRES 3 A 239 THR LEU GLU PRO LEU GLU ARG GLY PHE GLY HIS THR LEU
SEQRES 4 A 239 GLY ASN ALA LEU ARG ARG ILE LEU LEU SER SER MET PRO
SEQRES 5 A 239 GLY CYS ALA VAL THR GLU VAL GLU ILE ASP GLY VAL LEU
SEQRES 6 A 239 HIS GLU TYR SER THR LYS GLU GLY VAL GLN GLU ASP ILE
SEQRES 7 A 239 LEU GLU ILE LEU LEU ASN LEU LYS GLY LEU ALA VAL ARG
SEQRES 8 A 239 VAL GLN GLY LYS ASP GLU VAL ILE LEU THR LEU ASN LYS
SEQRES 9 A 239 SER GLY ILE GLY PRO VAL THR ALA ALA ASP ILE THR HIS
SEQRES 10 A 239 ASP GLY ASP VAL GLU ILE VAL LYS PRO GLN HIS VAL ILE
SEQRES 11 A 239 CYS HIS LEU THR ASP GLU ASN ALA SER ILE SER MET ARG
SEQRES 12 A 239 ILE LYS VAL GLN ARG GLY ARG GLY TYR VAL PRO ALA SER
SEQRES 13 A 239 THR ARG ILE HIS SER GLU GLU ASP GLU ARG PRO ILE GLY
SEQRES 14 A 239 ARG LEU LEU VAL ASP ALA CYS TYR SER PRO VAL GLU ARG
SEQRES 15 A 239 ILE ALA TYR ASN VAL GLU ALA ALA ARG VAL GLU GLN ARG
SEQRES 16 A 239 THR ASP LEU ASP LYS LEU VAL ILE GLU MET GLU THR ASN
SEQRES 17 A 239 GLY THR ILE ASP PRO GLU GLU ALA ILE ARG ARG ALA ALA
SEQRES 18 A 239 THR ILE LEU ALA GLU GLN LEU GLU ALA PHE VAL ASP LEU
SEQRES 19 A 239 GLU VAL LEU PHE GLN
SEQRES 1 B 239 MET GLN GLY SER VAL THR GLU PHE LEU LYS PRO ARG LEU
SEQRES 2 B 239 VAL ASP ILE GLU GLN VAL SER SER THR HIS ALA LYS VAL
SEQRES 3 B 239 THR LEU GLU PRO LEU GLU ARG GLY PHE GLY HIS THR LEU
SEQRES 4 B 239 GLY ASN ALA LEU ARG ARG ILE LEU LEU SER SER MET PRO
SEQRES 5 B 239 GLY CYS ALA VAL THR GLU VAL GLU ILE ASP GLY VAL LEU
SEQRES 6 B 239 HIS GLU TYR SER THR LYS GLU GLY VAL GLN GLU ASP ILE
SEQRES 7 B 239 LEU GLU ILE LEU LEU ASN LEU LYS GLY LEU ALA VAL ARG
SEQRES 8 B 239 VAL GLN GLY LYS ASP GLU VAL ILE LEU THR LEU ASN LYS
SEQRES 9 B 239 SER GLY ILE GLY PRO VAL THR ALA ALA ASP ILE THR HIS
SEQRES 10 B 239 ASP GLY ASP VAL GLU ILE VAL LYS PRO GLN HIS VAL ILE
SEQRES 11 B 239 CYS HIS LEU THR ASP GLU ASN ALA SER ILE SER MET ARG
SEQRES 12 B 239 ILE LYS VAL GLN ARG GLY ARG GLY TYR VAL PRO ALA SER
SEQRES 13 B 239 THR ARG ILE HIS SER GLU GLU ASP GLU ARG PRO ILE GLY
SEQRES 14 B 239 ARG LEU LEU VAL ASP ALA CYS TYR SER PRO VAL GLU ARG
SEQRES 15 B 239 ILE ALA TYR ASN VAL GLU ALA ALA ARG VAL GLU GLN ARG
SEQRES 16 B 239 THR ASP LEU ASP LYS LEU VAL ILE GLU MET GLU THR ASN
SEQRES 17 B 239 GLY THR ILE ASP PRO GLU GLU ALA ILE ARG ARG ALA ALA
SEQRES 18 B 239 THR ILE LEU ALA GLU GLN LEU GLU ALA PHE VAL ASP LEU
SEQRES 19 B 239 GLU VAL LEU PHE GLN
SEQRES 1 C 1342 MET VAL TYR SER TYR THR GLU LYS LYS ARG ILE ARG LYS
SEQRES 2 C 1342 ASP PHE GLY LYS ARG PRO GLN VAL LEU ASP VAL PRO TYR
SEQRES 3 C 1342 LEU LEU SER ILE GLN LEU ASP SER PHE GLN LYS PHE ILE
SEQRES 4 C 1342 GLU GLN ASP PRO GLU GLY GLN TYR GLY LEU GLU ALA ALA
SEQRES 5 C 1342 PHE ARG SER VAL PHE PRO ILE GLN SER TYR SER GLY ASN
SEQRES 6 C 1342 SER GLU LEU GLN TYR VAL SER TYR ARG LEU GLY GLU PRO
SEQRES 7 C 1342 VAL PHE ASP VAL GLN GLU CYS GLN ILE ARG GLY VAL THR
SEQRES 8 C 1342 TYR SER ALA PRO LEU ARG VAL LYS LEU ARG LEU VAL ILE
SEQRES 9 C 1342 TYR GLU ARG GLU ALA PRO GLU GLY THR VAL LYS ASP ILE
SEQRES 10 C 1342 LYS GLU GLN GLU VAL TYR MET GLY GLU ILE PRO LEU MET
SEQRES 11 C 1342 THR ASP ASN GLY THR PHE VAL ILE ASN GLY THR GLU ARG
SEQRES 12 C 1342 VAL ILE VAL SER GLN LEU HIS ARG SER PRO GLY VAL PHE
SEQRES 13 C 1342 PHE ASP SER ASP LYS GLY LYS THR HIS SER SER GLY LYS
SEQRES 14 C 1342 VAL LEU TYR ASN ALA ARG ILE ILE PRO TYR ARG GLY SER
SEQRES 15 C 1342 TRP LEU ASP PHE GLU PHE ASP PRO LYS ASP ASN LEU PHE
SEQRES 16 C 1342 VAL ARG ILE ASP ARG ARG ARG LYS LEU PRO ALA THR ILE
SEQRES 17 C 1342 ILE LEU ARG ALA LEU ASN TYR THR THR GLU GLN ILE LEU
SEQRES 18 C 1342 ASP LEU PHE PHE GLU LYS VAL ILE PHE GLU ILE ARG ASP
SEQRES 19 C 1342 ASN LYS LEU GLN MET GLU LEU VAL PRO GLU ARG LEU ARG
SEQRES 20 C 1342 GLY GLU THR ALA SER PHE ASP ILE GLU ALA ASN GLY LYS
SEQRES 21 C 1342 VAL TYR VAL GLU LYS GLY ARG ARG ILE THR ALA ARG HIS
SEQRES 22 C 1342 ILE ARG GLN LEU GLU LYS ASP ASP VAL LYS LEU ILE GLU
SEQRES 23 C 1342 VAL PRO VAL GLU TYR ILE ALA GLY LYS VAL VAL ALA LYS
SEQRES 24 C 1342 ASP TYR ILE ASP GLU SER THR GLY GLU LEU ILE CYS ALA
SEQRES 25 C 1342 ALA ASN MET GLU LEU SER LEU ASP LEU LEU ALA LYS LEU
SEQRES 26 C 1342 SER GLN SER GLY HIS LYS ARG ILE GLU THR LEU PHE THR
SEQRES 27 C 1342 ASN ASP LEU ASP HIS GLY PRO TYR ILE SER GLU THR LEU
SEQRES 28 C 1342 ARG VAL ASP PRO THR ASN ASP ARG LEU SER ALA LEU VAL
SEQRES 29 C 1342 GLU ILE TYR ARG MET MET ARG PRO GLY GLU PRO PRO THR
SEQRES 30 C 1342 ARG GLU ALA ALA GLU SER LEU PHE GLU ASN LEU PHE PHE
SEQRES 31 C 1342 SER GLU ASP ARG TYR ASP LEU SER ALA VAL GLY ARG MET
SEQRES 32 C 1342 LYS PHE ASN ARG SER LEU LEU ARG GLU GLU ILE GLU GLY
SEQRES 33 C 1342 SER GLY ILE LEU SER LYS ASP ASP ILE ILE ASP VAL MET
SEQRES 34 C 1342 LYS LYS LEU ILE ASP ILE ARG ASN GLY LYS GLY GLU VAL
SEQRES 35 C 1342 ASP ASP ILE ASP HIS LEU GLY ASN ARG ARG ILE ARG SER
SEQRES 36 C 1342 VAL GLY GLU MET ALA GLU ASN GLN PHE ARG VAL GLY LEU
SEQRES 37 C 1342 VAL ARG VAL GLU ARG ALA VAL LYS GLU ARG LEU SER LEU
SEQRES 38 C 1342 GLY ASP LEU ASP THR LEU MET PRO GLN ASP MET ILE ASN
SEQRES 39 C 1342 ALA LYS PRO ILE SER ALA ALA VAL LYS GLU PHE PHE GLY
SEQRES 40 C 1342 SER SER GLN LEU SER GLN PHE MET ASP GLN ASN ASN PRO
SEQRES 41 C 1342 LEU SER GLU ILE THR HIS LYS ARG ARG ILE SER ALA LEU
SEQRES 42 C 1342 GLY PRO GLY GLY LEU THR ARG GLU ARG ALA GLY PHE GLU
SEQRES 43 C 1342 VAL ARG ASP VAL HIS PRO THR HIS TYR GLY ARG VAL CYS
SEQRES 44 C 1342 PRO ILE GLU THR PRO GLU GLY PRO ASN ILE GLY LEU ILE
SEQRES 45 C 1342 ASN SER LEU SER VAL TYR ALA GLN THR ASN GLU TYR GLY
SEQRES 46 C 1342 PHE LEU GLU THR PRO TYR ARG LYS VAL THR ASP GLY VAL
SEQRES 47 C 1342 VAL THR ASP GLU ILE HIS TYR LEU SER ALA ILE GLU GLU
SEQRES 48 C 1342 GLY ASN TYR VAL ILE ALA GLN ALA ASN SER ASN LEU ASP
SEQRES 49 C 1342 GLU GLU GLY HIS PHE VAL GLU ASP LEU VAL THR CYS ARG
SEQRES 50 C 1342 SER LYS GLY GLU SER SER LEU PHE SER ARG ASP GLN VAL
SEQRES 51 C 1342 ASP TYR MET ASP VAL SER THR GLN GLN VAL VAL SER VAL
SEQRES 52 C 1342 GLY ALA SER LEU ILE PRO PHE LEU GLU HIS ASP ASP ALA
SEQRES 53 C 1342 ASN ARG ALA LEU MET GLY ALA ASN MET GLN ARG GLN ALA
SEQRES 54 C 1342 VAL PRO THR LEU ARG ALA ASP LYS PRO LEU VAL GLY THR
SEQRES 55 C 1342 GLY MET GLU ARG ALA VAL ALA VAL ASP SER GLY VAL THR
SEQRES 56 C 1342 ALA VAL ALA LYS ARG GLY GLY VAL VAL GLN TYR VAL ASP
SEQRES 57 C 1342 ALA SER ARG ILE VAL ILE LYS VAL ASN GLU ASP GLU MET
SEQRES 58 C 1342 TYR PRO GLY GLU ALA GLY ILE ASP ILE TYR ASN LEU THR
SEQRES 59 C 1342 LYS TYR THR ARG SER ASN GLN ASN THR CYS ILE ASN GLN
SEQRES 60 C 1342 MET PRO CYS VAL SER LEU GLY GLU PRO VAL GLU ARG GLY
SEQRES 61 C 1342 ASP VAL LEU ALA ASP GLY PRO SER THR ASP LEU GLY GLU
SEQRES 62 C 1342 LEU ALA LEU GLY GLN ASN MET ARG VAL ALA PHE MET PRO
SEQRES 63 C 1342 TRP ASN GLY TYR ASN PHE GLU ASP SER ILE LEU VAL SER
SEQRES 64 C 1342 GLU ARG VAL VAL GLN GLU ASP ARG PHE THR THR ILE HIS
SEQRES 65 C 1342 ILE GLN GLU LEU ALA CYS VAL SER ARG ASP THR LYS LEU
SEQRES 66 C 1342 GLY PRO GLU GLU ILE THR ALA ASP ILE PRO ASN VAL GLY
SEQRES 67 C 1342 GLU ALA ALA LEU SER LYS LEU ASP GLU SER GLY ILE VAL
SEQRES 68 C 1342 TYR ILE GLY ALA GLU VAL THR GLY GLY ASP ILE LEU VAL
SEQRES 69 C 1342 GLY LYS VAL THR PRO LYS GLY GLU THR GLN LEU THR PRO
SEQRES 70 C 1342 GLU GLU LYS LEU LEU ARG ALA ILE PHE GLY GLU LYS ALA
SEQRES 71 C 1342 SER ASP VAL LYS ASP SER SER LEU ARG VAL PRO ASN GLY
SEQRES 72 C 1342 VAL SER GLY THR VAL ILE ASP VAL GLN VAL PHE THR ARG
SEQRES 73 C 1342 ASP GLY VAL GLU LYS ASP LYS ARG ALA LEU GLU ILE GLU
SEQRES 74 C 1342 GLU MET GLN LEU LYS GLN ALA LYS LYS ASP LEU SER GLU
SEQRES 75 C 1342 GLU LEU GLN ILE LEU GLU ALA GLY LEU PHE SER ARG ILE
SEQRES 76 C 1342 ARG ALA VAL LEU VAL ALA GLY GLY VAL GLU ALA GLU LYS
SEQRES 77 C 1342 LEU ASP LYS LEU PRO ARG ASP ARG TRP LEU GLU LEU GLY
SEQRES 78 C 1342 LEU THR ASP GLU GLU LYS GLN ASN GLN LEU GLU GLN LEU
SEQRES 79 C 1342 ALA GLU GLN TYR ASP GLU LEU LYS HIS GLU PHE GLU LYS
SEQRES 80 C 1342 LYS LEU GLU ALA LYS ARG ARG LYS ILE THR GLN GLY ASP
SEQRES 81 C 1342 ASP LEU ALA PRO GLY VAL LEU LYS ILE VAL LYS VAL TYR
SEQRES 82 C 1342 LEU ALA VAL LYS ARG ARG ILE GLN PRO GLY ASP LYS MET
SEQRES 83 C 1342 ALA GLY ARG HIS GLY ASN LYS GLY VAL ILE SER LYS ILE
SEQRES 84 C 1342 ASN PRO ILE GLU ASP MET PRO TYR ASP GLU ASN GLY THR
SEQRES 85 C 1342 PRO VAL ASP ILE VAL LEU ASN PRO LEU GLY VAL PRO SER
SEQRES 86 C 1342 ARG MET ASN ILE GLY GLN ILE LEU GLU THR HIS LEU GLY
SEQRES 87 C 1342 MET ALA ALA LYS GLY ILE GLY ASP LYS ILE ASN ALA MET
SEQRES 88 C 1342 LEU LYS GLN GLN GLN GLU VAL ALA LYS LEU ARG GLU PHE
SEQRES 89 C 1342 ILE GLN ARG ALA TYR ASP LEU GLY ALA ASP VAL ARG GLN
SEQRES 90 C 1342 LYS VAL ASP LEU SER THR PHE SER ASP GLU GLU VAL MET
SEQRES 91 C 1342 ARG LEU ALA GLU ASN LEU ARG LYS GLY MET PRO ILE ALA
SEQRES 92 C 1342 THR PRO VAL PHE ASP GLY ALA LYS GLU ALA GLU ILE LYS
SEQRES 93 C 1342 GLU LEU LEU LYS LEU GLY ASP LEU PRO THR SER GLY GLN
SEQRES 94 C 1342 ILE ARG LEU TYR ASP GLY ARG THR GLY GLU GLN PHE GLU
SEQRES 95 C 1342 ARG PRO VAL THR VAL GLY TYR MET TYR MET LEU LYS LEU
SEQRES 96 C 1342 ASN HIS LEU VAL ASP ASP LYS MET HIS ALA ARG SER THR
SEQRES 97 C 1342 GLY SER TYR SER LEU VAL THR GLN GLN PRO LEU GLY GLY
SEQRES 98 C 1342 LYS ALA GLN PHE GLY GLY GLN ARG PHE GLY GLU MET GLU
SEQRES 99 C 1342 VAL TRP ALA LEU GLU ALA TYR GLY ALA ALA TYR THR LEU
SEQRES 100 C 1342 GLN GLU MET LEU THR VAL LYS SER ASP ASP VAL ASN GLY
SEQRES 101 C 1342 ARG THR LYS MET TYR LYS ASN ILE VAL ASP GLY ASN HIS
SEQRES 102 C 1342 GLN MET GLU PRO GLY MET PRO GLU SER PHE ASN VAL LEU
SEQRES 103 C 1342 LEU LYS GLU ILE ARG SER LEU GLY ILE ASN ILE GLU LEU
SEQRES 104 C 1342 GLU ASP GLU
SEQRES 1 D 1407 MET LYS ASP LEU LEU LYS PHE LEU LYS ALA GLN THR LYS
SEQRES 2 D 1407 THR GLU GLU PHE ASP ALA ILE LYS ILE ALA LEU ALA SER
SEQRES 3 D 1407 PRO ASP MET ILE ARG SER TRP SER PHE GLY GLU VAL LYS
SEQRES 4 D 1407 LYS PRO GLU THR ILE ASN TYR ARG THR PHE LYS PRO GLU
SEQRES 5 D 1407 ARG ASP GLY LEU PHE CYS ALA ARG ILE PHE GLY PRO VAL
SEQRES 6 D 1407 LYS ASP TYR GLU CYS LEU CYS GLY LYS TYR LYS ARG LEU
SEQRES 7 D 1407 LYS HIS ARG GLY VAL ILE CYS GLU LYS CYS GLY VAL GLU
SEQRES 8 D 1407 VAL THR GLN THR LYS VAL ARG ARG GLU ARG MET GLY HIS
SEQRES 9 D 1407 ILE GLU LEU ALA SER PRO THR ALA HIS ILE TRP PHE LEU
SEQRES 10 D 1407 LYS SER LEU PRO SER ARG ILE GLY LEU LEU LEU ASP MET
SEQRES 11 D 1407 PRO LEU ARG ASP ILE GLU ARG VAL LEU TYR PHE GLU SER
SEQRES 12 D 1407 TYR VAL VAL ILE GLU GLY GLY MET THR ASN LEU GLU ARG
SEQRES 13 D 1407 GLN GLN ILE LEU THR GLU GLU GLN TYR LEU ASP ALA LEU
SEQRES 14 D 1407 GLU GLU PHE GLY ASP GLU PHE ASP ALA LYS MET GLY ALA
SEQRES 15 D 1407 GLU ALA ILE GLN ALA LEU LEU LYS SER MET ASP LEU GLU
SEQRES 16 D 1407 GLN GLU CYS GLU GLN LEU ARG GLU GLU LEU ASN GLU THR
SEQRES 17 D 1407 ASN SER GLU THR LYS ARG LYS LYS LEU THR LYS ARG ILE
SEQRES 18 D 1407 LYS LEU LEU GLU ALA PHE VAL GLN SER GLY ASN LYS PRO
SEQRES 19 D 1407 GLU TRP MET ILE LEU THR VAL LEU PRO VAL LEU PRO PRO
SEQRES 20 D 1407 ASP LEU ARG PRO LEU VAL PRO LEU ASP GLY GLY ARG PHE
SEQRES 21 D 1407 ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG VAL ILE
SEQRES 22 D 1407 ASN ARG ASN ASN ARG LEU LYS ARG LEU LEU ASP LEU ALA
SEQRES 23 D 1407 ALA PRO ASP ILE ILE VAL ARG ASN GLU LYS ARG MET LEU
SEQRES 24 D 1407 GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY ARG ARG
SEQRES 25 D 1407 GLY ARG ALA ILE THR GLY SER ASN LYS ARG PRO LEU LYS
SEQRES 26 D 1407 SER LEU ALA ASP MET ILE LYS GLY LYS GLN GLY ARG PHE
SEQRES 27 D 1407 ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP TYR SER GLY
SEQRES 28 D 1407 ARG SER VAL ILE THR VAL GLY PRO TYR LEU ARG LEU HIS
SEQRES 29 D 1407 GLN CYS GLY LEU PRO LYS LYS MET ALA LEU GLU LEU PHE
SEQRES 30 D 1407 LYS PRO PHE ILE TYR GLY LYS LEU GLU LEU ARG GLY LEU
SEQRES 31 D 1407 ALA THR THR ILE LYS ALA ALA LYS LYS MET VAL GLU ARG
SEQRES 32 D 1407 GLU GLU ALA VAL VAL TRP ASP ILE LEU ASP GLU VAL ILE
SEQRES 33 D 1407 ARG GLU HIS PRO VAL LEU LEU ASN ARG ALA PRO THR LEU
SEQRES 34 D 1407 HIS ARG LEU GLY ILE GLN ALA PHE GLU PRO VAL LEU ILE
SEQRES 35 D 1407 GLU GLY LYS ALA ILE GLN LEU HIS PRO LEU VAL CYS ALA
SEQRES 36 D 1407 ALA TYR ASN ALA ASP PHE ASP GLY ASP GLN MET ALA VAL
SEQRES 37 D 1407 HIS VAL PRO LEU THR LEU GLU ALA GLN LEU GLU ALA ARG
SEQRES 38 D 1407 ALA LEU MET MET SER THR ASN ASN ILE LEU SER PRO ALA
SEQRES 39 D 1407 ASN GLY GLU PRO ILE ILE VAL PRO SER GLN ASP VAL VAL
SEQRES 40 D 1407 LEU GLY LEU TYR TYR MET THR ARG ASP CYS VAL ASN ALA
SEQRES 41 D 1407 LYS GLY GLU GLY MET VAL LEU THR GLY PRO LYS GLU ALA
SEQRES 42 D 1407 GLU ARG LEU TYR ARG SER GLY LEU ALA SER LEU HIS ALA
SEQRES 43 D 1407 ARG VAL LYS VAL ARG ILE THR GLU TYR GLU LYS ASP ALA
SEQRES 44 D 1407 ASN GLY GLU LEU VAL ALA LYS THR SER LEU LYS ASP THR
SEQRES 45 D 1407 THR VAL GLY ARG ALA ILE LEU TRP MET ILE VAL PRO LYS
SEQRES 46 D 1407 GLY LEU PRO TYR SER ILE VAL ASN GLN ALA LEU GLY LYS
SEQRES 47 D 1407 LYS ALA ILE SER LYS MET LEU ASN THR CYS TYR ARG ILE
SEQRES 48 D 1407 LEU GLY LEU LYS PRO THR VAL ILE PHE ALA ASP GLN ILE
SEQRES 49 D 1407 MET TYR THR GLY PHE ALA TYR ALA ALA ARG SER GLY ALA
SEQRES 50 D 1407 SER VAL GLY ILE ASP ASP MET VAL ILE PRO GLU LYS LYS
SEQRES 51 D 1407 HIS GLU ILE ILE SER GLU ALA GLU ALA GLU VAL ALA GLU
SEQRES 52 D 1407 ILE GLN GLU GLN PHE GLN SER GLY LEU VAL THR ALA GLY
SEQRES 53 D 1407 GLU ARG TYR ASN LYS VAL ILE ASP ILE TRP ALA ALA ALA
SEQRES 54 D 1407 ASN ASP ARG VAL SER LYS ALA MET MET ASP ASN LEU GLN
SEQRES 55 D 1407 THR GLU THR VAL ILE ASN ARG ASP GLY GLN GLU GLU LYS
SEQRES 56 D 1407 GLN VAL SER PHE ASN SER ILE TYR MET MET ALA ASP SER
SEQRES 57 D 1407 GLY ALA ARG GLY SER ALA ALA GLN ILE ARG GLN LEU ALA
SEQRES 58 D 1407 GLY MET ARG GLY LEU MET ALA LYS PRO ASP GLY SER ILE
SEQRES 59 D 1407 ILE GLU THR PRO ILE THR ALA ASN PHE ARG GLU GLY LEU
SEQRES 60 D 1407 ASN VAL LEU GLN TYR PHE ILE SER THR HIS GLY ALA ARG
SEQRES 61 D 1407 LYS GLY LEU ALA ASP THR ALA LEU LYS THR ALA ASN SER
SEQRES 62 D 1407 GLY TYR LEU THR ARG ARG LEU VAL ASP VAL ALA GLN ASP
SEQRES 63 D 1407 LEU VAL VAL THR GLU ASP ASP CYS GLY THR HIS GLU GLY
SEQRES 64 D 1407 ILE MET MET THR PRO VAL ILE GLU GLY GLY ASP VAL LYS
SEQRES 65 D 1407 GLU PRO LEU ARG ASP ARG VAL LEU GLY ARG VAL THR ALA
SEQRES 66 D 1407 GLU ASP VAL LEU LYS PRO GLY THR ALA ASP ILE LEU VAL
SEQRES 67 D 1407 PRO ARG ASN THR LEU LEU HIS GLU GLN TRP CYS ASP LEU
SEQRES 68 D 1407 LEU GLU GLU ASN SER VAL ASP ALA VAL LYS VAL ARG SER
SEQRES 69 D 1407 VAL VAL SER CYS ASP THR ASP PHE GLY VAL CYS ALA HIS
SEQRES 70 D 1407 CYS TYR GLY ARG ASP LEU ALA ARG GLY HIS ILE ILE ASN
SEQRES 71 D 1407 LYS GLY GLU ALA ILE GLY VAL ILE ALA ALA GLN SER ILE
SEQRES 72 D 1407 GLY GLU PRO GLY THR GLN LEU THR MET ARG THR PHE HIS
SEQRES 73 D 1407 ILE GLY GLY ALA ALA SER ARG ALA ALA ALA GLU SER SER
SEQRES 74 D 1407 ILE GLN VAL LYS ASN LYS GLY SER ILE LYS LEU SER ASN
SEQRES 75 D 1407 VAL LYS SER VAL VAL ASN SER SER GLY LYS LEU VAL ILE
SEQRES 76 D 1407 THR SER ARG ASN THR GLU LEU LYS LEU ILE ASP GLU PHE
SEQRES 77 D 1407 GLY ARG THR LYS GLU SER TYR LYS VAL PRO TYR GLY ALA
SEQRES 78 D 1407 VAL LEU ALA LYS GLY ASP GLY GLU GLN VAL ALA GLY GLY
SEQRES 79 D 1407 GLU THR VAL ALA ASN TRP ASP PRO HIS THR MET PRO VAL
SEQRES 80 D 1407 ILE THR GLU VAL SER GLY PHE VAL ARG PHE THR ASP MET
SEQRES 81 D 1407 ILE ASP GLY GLN THR ILE THR ARG GLN THR ASP GLU LEU
SEQRES 82 D 1407 THR GLY LEU SER SER LEU VAL VAL LEU ASP SER ALA GLU
SEQRES 83 D 1407 ARG THR ALA GLY GLY LYS ASP LEU ARG PRO ALA LEU LYS
SEQRES 84 D 1407 ILE VAL ASP ALA GLN GLY ASN ASP VAL LEU ILE PRO GLY
SEQRES 85 D 1407 THR ASP MET PRO ALA GLN TYR PHE LEU PRO GLY LYS ALA
SEQRES 86 D 1407 ILE VAL GLN LEU GLU ASP GLY VAL GLN ILE SER SER GLY
SEQRES 87 D 1407 ASP THR LEU ALA ARG ILE PRO GLN GLU SER GLY GLY THR
SEQRES 88 D 1407 LYS ASP ILE THR GLY GLY LEU PRO ARG VAL ALA ASP LEU
SEQRES 89 D 1407 PHE GLU ALA ARG ARG PRO LYS GLU PRO ALA ILE LEU ALA
SEQRES 90 D 1407 GLU ILE SER GLY ILE VAL SER PHE GLY LYS GLU THR LYS
SEQRES 91 D 1407 GLY LYS ARG ARG LEU VAL ILE THR PRO VAL ASP GLY SER
SEQRES 92 D 1407 ASP PRO TYR GLU GLU MET ILE PRO LYS TRP ARG GLN LEU
SEQRES 93 D 1407 ASN VAL PHE GLU GLY GLU ARG VAL GLU ARG GLY ASP VAL
SEQRES 94 D 1407 ILE SER ASP GLY PRO GLU ALA PRO HIS ASP ILE LEU ARG
SEQRES 95 D 1407 LEU ARG GLY VAL HIS ALA VAL THR ARG TYR ILE VAL ASN
SEQRES 96 D 1407 GLU VAL GLN ASP VAL TYR ARG LEU GLN GLY VAL LYS ILE
SEQRES 97 D 1407 ASN ASP LYS HIS ILE GLU VAL ILE VAL ARG GLN MET LEU
SEQRES 98 D 1407 ARG LYS ALA THR ILE VAL ASN ALA GLY SER SER ASP PHE
SEQRES 99 D 1407 LEU GLU GLY GLU GLN VAL GLU TYR SER ARG VAL LYS ILE
SEQRES 100 D 1407 ALA ASN ARG GLU LEU GLU ALA ASN GLY LYS VAL GLY ALA
SEQRES 101 D 1407 THR TYR SER ARG ASP LEU LEU GLY ILE THR LYS ALA SER
SEQRES 102 D 1407 LEU ALA THR GLU SER PHE ILE SER ALA ALA SER PHE GLN
SEQRES 103 D 1407 GLU THR THR ARG VAL LEU THR GLU ALA ALA VAL ALA GLY
SEQRES 104 D 1407 LYS ARG ASP GLU LEU ARG GLY LEU LYS GLU ASN VAL ILE
SEQRES 105 D 1407 VAL GLY ARG LEU ILE PRO ALA GLY THR GLY TYR ALA TYR
SEQRES 106 D 1407 HIS GLN ASP ARG MET ARG ARG ARG ALA ALA GLY GLU ALA
SEQRES 107 D 1407 PRO ALA ALA PRO GLN VAL THR ALA GLU ASP ALA SER ALA
SEQRES 108 D 1407 SER LEU ALA GLU LEU LEU ASN ALA GLY LEU GLY GLY SER
SEQRES 109 D 1407 ASP ASN GLU
SEQRES 1 E 91 MET ALA ARG VAL THR VAL GLN ASP ALA VAL GLU LYS ILE
SEQRES 2 E 91 GLY ASN ARG PHE ASP LEU VAL LEU VAL ALA ALA ARG ARG
SEQRES 3 E 91 ALA ARG GLN MET GLN VAL GLY GLY LYS ASP PRO LEU VAL
SEQRES 4 E 91 PRO GLU GLU ASN ASP LYS THR THR VAL ILE ALA LEU ARG
SEQRES 5 E 91 GLU ILE GLU GLU GLY LEU ILE ASN ASN GLN ILE LEU ASP
SEQRES 6 E 91 VAL ARG GLU ARG GLN GLU GLN GLN GLU GLN GLU ALA ALA
SEQRES 7 E 91 GLU LEU GLN ALA VAL THR ALA ILE ALA GLU GLY ARG ARG
SEQRES 1 F 522 GLY ARG THR THR ASP PRO VAL ARG MET TYR MET ARG GLU
SEQRES 2 F 522 MET GLY THR VAL GLU LEU LEU THR ARG GLU GLY GLU ILE
SEQRES 3 F 522 ASP ILE ALA LYS ARG ILE GLU ASP GLY ILE ASN GLN VAL
SEQRES 4 F 522 GLN CYS SER VAL ALA GLU TYR PRO GLU ALA ILE THR TYR
SEQRES 5 F 522 LEU LEU GLU GLN TYR ASP ARG VAL GLU ALA GLU GLU ALA
SEQRES 6 F 522 ARG LEU SER ASP LEU ILE THR GLY PHE VAL ASP PRO ASN
SEQRES 7 F 522 ALA GLU GLU ASP LEU ALA PRO THR ALA THR HIS VAL GLY
SEQRES 8 F 522 SER GLU LEU SER GLN GLU ASP LEU ASP ASP ASP GLU ASP
SEQRES 9 F 522 GLU ASP GLU GLU ASP GLY ASP ASP ASP SER ALA ASP ASP
SEQRES 10 F 522 ASP ASN SER ILE ASP PRO GLU LEU ALA ARG GLU LYS PHE
SEQRES 11 F 522 ALA GLU LEU ARG ALA GLN TYR VAL VAL THR ARG ASP THR
SEQRES 12 F 522 ILE LYS ALA LYS GLY ARG SER HIS ALA THR ALA GLN GLU
SEQRES 13 F 522 GLU ILE LEU LYS LEU SER GLU VAL PHE LYS GLN PHE ARG
SEQRES 14 F 522 LEU VAL PRO LYS GLN PHE ASP TYR LEU VAL ASN SER MET
SEQRES 15 F 522 ARG VAL MET MET ASP ARG VAL ARG THR GLN GLU ARG LEU
SEQRES 16 F 522 ILE MET LYS LEU CYS VAL GLU GLN CYS LYS MET PRO LYS
SEQRES 17 F 522 LYS ASN PHE ILE THR LEU PHE THR GLY ASN GLU THR SER
SEQRES 18 F 522 ASP THR TRP PHE ASN ALA ALA ILE ALA MET ASN LYS PRO
SEQRES 19 F 522 TRP SER GLU LYS LEU HIS ASP VAL SER GLU GLU VAL HIS
SEQRES 20 F 522 ARG ALA LEU GLN LYS LEU GLN GLN ILE GLU GLU GLU THR
SEQRES 21 F 522 GLY LEU THR ILE GLU GLN VAL LYS ASP ILE ASN ARG ARG
SEQRES 22 F 522 MET SER ILE GLY GLU ALA LYS ALA ARG ARG ALA LYS LYS
SEQRES 23 F 522 GLU MET VAL GLU ALA ASN LEU ARG LEU VAL ILE SER ILE
SEQRES 24 F 522 ALA LYS LYS TYR THR ASN ARG GLY LEU GLN PHE LEU ASP
SEQRES 25 F 522 LEU ILE GLN GLU GLY ASN ILE GLY LEU MET LYS ALA VAL
SEQRES 26 F 522 ASP LYS PHE GLU TYR ARG ARG GLY TYR LYS PHE SER THR
SEQRES 27 F 522 TYR ALA THR TRP TRP ILE ARG GLN ALA ILE THR ARG SER
SEQRES 28 F 522 ILE ALA ASP GLN ALA ARG THR ILE ARG ILE PRO VAL HIS
SEQRES 29 F 522 MET ILE GLU THR ILE ASN LYS LEU ASN ARG ILE SER ARG
SEQRES 30 F 522 GLN MET LEU GLN GLU MET GLY ARG GLU PRO THR PRO GLU
SEQRES 31 F 522 GLU LEU ALA GLU ARG MET LEU MET PRO GLU ASP LYS ILE
SEQRES 32 F 522 ARG LYS VAL LEU LYS ILE ALA LYS GLU PRO ILE SER MET
SEQRES 33 F 522 GLU THR PRO ILE GLY ASP ASP GLU ASP SER HIS LEU GLY
SEQRES 34 F 522 ASP PHE ILE GLU ASP THR THR LEU GLU LEU PRO LEU ASP
SEQRES 35 F 522 SER ALA THR THR GLU SER LEU ARG ALA ALA THR HIS ASP
SEQRES 36 F 522 VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS VAL LEU
SEQRES 37 F 522 ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP TYR THR
SEQRES 38 F 522 LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR ARG GLU
SEQRES 39 F 522 ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG LYS LEU
SEQRES 40 F 522 ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER PHE LEU
SEQRES 41 F 522 ASP ASP
SEQRES 1 G 239 MET GLN GLY SER VAL THR GLU PHE LEU LYS PRO ARG LEU
SEQRES 2 G 239 VAL ASP ILE GLU GLN VAL SER SER THR HIS ALA LYS VAL
SEQRES 3 G 239 THR LEU GLU PRO LEU GLU ARG GLY PHE GLY HIS THR LEU
SEQRES 4 G 239 GLY ASN ALA LEU ARG ARG ILE LEU LEU SER SER MET PRO
SEQRES 5 G 239 GLY CYS ALA VAL THR GLU VAL GLU ILE ASP GLY VAL LEU
SEQRES 6 G 239 HIS GLU TYR SER THR LYS GLU GLY VAL GLN GLU ASP ILE
SEQRES 7 G 239 LEU GLU ILE LEU LEU ASN LEU LYS GLY LEU ALA VAL ARG
SEQRES 8 G 239 VAL GLN GLY LYS ASP GLU VAL ILE LEU THR LEU ASN LYS
SEQRES 9 G 239 SER GLY ILE GLY PRO VAL THR ALA ALA ASP ILE THR HIS
SEQRES 10 G 239 ASP GLY ASP VAL GLU ILE VAL LYS PRO GLN HIS VAL ILE
SEQRES 11 G 239 CYS HIS LEU THR ASP GLU ASN ALA SER ILE SER MET ARG
SEQRES 12 G 239 ILE LYS VAL GLN ARG GLY ARG GLY TYR VAL PRO ALA SER
SEQRES 13 G 239 THR ARG ILE HIS SER GLU GLU ASP GLU ARG PRO ILE GLY
SEQRES 14 G 239 ARG LEU LEU VAL ASP ALA CYS TYR SER PRO VAL GLU ARG
SEQRES 15 G 239 ILE ALA TYR ASN VAL GLU ALA ALA ARG VAL GLU GLN ARG
SEQRES 16 G 239 THR ASP LEU ASP LYS LEU VAL ILE GLU MET GLU THR ASN
SEQRES 17 G 239 GLY THR ILE ASP PRO GLU GLU ALA ILE ARG ARG ALA ALA
SEQRES 18 G 239 THR ILE LEU ALA GLU GLN LEU GLU ALA PHE VAL ASP LEU
SEQRES 19 G 239 GLU VAL LEU PHE GLN
SEQRES 1 H 239 MET GLN GLY SER VAL THR GLU PHE LEU LYS PRO ARG LEU
SEQRES 2 H 239 VAL ASP ILE GLU GLN VAL SER SER THR HIS ALA LYS VAL
SEQRES 3 H 239 THR LEU GLU PRO LEU GLU ARG GLY PHE GLY HIS THR LEU
SEQRES 4 H 239 GLY ASN ALA LEU ARG ARG ILE LEU LEU SER SER MET PRO
SEQRES 5 H 239 GLY CYS ALA VAL THR GLU VAL GLU ILE ASP GLY VAL LEU
SEQRES 6 H 239 HIS GLU TYR SER THR LYS GLU GLY VAL GLN GLU ASP ILE
SEQRES 7 H 239 LEU GLU ILE LEU LEU ASN LEU LYS GLY LEU ALA VAL ARG
SEQRES 8 H 239 VAL GLN GLY LYS ASP GLU VAL ILE LEU THR LEU ASN LYS
SEQRES 9 H 239 SER GLY ILE GLY PRO VAL THR ALA ALA ASP ILE THR HIS
SEQRES 10 H 239 ASP GLY ASP VAL GLU ILE VAL LYS PRO GLN HIS VAL ILE
SEQRES 11 H 239 CYS HIS LEU THR ASP GLU ASN ALA SER ILE SER MET ARG
SEQRES 12 H 239 ILE LYS VAL GLN ARG GLY ARG GLY TYR VAL PRO ALA SER
SEQRES 13 H 239 THR ARG ILE HIS SER GLU GLU ASP GLU ARG PRO ILE GLY
SEQRES 14 H 239 ARG LEU LEU VAL ASP ALA CYS TYR SER PRO VAL GLU ARG
SEQRES 15 H 239 ILE ALA TYR ASN VAL GLU ALA ALA ARG VAL GLU GLN ARG
SEQRES 16 H 239 THR ASP LEU ASP LYS LEU VAL ILE GLU MET GLU THR ASN
SEQRES 17 H 239 GLY THR ILE ASP PRO GLU GLU ALA ILE ARG ARG ALA ALA
SEQRES 18 H 239 THR ILE LEU ALA GLU GLN LEU GLU ALA PHE VAL ASP LEU
SEQRES 19 H 239 GLU VAL LEU PHE GLN
SEQRES 1 I 1342 MET VAL TYR SER TYR THR GLU LYS LYS ARG ILE ARG LYS
SEQRES 2 I 1342 ASP PHE GLY LYS ARG PRO GLN VAL LEU ASP VAL PRO TYR
SEQRES 3 I 1342 LEU LEU SER ILE GLN LEU ASP SER PHE GLN LYS PHE ILE
SEQRES 4 I 1342 GLU GLN ASP PRO GLU GLY GLN TYR GLY LEU GLU ALA ALA
SEQRES 5 I 1342 PHE ARG SER VAL PHE PRO ILE GLN SER TYR SER GLY ASN
SEQRES 6 I 1342 SER GLU LEU GLN TYR VAL SER TYR ARG LEU GLY GLU PRO
SEQRES 7 I 1342 VAL PHE ASP VAL GLN GLU CYS GLN ILE ARG GLY VAL THR
SEQRES 8 I 1342 TYR SER ALA PRO LEU ARG VAL LYS LEU ARG LEU VAL ILE
SEQRES 9 I 1342 TYR GLU ARG GLU ALA PRO GLU GLY THR VAL LYS ASP ILE
SEQRES 10 I 1342 LYS GLU GLN GLU VAL TYR MET GLY GLU ILE PRO LEU MET
SEQRES 11 I 1342 THR ASP ASN GLY THR PHE VAL ILE ASN GLY THR GLU ARG
SEQRES 12 I 1342 VAL ILE VAL SER GLN LEU HIS ARG SER PRO GLY VAL PHE
SEQRES 13 I 1342 PHE ASP SER ASP LYS GLY LYS THR HIS SER SER GLY LYS
SEQRES 14 I 1342 VAL LEU TYR ASN ALA ARG ILE ILE PRO TYR ARG GLY SER
SEQRES 15 I 1342 TRP LEU ASP PHE GLU PHE ASP PRO LYS ASP ASN LEU PHE
SEQRES 16 I 1342 VAL ARG ILE ASP ARG ARG ARG LYS LEU PRO ALA THR ILE
SEQRES 17 I 1342 ILE LEU ARG ALA LEU ASN TYR THR THR GLU GLN ILE LEU
SEQRES 18 I 1342 ASP LEU PHE PHE GLU LYS VAL ILE PHE GLU ILE ARG ASP
SEQRES 19 I 1342 ASN LYS LEU GLN MET GLU LEU VAL PRO GLU ARG LEU ARG
SEQRES 20 I 1342 GLY GLU THR ALA SER PHE ASP ILE GLU ALA ASN GLY LYS
SEQRES 21 I 1342 VAL TYR VAL GLU LYS GLY ARG ARG ILE THR ALA ARG HIS
SEQRES 22 I 1342 ILE ARG GLN LEU GLU LYS ASP ASP VAL LYS LEU ILE GLU
SEQRES 23 I 1342 VAL PRO VAL GLU TYR ILE ALA GLY LYS VAL VAL ALA LYS
SEQRES 24 I 1342 ASP TYR ILE ASP GLU SER THR GLY GLU LEU ILE CYS ALA
SEQRES 25 I 1342 ALA ASN MET GLU LEU SER LEU ASP LEU LEU ALA LYS LEU
SEQRES 26 I 1342 SER GLN SER GLY HIS LYS ARG ILE GLU THR LEU PHE THR
SEQRES 27 I 1342 ASN ASP LEU ASP HIS GLY PRO TYR ILE SER GLU THR LEU
SEQRES 28 I 1342 ARG VAL ASP PRO THR ASN ASP ARG LEU SER ALA LEU VAL
SEQRES 29 I 1342 GLU ILE TYR ARG MET MET ARG PRO GLY GLU PRO PRO THR
SEQRES 30 I 1342 ARG GLU ALA ALA GLU SER LEU PHE GLU ASN LEU PHE PHE
SEQRES 31 I 1342 SER GLU ASP ARG TYR ASP LEU SER ALA VAL GLY ARG MET
SEQRES 32 I 1342 LYS PHE ASN ARG SER LEU LEU ARG GLU GLU ILE GLU GLY
SEQRES 33 I 1342 SER GLY ILE LEU SER LYS ASP ASP ILE ILE ASP VAL MET
SEQRES 34 I 1342 LYS LYS LEU ILE ASP ILE ARG ASN GLY LYS GLY GLU VAL
SEQRES 35 I 1342 ASP ASP ILE ASP HIS LEU GLY ASN ARG ARG ILE ARG SER
SEQRES 36 I 1342 VAL GLY GLU MET ALA GLU ASN GLN PHE ARG VAL GLY LEU
SEQRES 37 I 1342 VAL ARG VAL GLU ARG ALA VAL LYS GLU ARG LEU SER LEU
SEQRES 38 I 1342 GLY ASP LEU ASP THR LEU MET PRO GLN ASP MET ILE ASN
SEQRES 39 I 1342 ALA LYS PRO ILE SER ALA ALA VAL LYS GLU PHE PHE GLY
SEQRES 40 I 1342 SER SER GLN LEU SER GLN PHE MET ASP GLN ASN ASN PRO
SEQRES 41 I 1342 LEU SER GLU ILE THR HIS LYS ARG ARG ILE SER ALA LEU
SEQRES 42 I 1342 GLY PRO GLY GLY LEU THR ARG GLU ARG ALA GLY PHE GLU
SEQRES 43 I 1342 VAL ARG ASP VAL HIS PRO THR HIS TYR GLY ARG VAL CYS
SEQRES 44 I 1342 PRO ILE GLU THR PRO GLU GLY PRO ASN ILE GLY LEU ILE
SEQRES 45 I 1342 ASN SER LEU SER VAL TYR ALA GLN THR ASN GLU TYR GLY
SEQRES 46 I 1342 PHE LEU GLU THR PRO TYR ARG LYS VAL THR ASP GLY VAL
SEQRES 47 I 1342 VAL THR ASP GLU ILE HIS TYR LEU SER ALA ILE GLU GLU
SEQRES 48 I 1342 GLY ASN TYR VAL ILE ALA GLN ALA ASN SER ASN LEU ASP
SEQRES 49 I 1342 GLU GLU GLY HIS PHE VAL GLU ASP LEU VAL THR CYS ARG
SEQRES 50 I 1342 SER LYS GLY GLU SER SER LEU PHE SER ARG ASP GLN VAL
SEQRES 51 I 1342 ASP TYR MET ASP VAL SER THR GLN GLN VAL VAL SER VAL
SEQRES 52 I 1342 GLY ALA SER LEU ILE PRO PHE LEU GLU HIS ASP ASP ALA
SEQRES 53 I 1342 ASN ARG ALA LEU MET GLY ALA ASN MET GLN ARG GLN ALA
SEQRES 54 I 1342 VAL PRO THR LEU ARG ALA ASP LYS PRO LEU VAL GLY THR
SEQRES 55 I 1342 GLY MET GLU ARG ALA VAL ALA VAL ASP SER GLY VAL THR
SEQRES 56 I 1342 ALA VAL ALA LYS ARG GLY GLY VAL VAL GLN TYR VAL ASP
SEQRES 57 I 1342 ALA SER ARG ILE VAL ILE LYS VAL ASN GLU ASP GLU MET
SEQRES 58 I 1342 TYR PRO GLY GLU ALA GLY ILE ASP ILE TYR ASN LEU THR
SEQRES 59 I 1342 LYS TYR THR ARG SER ASN GLN ASN THR CYS ILE ASN GLN
SEQRES 60 I 1342 MET PRO CYS VAL SER LEU GLY GLU PRO VAL GLU ARG GLY
SEQRES 61 I 1342 ASP VAL LEU ALA ASP GLY PRO SER THR ASP LEU GLY GLU
SEQRES 62 I 1342 LEU ALA LEU GLY GLN ASN MET ARG VAL ALA PHE MET PRO
SEQRES 63 I 1342 TRP ASN GLY TYR ASN PHE GLU ASP SER ILE LEU VAL SER
SEQRES 64 I 1342 GLU ARG VAL VAL GLN GLU ASP ARG PHE THR THR ILE HIS
SEQRES 65 I 1342 ILE GLN GLU LEU ALA CYS VAL SER ARG ASP THR LYS LEU
SEQRES 66 I 1342 GLY PRO GLU GLU ILE THR ALA ASP ILE PRO ASN VAL GLY
SEQRES 67 I 1342 GLU ALA ALA LEU SER LYS LEU ASP GLU SER GLY ILE VAL
SEQRES 68 I 1342 TYR ILE GLY ALA GLU VAL THR GLY GLY ASP ILE LEU VAL
SEQRES 69 I 1342 GLY LYS VAL THR PRO LYS GLY GLU THR GLN LEU THR PRO
SEQRES 70 I 1342 GLU GLU LYS LEU LEU ARG ALA ILE PHE GLY GLU LYS ALA
SEQRES 71 I 1342 SER ASP VAL LYS ASP SER SER LEU ARG VAL PRO ASN GLY
SEQRES 72 I 1342 VAL SER GLY THR VAL ILE ASP VAL GLN VAL PHE THR ARG
SEQRES 73 I 1342 ASP GLY VAL GLU LYS ASP LYS ARG ALA LEU GLU ILE GLU
SEQRES 74 I 1342 GLU MET GLN LEU LYS GLN ALA LYS LYS ASP LEU SER GLU
SEQRES 75 I 1342 GLU LEU GLN ILE LEU GLU ALA GLY LEU PHE SER ARG ILE
SEQRES 76 I 1342 ARG ALA VAL LEU VAL ALA GLY GLY VAL GLU ALA GLU LYS
SEQRES 77 I 1342 LEU ASP LYS LEU PRO ARG ASP ARG TRP LEU GLU LEU GLY
SEQRES 78 I 1342 LEU THR ASP GLU GLU LYS GLN ASN GLN LEU GLU GLN LEU
SEQRES 79 I 1342 ALA GLU GLN TYR ASP GLU LEU LYS HIS GLU PHE GLU LYS
SEQRES 80 I 1342 LYS LEU GLU ALA LYS ARG ARG LYS ILE THR GLN GLY ASP
SEQRES 81 I 1342 ASP LEU ALA PRO GLY VAL LEU LYS ILE VAL LYS VAL TYR
SEQRES 82 I 1342 LEU ALA VAL LYS ARG ARG ILE GLN PRO GLY ASP LYS MET
SEQRES 83 I 1342 ALA GLY ARG HIS GLY ASN LYS GLY VAL ILE SER LYS ILE
SEQRES 84 I 1342 ASN PRO ILE GLU ASP MET PRO TYR ASP GLU ASN GLY THR
SEQRES 85 I 1342 PRO VAL ASP ILE VAL LEU ASN PRO LEU GLY VAL PRO SER
SEQRES 86 I 1342 ARG MET ASN ILE GLY GLN ILE LEU GLU THR HIS LEU GLY
SEQRES 87 I 1342 MET ALA ALA LYS GLY ILE GLY ASP LYS ILE ASN ALA MET
SEQRES 88 I 1342 LEU LYS GLN GLN GLN GLU VAL ALA LYS LEU ARG GLU PHE
SEQRES 89 I 1342 ILE GLN ARG ALA TYR ASP LEU GLY ALA ASP VAL ARG GLN
SEQRES 90 I 1342 LYS VAL ASP LEU SER THR PHE SER ASP GLU GLU VAL MET
SEQRES 91 I 1342 ARG LEU ALA GLU ASN LEU ARG LYS GLY MET PRO ILE ALA
SEQRES 92 I 1342 THR PRO VAL PHE ASP GLY ALA LYS GLU ALA GLU ILE LYS
SEQRES 93 I 1342 GLU LEU LEU LYS LEU GLY ASP LEU PRO THR SER GLY GLN
SEQRES 94 I 1342 ILE ARG LEU TYR ASP GLY ARG THR GLY GLU GLN PHE GLU
SEQRES 95 I 1342 ARG PRO VAL THR VAL GLY TYR MET TYR MET LEU LYS LEU
SEQRES 96 I 1342 ASN HIS LEU VAL ASP ASP LYS MET HIS ALA ARG SER THR
SEQRES 97 I 1342 GLY SER TYR SER LEU VAL THR GLN GLN PRO LEU GLY GLY
SEQRES 98 I 1342 LYS ALA GLN PHE GLY GLY GLN ARG PHE GLY GLU MET GLU
SEQRES 99 I 1342 VAL TRP ALA LEU GLU ALA TYR GLY ALA ALA TYR THR LEU
SEQRES 100 I 1342 GLN GLU MET LEU THR VAL LYS SER ASP ASP VAL ASN GLY
SEQRES 101 I 1342 ARG THR LYS MET TYR LYS ASN ILE VAL ASP GLY ASN HIS
SEQRES 102 I 1342 GLN MET GLU PRO GLY MET PRO GLU SER PHE ASN VAL LEU
SEQRES 103 I 1342 LEU LYS GLU ILE ARG SER LEU GLY ILE ASN ILE GLU LEU
SEQRES 104 I 1342 GLU ASP GLU
SEQRES 1 J 1407 MET LYS ASP LEU LEU LYS PHE LEU LYS ALA GLN THR LYS
SEQRES 2 J 1407 THR GLU GLU PHE ASP ALA ILE LYS ILE ALA LEU ALA SER
SEQRES 3 J 1407 PRO ASP MET ILE ARG SER TRP SER PHE GLY GLU VAL LYS
SEQRES 4 J 1407 LYS PRO GLU THR ILE ASN TYR ARG THR PHE LYS PRO GLU
SEQRES 5 J 1407 ARG ASP GLY LEU PHE CYS ALA ARG ILE PHE GLY PRO VAL
SEQRES 6 J 1407 LYS ASP TYR GLU CYS LEU CYS GLY LYS TYR LYS ARG LEU
SEQRES 7 J 1407 LYS HIS ARG GLY VAL ILE CYS GLU LYS CYS GLY VAL GLU
SEQRES 8 J 1407 VAL THR GLN THR LYS VAL ARG ARG GLU ARG MET GLY HIS
SEQRES 9 J 1407 ILE GLU LEU ALA SER PRO THR ALA HIS ILE TRP PHE LEU
SEQRES 10 J 1407 LYS SER LEU PRO SER ARG ILE GLY LEU LEU LEU ASP MET
SEQRES 11 J 1407 PRO LEU ARG ASP ILE GLU ARG VAL LEU TYR PHE GLU SER
SEQRES 12 J 1407 TYR VAL VAL ILE GLU GLY GLY MET THR ASN LEU GLU ARG
SEQRES 13 J 1407 GLN GLN ILE LEU THR GLU GLU GLN TYR LEU ASP ALA LEU
SEQRES 14 J 1407 GLU GLU PHE GLY ASP GLU PHE ASP ALA LYS MET GLY ALA
SEQRES 15 J 1407 GLU ALA ILE GLN ALA LEU LEU LYS SER MET ASP LEU GLU
SEQRES 16 J 1407 GLN GLU CYS GLU GLN LEU ARG GLU GLU LEU ASN GLU THR
SEQRES 17 J 1407 ASN SER GLU THR LYS ARG LYS LYS LEU THR LYS ARG ILE
SEQRES 18 J 1407 LYS LEU LEU GLU ALA PHE VAL GLN SER GLY ASN LYS PRO
SEQRES 19 J 1407 GLU TRP MET ILE LEU THR VAL LEU PRO VAL LEU PRO PRO
SEQRES 20 J 1407 ASP LEU ARG PRO LEU VAL PRO LEU ASP GLY GLY ARG PHE
SEQRES 21 J 1407 ALA THR SER ASP LEU ASN ASP LEU TYR ARG ARG VAL ILE
SEQRES 22 J 1407 ASN ARG ASN ASN ARG LEU LYS ARG LEU LEU ASP LEU ALA
SEQRES 23 J 1407 ALA PRO ASP ILE ILE VAL ARG ASN GLU LYS ARG MET LEU
SEQRES 24 J 1407 GLN GLU ALA VAL ASP ALA LEU LEU ASP ASN GLY ARG ARG
SEQRES 25 J 1407 GLY ARG ALA ILE THR GLY SER ASN LYS ARG PRO LEU LYS
SEQRES 26 J 1407 SER LEU ALA ASP MET ILE LYS GLY LYS GLN GLY ARG PHE
SEQRES 27 J 1407 ARG GLN ASN LEU LEU GLY LYS ARG VAL ASP TYR SER GLY
SEQRES 28 J 1407 ARG SER VAL ILE THR VAL GLY PRO TYR LEU ARG LEU HIS
SEQRES 29 J 1407 GLN CYS GLY LEU PRO LYS LYS MET ALA LEU GLU LEU PHE
SEQRES 30 J 1407 LYS PRO PHE ILE TYR GLY LYS LEU GLU LEU ARG GLY LEU
SEQRES 31 J 1407 ALA THR THR ILE LYS ALA ALA LYS LYS MET VAL GLU ARG
SEQRES 32 J 1407 GLU GLU ALA VAL VAL TRP ASP ILE LEU ASP GLU VAL ILE
SEQRES 33 J 1407 ARG GLU HIS PRO VAL LEU LEU ASN ARG ALA PRO THR LEU
SEQRES 34 J 1407 HIS ARG LEU GLY ILE GLN ALA PHE GLU PRO VAL LEU ILE
SEQRES 35 J 1407 GLU GLY LYS ALA ILE GLN LEU HIS PRO LEU VAL CYS ALA
SEQRES 36 J 1407 ALA TYR ASN ALA ASP PHE ASP GLY ASP GLN MET ALA VAL
SEQRES 37 J 1407 HIS VAL PRO LEU THR LEU GLU ALA GLN LEU GLU ALA ARG
SEQRES 38 J 1407 ALA LEU MET MET SER THR ASN ASN ILE LEU SER PRO ALA
SEQRES 39 J 1407 ASN GLY GLU PRO ILE ILE VAL PRO SER GLN ASP VAL VAL
SEQRES 40 J 1407 LEU GLY LEU TYR TYR MET THR ARG ASP CYS VAL ASN ALA
SEQRES 41 J 1407 LYS GLY GLU GLY MET VAL LEU THR GLY PRO LYS GLU ALA
SEQRES 42 J 1407 GLU ARG LEU TYR ARG SER GLY LEU ALA SER LEU HIS ALA
SEQRES 43 J 1407 ARG VAL LYS VAL ARG ILE THR GLU TYR GLU LYS ASP ALA
SEQRES 44 J 1407 ASN GLY GLU LEU VAL ALA LYS THR SER LEU LYS ASP THR
SEQRES 45 J 1407 THR VAL GLY ARG ALA ILE LEU TRP MET ILE VAL PRO LYS
SEQRES 46 J 1407 GLY LEU PRO TYR SER ILE VAL ASN GLN ALA LEU GLY LYS
SEQRES 47 J 1407 LYS ALA ILE SER LYS MET LEU ASN THR CYS TYR ARG ILE
SEQRES 48 J 1407 LEU GLY LEU LYS PRO THR VAL ILE PHE ALA ASP GLN ILE
SEQRES 49 J 1407 MET TYR THR GLY PHE ALA TYR ALA ALA ARG SER GLY ALA
SEQRES 50 J 1407 SER VAL GLY ILE ASP ASP MET VAL ILE PRO GLU LYS LYS
SEQRES 51 J 1407 HIS GLU ILE ILE SER GLU ALA GLU ALA GLU VAL ALA GLU
SEQRES 52 J 1407 ILE GLN GLU GLN PHE GLN SER GLY LEU VAL THR ALA GLY
SEQRES 53 J 1407 GLU ARG TYR ASN LYS VAL ILE ASP ILE TRP ALA ALA ALA
SEQRES 54 J 1407 ASN ASP ARG VAL SER LYS ALA MET MET ASP ASN LEU GLN
SEQRES 55 J 1407 THR GLU THR VAL ILE ASN ARG ASP GLY GLN GLU GLU LYS
SEQRES 56 J 1407 GLN VAL SER PHE ASN SER ILE TYR MET MET ALA ASP SER
SEQRES 57 J 1407 GLY ALA ARG GLY SER ALA ALA GLN ILE ARG GLN LEU ALA
SEQRES 58 J 1407 GLY MET ARG GLY LEU MET ALA LYS PRO ASP GLY SER ILE
SEQRES 59 J 1407 ILE GLU THR PRO ILE THR ALA ASN PHE ARG GLU GLY LEU
SEQRES 60 J 1407 ASN VAL LEU GLN TYR PHE ILE SER THR HIS GLY ALA ARG
SEQRES 61 J 1407 LYS GLY LEU ALA ASP THR ALA LEU LYS THR ALA ASN SER
SEQRES 62 J 1407 GLY TYR LEU THR ARG ARG LEU VAL ASP VAL ALA GLN ASP
SEQRES 63 J 1407 LEU VAL VAL THR GLU ASP ASP CYS GLY THR HIS GLU GLY
SEQRES 64 J 1407 ILE MET MET THR PRO VAL ILE GLU GLY GLY ASP VAL LYS
SEQRES 65 J 1407 GLU PRO LEU ARG ASP ARG VAL LEU GLY ARG VAL THR ALA
SEQRES 66 J 1407 GLU ASP VAL LEU LYS PRO GLY THR ALA ASP ILE LEU VAL
SEQRES 67 J 1407 PRO ARG ASN THR LEU LEU HIS GLU GLN TRP CYS ASP LEU
SEQRES 68 J 1407 LEU GLU GLU ASN SER VAL ASP ALA VAL LYS VAL ARG SER
SEQRES 69 J 1407 VAL VAL SER CYS ASP THR ASP PHE GLY VAL CYS ALA HIS
SEQRES 70 J 1407 CYS TYR GLY ARG ASP LEU ALA ARG GLY HIS ILE ILE ASN
SEQRES 71 J 1407 LYS GLY GLU ALA ILE GLY VAL ILE ALA ALA GLN SER ILE
SEQRES 72 J 1407 GLY GLU PRO GLY THR GLN LEU THR MET ARG THR PHE HIS
SEQRES 73 J 1407 ILE GLY GLY ALA ALA SER ARG ALA ALA ALA GLU SER SER
SEQRES 74 J 1407 ILE GLN VAL LYS ASN LYS GLY SER ILE LYS LEU SER ASN
SEQRES 75 J 1407 VAL LYS SER VAL VAL ASN SER SER GLY LYS LEU VAL ILE
SEQRES 76 J 1407 THR SER ARG ASN THR GLU LEU LYS LEU ILE ASP GLU PHE
SEQRES 77 J 1407 GLY ARG THR LYS GLU SER TYR LYS VAL PRO TYR GLY ALA
SEQRES 78 J 1407 VAL LEU ALA LYS GLY ASP GLY GLU GLN VAL ALA GLY GLY
SEQRES 79 J 1407 GLU THR VAL ALA ASN TRP ASP PRO HIS THR MET PRO VAL
SEQRES 80 J 1407 ILE THR GLU VAL SER GLY PHE VAL ARG PHE THR ASP MET
SEQRES 81 J 1407 ILE ASP GLY GLN THR ILE THR ARG GLN THR ASP GLU LEU
SEQRES 82 J 1407 THR GLY LEU SER SER LEU VAL VAL LEU ASP SER ALA GLU
SEQRES 83 J 1407 ARG THR ALA GLY GLY LYS ASP LEU ARG PRO ALA LEU LYS
SEQRES 84 J 1407 ILE VAL ASP ALA GLN GLY ASN ASP VAL LEU ILE PRO GLY
SEQRES 85 J 1407 THR ASP MET PRO ALA GLN TYR PHE LEU PRO GLY LYS ALA
SEQRES 86 J 1407 ILE VAL GLN LEU GLU ASP GLY VAL GLN ILE SER SER GLY
SEQRES 87 J 1407 ASP THR LEU ALA ARG ILE PRO GLN GLU SER GLY GLY THR
SEQRES 88 J 1407 LYS ASP ILE THR GLY GLY LEU PRO ARG VAL ALA ASP LEU
SEQRES 89 J 1407 PHE GLU ALA ARG ARG PRO LYS GLU PRO ALA ILE LEU ALA
SEQRES 90 J 1407 GLU ILE SER GLY ILE VAL SER PHE GLY LYS GLU THR LYS
SEQRES 91 J 1407 GLY LYS ARG ARG LEU VAL ILE THR PRO VAL ASP GLY SER
SEQRES 92 J 1407 ASP PRO TYR GLU GLU MET ILE PRO LYS TRP ARG GLN LEU
SEQRES 93 J 1407 ASN VAL PHE GLU GLY GLU ARG VAL GLU ARG GLY ASP VAL
SEQRES 94 J 1407 ILE SER ASP GLY PRO GLU ALA PRO HIS ASP ILE LEU ARG
SEQRES 95 J 1407 LEU ARG GLY VAL HIS ALA VAL THR ARG TYR ILE VAL ASN
SEQRES 96 J 1407 GLU VAL GLN ASP VAL TYR ARG LEU GLN GLY VAL LYS ILE
SEQRES 97 J 1407 ASN ASP LYS HIS ILE GLU VAL ILE VAL ARG GLN MET LEU
SEQRES 98 J 1407 ARG LYS ALA THR ILE VAL ASN ALA GLY SER SER ASP PHE
SEQRES 99 J 1407 LEU GLU GLY GLU GLN VAL GLU TYR SER ARG VAL LYS ILE
SEQRES 100 J 1407 ALA ASN ARG GLU LEU GLU ALA ASN GLY LYS VAL GLY ALA
SEQRES 101 J 1407 THR TYR SER ARG ASP LEU LEU GLY ILE THR LYS ALA SER
SEQRES 102 J 1407 LEU ALA THR GLU SER PHE ILE SER ALA ALA SER PHE GLN
SEQRES 103 J 1407 GLU THR THR ARG VAL LEU THR GLU ALA ALA VAL ALA GLY
SEQRES 104 J 1407 LYS ARG ASP GLU LEU ARG GLY LEU LYS GLU ASN VAL ILE
SEQRES 105 J 1407 VAL GLY ARG LEU ILE PRO ALA GLY THR GLY TYR ALA TYR
SEQRES 106 J 1407 HIS GLN ASP ARG MET ARG ARG ARG ALA ALA GLY GLU ALA
SEQRES 107 J 1407 PRO ALA ALA PRO GLN VAL THR ALA GLU ASP ALA SER ALA
SEQRES 108 J 1407 SER LEU ALA GLU LEU LEU ASN ALA GLY LEU GLY GLY SER
SEQRES 109 J 1407 ASP ASN GLU
SEQRES 1 K 91 MET ALA ARG VAL THR VAL GLN ASP ALA VAL GLU LYS ILE
SEQRES 2 K 91 GLY ASN ARG PHE ASP LEU VAL LEU VAL ALA ALA ARG ARG
SEQRES 3 K 91 ALA ARG GLN MET GLN VAL GLY GLY LYS ASP PRO LEU VAL
SEQRES 4 K 91 PRO GLU GLU ASN ASP LYS THR THR VAL ILE ALA LEU ARG
SEQRES 5 K 91 GLU ILE GLU GLU GLY LEU ILE ASN ASN GLN ILE LEU ASP
SEQRES 6 K 91 VAL ARG GLU ARG GLN GLU GLN GLN GLU GLN GLU ALA ALA
SEQRES 7 K 91 GLU LEU GLN ALA VAL THR ALA ILE ALA GLU GLY ARG ARG
SEQRES 1 L 522 GLY ARG THR THR ASP PRO VAL ARG MET TYR MET ARG GLU
SEQRES 2 L 522 MET GLY THR VAL GLU LEU LEU THR ARG GLU GLY GLU ILE
SEQRES 3 L 522 ASP ILE ALA LYS ARG ILE GLU ASP GLY ILE ASN GLN VAL
SEQRES 4 L 522 GLN CYS SER VAL ALA GLU TYR PRO GLU ALA ILE THR TYR
SEQRES 5 L 522 LEU LEU GLU GLN TYR ASP ARG VAL GLU ALA GLU GLU ALA
SEQRES 6 L 522 ARG LEU SER ASP LEU ILE THR GLY PHE VAL ASP PRO ASN
SEQRES 7 L 522 ALA GLU GLU ASP LEU ALA PRO THR ALA THR HIS VAL GLY
SEQRES 8 L 522 SER GLU LEU SER GLN GLU ASP LEU ASP ASP ASP GLU ASP
SEQRES 9 L 522 GLU ASP GLU GLU ASP GLY ASP ASP ASP SER ALA ASP ASP
SEQRES 10 L 522 ASP ASN SER ILE ASP PRO GLU LEU ALA ARG GLU LYS PHE
SEQRES 11 L 522 ALA GLU LEU ARG ALA GLN TYR VAL VAL THR ARG ASP THR
SEQRES 12 L 522 ILE LYS ALA LYS GLY ARG SER HIS ALA THR ALA GLN GLU
SEQRES 13 L 522 GLU ILE LEU LYS LEU SER GLU VAL PHE LYS GLN PHE ARG
SEQRES 14 L 522 LEU VAL PRO LYS GLN PHE ASP TYR LEU VAL ASN SER MET
SEQRES 15 L 522 ARG VAL MET MET ASP ARG VAL ARG THR GLN GLU ARG LEU
SEQRES 16 L 522 ILE MET LYS LEU CYS VAL GLU GLN CYS LYS MET PRO LYS
SEQRES 17 L 522 LYS ASN PHE ILE THR LEU PHE THR GLY ASN GLU THR SER
SEQRES 18 L 522 ASP THR TRP PHE ASN ALA ALA ILE ALA MET ASN LYS PRO
SEQRES 19 L 522 TRP SER GLU LYS LEU HIS ASP VAL SER GLU GLU VAL HIS
SEQRES 20 L 522 ARG ALA LEU GLN LYS LEU GLN GLN ILE GLU GLU GLU THR
SEQRES 21 L 522 GLY LEU THR ILE GLU GLN VAL LYS ASP ILE ASN ARG ARG
SEQRES 22 L 522 MET SER ILE GLY GLU ALA LYS ALA ARG ARG ALA LYS LYS
SEQRES 23 L 522 GLU MET VAL GLU ALA ASN LEU ARG LEU VAL ILE SER ILE
SEQRES 24 L 522 ALA LYS LYS TYR THR ASN ARG GLY LEU GLN PHE LEU ASP
SEQRES 25 L 522 LEU ILE GLN GLU GLY ASN ILE GLY LEU MET LYS ALA VAL
SEQRES 26 L 522 ASP LYS PHE GLU TYR ARG ARG GLY TYR LYS PHE SER THR
SEQRES 27 L 522 TYR ALA THR TRP TRP ILE ARG GLN ALA ILE THR ARG SER
SEQRES 28 L 522 ILE ALA ASP GLN ALA ARG THR ILE ARG ILE PRO VAL HIS
SEQRES 29 L 522 MET ILE GLU THR ILE ASN LYS LEU ASN ARG ILE SER ARG
SEQRES 30 L 522 GLN MET LEU GLN GLU MET GLY ARG GLU PRO THR PRO GLU
SEQRES 31 L 522 GLU LEU ALA GLU ARG MET LEU MET PRO GLU ASP LYS ILE
SEQRES 32 L 522 ARG LYS VAL LEU LYS ILE ALA LYS GLU PRO ILE SER MET
SEQRES 33 L 522 GLU THR PRO ILE GLY ASP ASP GLU ASP SER HIS LEU GLY
SEQRES 34 L 522 ASP PHE ILE GLU ASP THR THR LEU GLU LEU PRO LEU ASP
SEQRES 35 L 522 SER ALA THR THR GLU SER LEU ARG ALA ALA THR HIS ASP
SEQRES 36 L 522 VAL LEU ALA GLY LEU THR ALA ARG GLU ALA LYS VAL LEU
SEQRES 37 L 522 ARG MET ARG PHE GLY ILE ASP MET ASN THR ASP TYR THR
SEQRES 38 L 522 LEU GLU GLU VAL GLY LYS GLN PHE ASP VAL THR ARG GLU
SEQRES 39 L 522 ARG ILE ARG GLN ILE GLU ALA LYS ALA LEU ARG LYS LEU
SEQRES 40 L 522 ARG HIS PRO SER ARG SER GLU VAL LEU ARG SER PHE LEU
SEQRES 41 L 522 ASP ASP
HET MG D1501 1
HET ZN D1502 1
HET ZN D1503 1
HET MG J1501 1
HET ZN J1502 1
HET ZN J1503 1
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
FORMUL 13 MG 2(MG 2+)
FORMUL 14 ZN 4(ZN 2+)
HELIX 1 1 GLY A 34 SER A 50 1 17
HELIX 2 2 ASP A 77 LYS A 86 1 10
HELIX 3 3 ASP A 212 LEU A 228 1 17
HELIX 4 4 GLU A 229 PHE A 231 5 3
HELIX 5 5 GLY B 34 SER B 50 1 17
HELIX 6 6 ASP B 77 GLY B 87 1 11
HELIX 7 7 ALA B 113 ILE B 115 5 3
HELIX 8 8 ASP B 212 LEU B 228 1 17
HELIX 9 9 LEU C 28 ILE C 39 1 12
HELIX 10 10 GLY C 48 PHE C 57 1 10
HELIX 11 11 ASP C 81 GLY C 89 1 9
HELIX 12 12 ALA C 206 LEU C 213 1 8
HELIX 13 13 THR C 216 PHE C 225 1 10
HELIX 14 14 THR C 270 ASP C 281 1 12
HELIX 15 15 GLU C 290 GLY C 294 5 5
HELIX 16 16 SER C 318 GLN C 327 1 10
HELIX 17 17 PRO C 345 VAL C 353 1 9
HELIX 18 18 ASP C 358 ARG C 371 1 14
HELIX 19 19 THR C 377 PHE C 389 1 13
HELIX 20 20 LEU C 397 LEU C 409 1 13
HELIX 21 21 SER C 421 GLY C 438 1 18
HELIX 22 22 SER C 455 LEU C 479 1 25
HELIX 23 23 ALA C 495 SER C 508 1 14
HELIX 24 24 ASN C 519 ARG C 528 1 10
HELIX 25 25 GLY C 544 ASP C 549 1 6
HELIX 26 26 HIS C 551 TYR C 555 5 5
HELIX 27 27 ASP C 648 VAL C 650 5 3
HELIX 28 28 GLY C 664 ILE C 668 5 5
HELIX 29 29 PHE C 670 ASP C 674 5 5
HELIX 30 30 ASP C 675 GLN C 686 1 12
HELIX 31 31 ARG C 687 ALA C 689 5 3
HELIX 32 32 MET C 704 SER C 712 1 9
HELIX 33 33 GLU C 820 GLU C 825 1 6
HELIX 34 34 GLY C 858 LYS C 864 1 7
HELIX 35 35 THR C 896 GLY C 907 1 12
HELIX 36 36 ASP C 942 VAL C 980 1 39
HELIX 37 37 GLU C 985 ASP C 990 1 6
HELIX 38 38 PRO C 993 TRP C 997 5 5
HELIX 39 39 GLU C 1005 GLN C 1038 1 34
HELIX 40 40 PRO C 1081 MET C 1085 5 5
HELIX 41 41 LEU C 1101 ARG C 1106 1 6
HELIX 42 42 ILE C 1109 GLN C 1135 1 27
HELIX 43 43 GLU C 1137 LEU C 1151 1 15
HELIX 44 44 GLU C 1168 ARG C 1177 1 10
HELIX 45 45 LYS C 1191 LEU C 1201 1 11
HELIX 46 46 LEU C 1238 MET C 1243 1 6
HELIX 47 47 GLU C 1272 TYR C 1281 1 10
HELIX 48 48 ALA C 1284 THR C 1292 1 9
HELIX 49 49 ASP C 1297 GLY C 1311 1 15
HELIX 50 50 PRO C 1320 SER C 1332 1 13
HELIX 51 51 SER D 26 TRP D 33 1 8
HELIX 52 52 GLN D 94 GLU D 100 5 7
HELIX 53 53 HIS D 113 SER D 119 1 7
HELIX 54 54 SER D 122 LEU D 128 1 7
HELIX 55 55 PRO D 131 TYR D 140 1 10
HELIX 56 56 THR D 161 GLY D 173 1 13
HELIX 57 57 GLY D 181 MET D 192 1 12
HELIX 58 58 ASP D 193 THR D 208 1 16
HELIX 59 59 SER D 210 SER D 230 1 21
HELIX 60 60 LYS D 233 TRP D 236 5 4
HELIX 61 61 PRO D 246 ARG D 250 5 5
HELIX 62 62 LEU D 255 ARG D 259 5 5
HELIX 63 63 ASP D 264 LEU D 285 1 22
HELIX 64 64 PRO D 288 ASP D 308 1 21
HELIX 65 65 SER D 326 GLY D 333 1 8
HELIX 66 66 LYS D 370 PHE D 377 1 8
HELIX 67 67 PHE D 377 ARG D 388 1 12
HELIX 68 68 THR D 393 GLU D 404 1 12
HELIX 69 69 VAL D 407 ARG D 417 1 11
HELIX 70 70 HIS D 430 LEU D 432 5 3
HELIX 71 71 HIS D 450 LEU D 452 5 3
HELIX 72 72 VAL D 453 ASN D 458 1 6
HELIX 73 73 THR D 473 LEU D 483 1 11
HELIX 74 74 GLN D 504 THR D 514 1 11
HELIX 75 75 GLY D 529 SER D 539 1 11
HELIX 76 76 VAL D 574 TRP D 580 1 7
HELIX 77 77 PRO D 588 ASN D 593 5 6
HELIX 78 78 LYS D 599 GLY D 613 1 15
HELIX 79 79 GLY D 613 GLY D 636 1 24
HELIX 80 80 LYS D 649 SER D 670 1 22
HELIX 81 81 THR D 674 GLU D 704 1 31
HELIX 82 82 ASN D 720 GLY D 729 1 10
HELIX 83 83 SER D 733 ALA D 741 1 9
HELIX 84 84 ASN D 768 ALA D 804 1 37
HELIX 85 85 PRO D 834 LEU D 840 1 7
HELIX 86 86 HIS D 865 ASN D 875 1 11
HELIX 87 87 CYS D 895 GLY D 900 1 6
HELIX 88 88 ALA D 914 GLU D 925 1 12
HELIX 89 89 PRO D 926 GLN D 929 5 4
HELIX 90 90 GLY D 1136 GLU D 1146 1 11
HELIX 91 91 ALA D 1216 ARG D 1224 1 9
HELIX 92 92 GLY D 1225 LEU D 1243 1 19
HELIX 93 93 ASN D 1249 LEU D 1261 1 13
HELIX 94 94 VAL D 1280 ASN D 1289 1 10
HELIX 95 95 GLY D 1308 SER D 1313 1 6
HELIX 96 96 SER D 1318 GLN D 1326 1 9
HELIX 97 97 GLU D 1327 GLY D 1339 1 13
HELIX 98 98 GLY D 1346 VAL D 1353 1 8
HELIX 99 99 THR D 1361 ARG D 1373 1 13
HELIX 100 100 VAL E 6 ILE E 13 1 8
HELIX 101 101 PHE E 17 VAL E 32 1 16
HELIX 102 102 LYS E 45 GLU E 56 1 12
HELIX 103 103 ASN E 60 ALA E 85 1 26
HELIX 104 104 ILE E 86 ARG E 90 5 5
HELIX 105 105 PRO F 97 GLY F 106 1 10
HELIX 106 106 THR F 112 GLU F 136 1 25
HELIX 107 107 TYR F 137 GLU F 152 1 16
HELIX 108 108 PRO F 214 THR F 234 1 21
HELIX 109 109 ALA F 245 GLN F 258 1 14
HELIX 110 110 VAL F 262 LEU F 290 1 29
HELIX 111 111 PRO F 298 ILE F 303 1 6
HELIX 112 112 SER F 312 ASN F 317 1 6
HELIX 113 113 ALA F 319 ASN F 323 5 5
HELIX 114 114 SER F 327 ASP F 332 5 6
HELIX 115 115 VAL F 333 THR F 351 1 19
HELIX 116 116 THR F 354 LYS F 392 1 39
HELIX 117 117 GLN F 400 PHE F 419 1 20
HELIX 118 118 GLU F 420 GLY F 424 5 5
HELIX 119 119 LYS F 426 ALA F 447 1 22
HELIX 120 120 PRO F 453 LEU F 471 1 19
HELIX 121 121 GLU F 481 MET F 487 1 7
HELIX 122 122 ASP F 492 ALA F 501 1 10
HELIX 123 123 ILE F 511 GLU F 515 5 5
HELIX 124 124 HIS F 518 ILE F 523 5 6
HELIX 125 125 LEU F 530 LEU F 551 1 22
HELIX 126 126 THR F 552 PHE F 563 1 12
HELIX 127 127 THR F 572 ASP F 581 1 10
HELIX 128 128 ARG F 584 HIS F 600 1 17
HELIX 129 129 ARG F 603 PHE F 610 1 8
HELIX 130 130 GLY G 34 SER G 50 1 17
HELIX 131 131 ASP G 77 LYS G 86 1 10
HELIX 132 132 ASP G 212 LEU G 228 1 17
HELIX 133 133 GLU G 229 PHE G 231 5 3
HELIX 134 134 GLY H 34 SER H 50 1 17
HELIX 135 135 ASP H 77 GLY H 87 1 11
HELIX 136 136 ALA H 113 ILE H 115 5 3
HELIX 137 137 ASP H 212 LEU H 228 1 17
HELIX 138 138 LEU I 28 ILE I 39 1 12
HELIX 139 139 GLY I 48 PHE I 57 1 10
HELIX 140 140 ASP I 81 GLY I 89 1 9
HELIX 141 141 ALA I 206 LEU I 213 1 8
HELIX 142 142 THR I 216 PHE I 225 1 10
HELIX 143 143 THR I 270 ASP I 281 1 12
HELIX 144 144 GLU I 290 GLY I 294 5 5
HELIX 145 145 SER I 318 GLN I 327 1 10
HELIX 146 146 PRO I 345 VAL I 353 1 9
HELIX 147 147 ASP I 358 ARG I 371 1 14
HELIX 148 148 THR I 377 PHE I 389 1 13
HELIX 149 149 LEU I 397 LEU I 409 1 13
HELIX 150 150 SER I 421 GLY I 438 1 18
HELIX 151 151 SER I 455 LEU I 479 1 25
HELIX 152 152 ALA I 495 SER I 508 1 14
HELIX 153 153 ASN I 519 ARG I 528 1 10
HELIX 154 154 GLY I 544 ASP I 549 1 6
HELIX 155 155 HIS I 551 TYR I 555 5 5
HELIX 156 156 ASP I 648 VAL I 650 5 3
HELIX 157 157 GLY I 664 ILE I 668 5 5
HELIX 158 158 PHE I 670 ASP I 674 5 5
HELIX 159 159 ASP I 675 GLN I 686 1 12
HELIX 160 160 ARG I 687 ALA I 689 5 3
HELIX 161 161 MET I 704 SER I 712 1 9
HELIX 162 162 GLU I 820 GLU I 825 1 6
HELIX 163 163 GLY I 858 LYS I 864 1 7
HELIX 164 164 THR I 896 GLY I 907 1 12
HELIX 165 165 ASP I 942 VAL I 980 1 39
HELIX 166 166 GLU I 985 ASP I 990 1 6
HELIX 167 167 PRO I 993 TRP I 997 5 5
HELIX 168 168 GLU I 1005 GLN I 1038 1 34
HELIX 169 169 PRO I 1081 MET I 1085 5 5
HELIX 170 170 LEU I 1101 ARG I 1106 1 6
HELIX 171 171 ILE I 1109 GLN I 1134 1 26
HELIX 172 172 GLU I 1137 LEU I 1151 1 15
HELIX 173 173 GLU I 1168 ARG I 1177 1 10
HELIX 174 174 LYS I 1191 LEU I 1201 1 11
HELIX 175 175 LEU I 1238 MET I 1243 1 6
HELIX 176 176 GLU I 1272 TYR I 1281 1 10
HELIX 177 177 ALA I 1284 THR I 1292 1 9
HELIX 178 178 ASP I 1297 GLY I 1311 1 15
HELIX 179 179 PRO I 1320 SER I 1332 1 13
HELIX 180 180 SER J 26 TRP J 33 1 8
HELIX 181 181 GLN J 94 GLU J 100 5 7
HELIX 182 182 HIS J 113 SER J 119 1 7
HELIX 183 183 SER J 122 LEU J 128 1 7
HELIX 184 184 PRO J 131 TYR J 140 1 10
HELIX 185 185 THR J 161 PHE J 172 1 12
HELIX 186 186 GLY J 181 MET J 192 1 12
HELIX 187 187 ASP J 193 THR J 208 1 16
HELIX 188 188 SER J 210 SER J 230 1 21
HELIX 189 189 LYS J 233 TRP J 236 5 4
HELIX 190 190 PRO J 246 ARG J 250 5 5
HELIX 191 191 LEU J 255 ARG J 259 5 5
HELIX 192 192 ASP J 264 LEU J 285 1 22
HELIX 193 193 PRO J 288 ASP J 308 1 21
HELIX 194 194 SER J 326 GLY J 333 1 8
HELIX 195 195 LYS J 370 PHE J 377 1 8
HELIX 196 196 PHE J 377 ARG J 388 1 12
HELIX 197 197 THR J 393 GLU J 404 1 12
HELIX 198 198 VAL J 407 ARG J 417 1 11
HELIX 199 199 HIS J 430 LEU J 432 5 3
HELIX 200 200 HIS J 450 LEU J 452 5 3
HELIX 201 201 VAL J 453 ASN J 458 1 6
HELIX 202 202 THR J 473 LEU J 483 1 11
HELIX 203 203 GLN J 504 THR J 514 1 11
HELIX 204 204 GLY J 529 SER J 539 1 11
HELIX 205 205 VAL J 574 TRP J 580 1 7
HELIX 206 206 PRO J 588 ASN J 593 5 6
HELIX 207 207 LYS J 599 GLY J 613 1 15
HELIX 208 208 GLY J 613 GLY J 636 1 24
HELIX 209 209 LYS J 649 SER J 670 1 22
HELIX 210 210 THR J 674 GLU J 704 1 31
HELIX 211 211 ASN J 720 GLY J 729 1 10
HELIX 212 212 SER J 733 ALA J 741 1 9
HELIX 213 213 ASN J 768 ALA J 804 1 37
HELIX 214 214 PRO J 834 LEU J 840 1 7
HELIX 215 215 HIS J 865 ASN J 875 1 11
HELIX 216 216 CYS J 895 GLY J 900 1 6
HELIX 217 217 ALA J 914 GLU J 925 1 12
HELIX 218 218 PRO J 926 GLN J 929 5 4
HELIX 219 219 LEU J 1138 GLU J 1146 1 9
HELIX 220 220 ALA J 1216 ARG J 1224 1 9
HELIX 221 221 GLY J 1225 LEU J 1243 1 19
HELIX 222 222 ASN J 1249 LEU J 1261 1 13
HELIX 223 223 VAL J 1280 ASN J 1289 1 10
HELIX 224 224 GLY J 1308 SER J 1313 1 6
HELIX 225 225 SER J 1318 GLN J 1326 1 9
HELIX 226 226 GLU J 1327 GLY J 1339 1 13
HELIX 227 227 GLY J 1346 VAL J 1353 1 8
HELIX 228 228 THR J 1361 ARG J 1373 1 13
HELIX 229 229 VAL K 6 ILE K 13 1 8
HELIX 230 230 PHE K 17 VAL K 32 1 16
HELIX 231 231 LYS K 45 GLU K 56 1 12
HELIX 232 232 ASN K 60 ALA K 78 1 19
HELIX 233 233 PRO L 97 GLY L 106 1 10
HELIX 234 234 THR L 112 GLU L 136 1 25
HELIX 235 235 TYR L 137 GLU L 152 1 16
HELIX 236 236 PRO L 214 THR L 234 1 21
HELIX 237 237 ALA L 245 GLN L 258 1 14
HELIX 238 238 VAL L 262 LEU L 290 1 29
HELIX 239 239 PRO L 298 ILE L 303 1 6
HELIX 240 240 SER L 312 ASN L 317 1 6
HELIX 241 241 ALA L 319 ASN L 323 5 5
HELIX 242 242 SER L 327 ASP L 332 5 6
HELIX 243 243 VAL L 333 THR L 351 1 19
HELIX 244 244 THR L 354 LYS L 392 1 39
HELIX 245 245 GLN L 400 PHE L 419 1 20
HELIX 246 246 GLU L 420 GLY L 424 5 5
HELIX 247 247 LYS L 426 ALA L 447 1 22
HELIX 248 248 PRO L 453 LEU L 471 1 19
HELIX 249 249 GLU L 481 MET L 487 1 7
HELIX 250 250 ASP L 492 ALA L 501 1 10
HELIX 251 251 ILE L 511 GLU L 515 5 5
HELIX 252 252 HIS L 518 ILE L 523 5 6
HELIX 253 253 LEU L 530 GLY L 550 1 21
HELIX 254 254 THR L 552 PHE L 563 1 12
HELIX 255 255 THR L 572 ASP L 581 1 10
HELIX 256 256 ARG L 584 HIS L 600 1 17
HELIX 257 257 ARG L 603 PHE L 610 1 8
SHEET 1 A 4 GLU A 17 GLN A 18 0
SHEET 2 A 4 HIS A 23 THR A 27 -1 O LYS A 25 N GLU A 17
SHEET 3 A 4 VAL A 202 GLU A 206 -1 O ILE A 203 N VAL A 26
SHEET 4 A 4 ALA A 184 ASN A 186 -1 N ASN A 186 O VAL A 202
SHEET 1 B 2 PRO A 52 GLY A 53 0
SHEET 2 B 2 GLY A 149 ARG A 150 -1 O GLY A 149 N GLY A 53
SHEET 1 C 4 GLU A 97 LEU A 102 0
SHEET 2 C 4 MET A 142 GLN A 147 -1 O ILE A 144 N LEU A 100
SHEET 3 C 4 VAL A 56 GLU A 60 -1 N GLU A 58 O LYS A 145
SHEET 4 C 4 ARG A 170 LEU A 172 -1 O LEU A 171 N VAL A 59
SHEET 1 D 2 VAL A 90 ARG A 91 0
SHEET 2 D 2 GLU A 122 ILE A 123 -1 O GLU A 122 N ARG A 91
SHEET 1 E 2 GLY A 108 THR A 111 0
SHEET 2 E 2 VAL A 129 LEU A 133 -1 O CYS A 131 N VAL A 110
SHEET 1 F 4 ASP B 15 GLU B 17 0
SHEET 2 F 4 HIS B 23 LEU B 28 -1 O THR B 27 N ASP B 15
SHEET 3 F 4 ARG B 195 THR B 207 -1 O MET B 205 N ALA B 24
SHEET 4 F 4 VAL B 180 VAL B 192 -1 N ASN B 186 O VAL B 202
SHEET 1 G 2 GLY B 53 CYS B 54 0
SHEET 2 G 2 ARG B 148 GLY B 149 -1 O GLY B 149 N GLY B 53
SHEET 1 H 3 GLU B 58 VAL B 59 0
SHEET 2 H 3 ARG B 143 LYS B 145 -1 O LYS B 145 N GLU B 58
SHEET 3 H 3 ILE B 99 THR B 101 -1 N LEU B 100 O ILE B 144
SHEET 1 I 2 VAL B 90 VAL B 92 0
SHEET 2 I 2 VAL B 121 ILE B 123 -1 O GLU B 122 N ARG B 91
SHEET 1 J 2 VAL B 110 THR B 111 0
SHEET 2 J 2 VAL B 129 CYS B 131 -1 O CYS B 131 N VAL B 110
SHEET 1 K 2 LYS C 13 ASP C 14 0
SHEET 2 K 2 ILE C1182 ALA C1183 1 O ALA C1183 N LYS C 13
SHEET 1 L 4 ILE C 59 GLN C 60 0
SHEET 2 L 4 SER C 66 LEU C 75 -1 O LEU C 68 N ILE C 59
SHEET 3 L 4 SER C 93 ILE C 104 -1 O LYS C 99 N SER C 72
SHEET 4 L 4 ASP C 116 ILE C 117 -1 O ILE C 117 N LEU C 102
SHEET 1 M 4 ILE C 59 GLN C 60 0
SHEET 2 M 4 SER C 66 LEU C 75 -1 O LEU C 68 N ILE C 59
SHEET 3 M 4 SER C 93 ILE C 104 -1 O LYS C 99 N SER C 72
SHEET 4 M 4 VAL C 122 PRO C 128 -1 O VAL C 122 N VAL C 98
SHEET 1 N 3 PHE C 136 VAL C 137 0
SHEET 2 N 3 GLU C 142 ILE C 145 -1 O ARG C 143 N PHE C 136
SHEET 3 N 3 SER C 512 PHE C 514 -1 O GLN C 513 N VAL C 144
SHEET 1 O 3 ARG C 451 ILE C 453 0
SHEET 2 O 3 SER C 147 ARG C 151 -1 N HIS C 150 O ARG C 452
SHEET 3 O 3 ILE C 530 SER C 531 1 O SER C 531 N LEU C 149
SHEET 1 P 5 GLY C 154 ASP C 158 0
SHEET 2 P 5 ASN C 173 ILE C 177 -1 O ASN C 173 N ASP C 158
SHEET 3 P 5 LEU C 184 GLU C 187 -1 O LEU C 184 N ILE C 176
SHEET 4 P 5 PHE C 195 ILE C 198 -1 O PHE C 195 N GLU C 187
SHEET 5 P 5 LEU C 204 PRO C 205 -1 O LEU C 204 N VAL C 196
SHEET 1 Q 4 LEU C 284 GLU C 286 0
SHEET 2 Q 4 GLN C 238 GLU C 240 -1 N MET C 239 O ILE C 285
SHEET 3 Q 4 LYS C 227 GLU C 231 -1 N GLU C 231 O GLN C 238
SHEET 4 Q 4 ARG C 332 LEU C 336 -1 O ILE C 333 N PHE C 230
SHEET 1 R 2 GLU C 249 THR C 250 0
SHEET 2 R 2 ARG C 268 ILE C 269 -1 O ILE C 269 N GLU C 249
SHEET 1 S 2 ILE C 255 ALA C 257 0
SHEET 2 S 2 LYS C 260 VAL C 263 -1 O VAL C 263 N ILE C 255
SHEET 1 T 2 TYR C 301 ASP C 303 0
SHEET 2 T 2 GLU C 308 CYS C 311 -1 O CYS C 311 N TYR C 301
SHEET 1 U 3 GLN C 580 THR C 581 0
SHEET 2 U 3 LEU C 587 THR C 595 -1 O GLU C 588 N GLN C 580
SHEET 3 U 3 VAL C 598 LEU C 606 -1 O HIS C 604 N TYR C 591
SHEET 1 V 3 GLN C 580 THR C 581 0
SHEET 2 V 3 LEU C 587 THR C 595 -1 O GLU C 588 N GLN C 580
SHEET 3 V 3 TYR C 652 ASP C 654 -1 O MET C 653 N ARG C 592
SHEET 1 W 2 LEU C 623 ASP C 624 0
SHEET 2 W 2 HIS C 628 PHE C 629 -1 O HIS C 628 N ASP C 624
SHEET 1 X 2 LEU C 633 ARG C 637 0
SHEET 2 X 2 SER C 642 SER C 646 -1 O SER C 643 N CYS C 636
SHEET 1 Y 3 ALA C 716 VAL C 717 0
SHEET 2 Y 3 VAL C 782 ASP C 785 -1 O LEU C 783 N ALA C 716
SHEET 3 Y 3 MET C 768 PRO C 769 -1 N MET C 768 O ASP C 785
SHEET 1 Z 4 ILE C 748 ASN C 752 0
SHEET 2 Z 4 ARG C 731 VAL C 736 -1 N ILE C 734 O ASP C 749
SHEET 3 Z 4 GLY C 722 VAL C 727 -1 N VAL C 723 O LYS C 735
SHEET 4 Z 4 PRO C 776 VAL C 777 -1 O VAL C 777 N GLY C 722
SHEET 1 AA 2 THR C 757 ARG C 758 0
SHEET 2 AA 2 CYS C 764 ILE C 765 -1 O ILE C 765 N THR C 757
SHEET 1 AB 2 THR C 789 ASP C 790 0
SHEET 2 AB 2 GLU C 793 LEU C 794 -1 O GLU C 793 N ASP C 790
SHEET 1 AC 6 MET C1066 GLY C1068 0
SHEET 2 AC 6 VAL C1225 LYS C1234 -1 O LEU C1233 N ALA C1067
SHEET 3 AC 6 GLN C 798 PHE C 804 -1 N PHE C 804 O THR C1226
SHEET 4 AC 6 ILE C1096 LEU C1098 1 O ILE C1096 N ALA C 803
SHEET 5 AC 6 ILE C 816 SER C 819 -1 N LEU C 817 O VAL C1097
SHEET 6 AC 6 ILE C1076 ASN C1080 1 O SER C1077 N ILE C 816
SHEET 1 AD 3 MET C1066 GLY C1068 0
SHEET 2 AD 3 VAL C1225 LYS C1234 -1 O LEU C1233 N ALA C1067
SHEET 3 AD 3 GLN C1209 ILE C1210 -1 N ILE C1210 O VAL C1225
SHEET 1 AE 5 GLY C 846 PRO C 847 0
SHEET 2 AE 5 THR C 830 THR C 843 -1 N THR C 843 O GLY C 846
SHEET 3 AE 5 VAL C1046 ARG C1058 -1 O ARG C1058 N THR C 830
SHEET 4 AE 5 GLY C 926 THR C 935 -1 N THR C 927 O ALA C1055
SHEET 5 AE 5 GLU C 876 VAL C 877 -1 N VAL C 877 O GLY C 926
SHEET 1 AF 2 ILE C 882 VAL C 884 0
SHEET 2 AF 2 LEU C 918 ARG C 919 -1 O LEU C 918 N VAL C 884
SHEET 1 AG 2 VAL C 887 PRO C 889 0
SHEET 2 AG 2 VAL C 913 ASP C 915 -1 O LYS C 914 N THR C 888
SHEET 1 AH 8 HIS C1244 ARG C1246 0
SHEET 2 AH 8 SER D 350 THR D 356 -1 O ARG D 352 N HIS C1244
SHEET 3 AH 8 GLN D 465 HIS D 469 -1 O MET D 466 N SER D 353
SHEET 4 AH 8 VAL D 421 ASN D 424 -1 N LEU D 422 O HIS D 469
SHEET 5 AH 8 ILE D 434 ILE D 442 -1 O GLN D 435 N LEU D 423
SHEET 6 AH 8 GLN D 365 PRO D 369 1 N LEU D 368 O VAL D 440
SHEET 7 AH 8 ILE D 447 GLN D 448 -1 O GLN D 448 N GLY D 367
SHEET 8 AH 8 SER D 350 THR D 356 1 N THR D 356 O ILE D 447
SHEET 1 AI 2 ARG C1269 GLY C1271 0
SHEET 2 AI 2 GLY D 344 ARG D 346 -1 O LYS D 345 N PHE C1270
SHEET 1 AJ 3 ILE C1335 GLU C1338 0
SHEET 2 AJ 3 ILE D 20 LEU D 24 -1 O LYS D 21 N GLU C1338
SHEET 3 AJ 3 ARG D1341 ASP D1342 -1 O ASP D1342 N ILE D 20
SHEET 1 AK 3 SER D 34 GLU D 37 0
SHEET 2 AK 3 MET D 102 ALA D 112 1 O HIS D 104 N GLY D 36
SHEET 3 AK 3 ILE D 238 VAL D 244 -1 O LEU D 239 N THR D 111
SHEET 1 AL 3 ILE D 159 LEU D 160 0
SHEET 2 AL 3 TYR D 144 VAL D 146 -1 N TYR D 144 O LEU D 160
SHEET 3 AL 3 ALA D 178 LYS D 179 -1 O LYS D 179 N VAL D 145
SHEET 1 AM 2 ALA D 261 THR D 262 0
SHEET 2 AM 2 ILE F 505 SER F 506 1 O ILE F 505 N THR D 262
SHEET 1 AN 3 VAL D 526 LEU D 527 0
SHEET 2 AN 3 ARG D 547 GLU D 556 1 O ARG D 551 N LEU D 527
SHEET 3 AN 3 VAL D 564 THR D 573 -1 O VAL D 564 N GLU D 556
SHEET 1 AO 2 THR D 705 ILE D 707 0
SHEET 2 AO 2 GLU D 714 GLN D 716 -1 O GLU D 714 N ILE D 707
SHEET 1 AP 2 ILE D 820 MET D 822 0
SHEET 2 AP 2 VAL D 880 VAL D 882 -1 O VAL D 882 N ILE D 820
SHEET 1 AQ 3 ILE D1162 PHE D1165 0
SHEET 2 AQ 3 ARG D1173 THR D1178 -1 O VAL D1176 N SER D1164
SHEET 3 AQ 3 GLU D1187 ILE D1190 -1 O GLU D1188 N LEU D1175
SHEET 1 AR 2 LYS D1263 THR D1265 0
SHEET 2 AR 2 GLY D1277 GLN D1279 -1 O GLU D1278 N ALA D1264
SHEET 1 AS 2 ILE F 162 PHE F 165 0
SHEET 2 AS 2 PHE F 259 LEU F 261 -1 O ARG F 260 N THR F 163
SHEET 1 AT 4 GLU G 17 GLN G 18 0
SHEET 2 AT 4 HIS G 23 THR G 27 -1 O LYS G 25 N GLU G 17
SHEET 3 AT 4 VAL G 202 GLU G 206 -1 O ILE G 203 N VAL G 26
SHEET 4 AT 4 ALA G 184 ASN G 186 -1 N ASN G 186 O VAL G 202
SHEET 1 AU 2 PRO G 52 GLY G 53 0
SHEET 2 AU 2 GLY G 149 ARG G 150 -1 O GLY G 149 N GLY G 53
SHEET 1 AV 4 GLU G 97 LEU G 102 0
SHEET 2 AV 4 MET G 142 GLN G 147 -1 O ILE G 144 N LEU G 100
SHEET 3 AV 4 VAL G 56 GLU G 60 -1 N GLU G 58 O LYS G 145
SHEET 4 AV 4 ARG G 170 LEU G 172 -1 O LEU G 171 N VAL G 59
SHEET 1 AW 2 VAL G 90 ARG G 91 0
SHEET 2 AW 2 GLU G 122 ILE G 123 -1 O GLU G 122 N ARG G 91
SHEET 1 AX 2 GLY G 108 THR G 111 0
SHEET 2 AX 2 VAL G 129 LEU G 133 -1 O CYS G 131 N VAL G 110
SHEET 1 AY 4 ASP H 15 GLU H 17 0
SHEET 2 AY 4 HIS H 23 LEU H 28 -1 O THR H 27 N ASP H 15
SHEET 3 AY 4 ARG H 195 THR H 207 -1 O MET H 205 N ALA H 24
SHEET 4 AY 4 VAL H 180 VAL H 192 -1 N ASN H 186 O VAL H 202
SHEET 1 AZ 3 GLY H 53 VAL H 59 0
SHEET 2 AZ 3 ARG H 143 GLY H 149 -1 O LYS H 145 N GLU H 58
SHEET 3 AZ 3 ILE H 99 THR H 101 -1 N LEU H 100 O ILE H 144
SHEET 1 BA 2 VAL H 90 VAL H 92 0
SHEET 2 BA 2 VAL H 121 ILE H 123 -1 O GLU H 122 N ARG H 91
SHEET 1 BB 2 VAL H 110 THR H 111 0
SHEET 2 BB 2 VAL H 129 CYS H 131 -1 O CYS H 131 N VAL H 110
SHEET 1 BC 3 LYS I 13 ASP I 14 0
SHEET 2 BC 3 ILE I1182 ALA I1183 1 O ALA I1183 N LYS I 13
SHEET 3 BC 3 VAL I 700 GLY I 701 1 N GLY I 701 O ILE I1182
SHEET 1 BD 4 ILE I 59 GLN I 60 0
SHEET 2 BD 4 SER I 66 LEU I 75 -1 O LEU I 68 N ILE I 59
SHEET 3 BD 4 SER I 93 ILE I 104 -1 O LYS I 99 N SER I 72
SHEET 4 BD 4 ASP I 116 PRO I 128 -1 O ILE I 117 N LEU I 102
SHEET 1 BE 3 PHE I 136 VAL I 137 0
SHEET 2 BE 3 GLU I 142 ILE I 145 -1 O ARG I 143 N PHE I 136
SHEET 3 BE 3 SER I 512 PHE I 514 -1 O GLN I 513 N VAL I 144
SHEET 1 BF 3 ARG I 451 ILE I 453 0
SHEET 2 BF 3 SER I 147 ARG I 151 -1 N HIS I 150 O ARG I 452
SHEET 3 BF 3 ILE I 530 SER I 531 1 O SER I 531 N LEU I 149
SHEET 1 BG 5 GLY I 154 ASP I 158 0
SHEET 2 BG 5 ASN I 173 ILE I 177 -1 O ASN I 173 N ASP I 158
SHEET 3 BG 5 LEU I 184 GLU I 187 -1 O LEU I 184 N ILE I 176
SHEET 4 BG 5 PHE I 195 ILE I 198 -1 O PHE I 195 N GLU I 187
SHEET 5 BG 5 LEU I 204 PRO I 205 -1 O LEU I 204 N VAL I 196
SHEET 1 BH 4 LEU I 284 GLU I 286 0
SHEET 2 BH 4 GLN I 238 GLU I 240 -1 N MET I 239 O ILE I 285
SHEET 3 BH 4 LYS I 227 GLU I 231 -1 N GLU I 231 O GLN I 238
SHEET 4 BH 4 ARG I 332 LEU I 336 -1 O ILE I 333 N PHE I 230
SHEET 1 BI 2 GLU I 249 THR I 250 0
SHEET 2 BI 2 ARG I 268 ILE I 269 -1 O ILE I 269 N GLU I 249
SHEET 1 BJ 2 ILE I 255 ALA I 257 0
SHEET 2 BJ 2 LYS I 260 VAL I 263 -1 O VAL I 263 N ILE I 255
SHEET 1 BK 2 TYR I 301 ILE I 302 0
SHEET 2 BK 2 LEU I 309 CYS I 311 -1 O CYS I 311 N TYR I 301
SHEET 1 BL 3 GLN I 580 THR I 581 0
SHEET 2 BL 3 LEU I 587 THR I 595 -1 O GLU I 588 N GLN I 580
SHEET 3 BL 3 VAL I 598 LEU I 606 -1 O HIS I 604 N TYR I 591
SHEET 1 BM 3 GLN I 580 THR I 581 0
SHEET 2 BM 3 LEU I 587 THR I 595 -1 O GLU I 588 N GLN I 580
SHEET 3 BM 3 TYR I 652 ASP I 654 -1 O MET I 653 N ARG I 592
SHEET 1 BN 2 LEU I 623 ASP I 624 0
SHEET 2 BN 2 HIS I 628 PHE I 629 -1 O HIS I 628 N ASP I 624
SHEET 1 BO 2 LEU I 633 ARG I 637 0
SHEET 2 BO 2 SER I 642 SER I 646 -1 O SER I 643 N CYS I 636
SHEET 1 BP 3 ALA I 716 VAL I 717 0
SHEET 2 BP 3 VAL I 782 ASP I 785 -1 O LEU I 783 N ALA I 716
SHEET 3 BP 3 MET I 768 PRO I 769 -1 N MET I 768 O ASP I 785
SHEET 1 BQ 4 ILE I 748 ASN I 752 0
SHEET 2 BQ 4 ARG I 731 VAL I 736 -1 N ILE I 734 O ASP I 749
SHEET 3 BQ 4 GLY I 722 VAL I 727 -1 N VAL I 723 O LYS I 735
SHEET 4 BQ 4 PRO I 776 VAL I 777 -1 O VAL I 777 N GLY I 722
SHEET 1 BR 2 THR I 757 ARG I 758 0
SHEET 2 BR 2 CYS I 764 ILE I 765 -1 O ILE I 765 N THR I 757
SHEET 1 BS 2 THR I 789 ASP I 790 0
SHEET 2 BS 2 GLU I 793 LEU I 794 -1 O GLU I 793 N ASP I 790
SHEET 1 BT 6 MET I1066 GLY I1068 0
SHEET 2 BT 6 VAL I1225 LYS I1234 -1 O LEU I1233 N ALA I1067
SHEET 3 BT 6 GLN I 798 PHE I 804 -1 N PHE I 804 O THR I1226
SHEET 4 BT 6 ILE I1096 LEU I1098 1 O ILE I1096 N ALA I 803
SHEET 5 BT 6 ILE I 816 SER I 819 -1 N LEU I 817 O VAL I1097
SHEET 6 BT 6 ILE I1076 ASN I1080 1 O SER I1077 N ILE I 816
SHEET 1 BU 3 MET I1066 GLY I1068 0
SHEET 2 BU 3 VAL I1225 LYS I1234 -1 O LEU I1233 N ALA I1067
SHEET 3 BU 3 GLN I1209 ILE I1210 -1 N ILE I1210 O VAL I1225
SHEET 1 BV 5 GLY I 846 PRO I 847 0
SHEET 2 BV 5 THR I 830 THR I 843 -1 N THR I 843 O GLY I 846
SHEET 3 BV 5 VAL I1046 ARG I1058 -1 O ARG I1058 N THR I 830
SHEET 4 BV 5 GLY I 926 THR I 935 -1 N PHE I 934 O ILE I1049
SHEET 5 BV 5 GLU I 876 VAL I 877 -1 N VAL I 877 O GLY I 926
SHEET 1 BW 2 ILE I 882 VAL I 884 0
SHEET 2 BW 2 LEU I 918 ARG I 919 -1 O LEU I 918 N VAL I 884
SHEET 1 BX 2 VAL I 887 PRO I 889 0
SHEET 2 BX 2 VAL I 913 ASP I 915 -1 O LYS I 914 N THR I 888
SHEET 1 BY 8 HIS I1244 ARG I1246 0
SHEET 2 BY 8 SER J 350 THR J 356 -1 O ARG J 352 N HIS I1244
SHEET 3 BY 8 GLN J 465 HIS J 469 -1 O MET J 466 N SER J 353
SHEET 4 BY 8 VAL J 421 ASN J 424 -1 N LEU J 422 O HIS J 469
SHEET 5 BY 8 ILE J 434 ILE J 442 -1 O GLN J 435 N LEU J 423
SHEET 6 BY 8 GLN J 365 PRO J 369 1 N LEU J 368 O VAL J 440
SHEET 7 BY 8 ILE J 447 GLN J 448 -1 O GLN J 448 N GLY J 367
SHEET 8 BY 8 SER J 350 THR J 356 1 N THR J 356 O ILE J 447
SHEET 1 BZ 2 ARG I1269 GLY I1271 0
SHEET 2 BZ 2 GLY J 344 ARG J 346 -1 O LYS J 345 N PHE I1270
SHEET 1 CA 3 ILE I1335 GLU I1338 0
SHEET 2 CA 3 ILE J 20 LEU J 24 -1 O LYS J 21 N GLU I1338
SHEET 3 CA 3 ARG J1341 ASP J1342 -1 O ASP J1342 N ILE J 20
SHEET 1 CB 3 SER J 34 GLU J 37 0
SHEET 2 CB 3 MET J 102 ALA J 112 1 O HIS J 104 N GLY J 36
SHEET 3 CB 3 ILE J 238 VAL J 244 -1 O LEU J 239 N THR J 111
SHEET 1 CC 3 ILE J 159 LEU J 160 0
SHEET 2 CC 3 TYR J 144 VAL J 146 -1 N TYR J 144 O LEU J 160
SHEET 3 CC 3 ALA J 178 LYS J 179 -1 O LYS J 179 N VAL J 145
SHEET 1 CD 2 ALA J 261 THR J 262 0
SHEET 2 CD 2 ILE L 505 SER L 506 1 O ILE L 505 N THR J 262
SHEET 1 CE 3 VAL J 526 LEU J 527 0
SHEET 2 CE 3 ARG J 547 GLU J 556 1 O ARG J 551 N LEU J 527
SHEET 3 CE 3 VAL J 564 THR J 573 -1 O VAL J 564 N GLU J 556
SHEET 1 CF 2 THR J 705 ILE J 707 0
SHEET 2 CF 2 GLU J 714 GLN J 716 -1 O GLU J 714 N ILE J 707
SHEET 1 CG 2 ILE J 820 MET J 822 0
SHEET 2 CG 2 VAL J 880 VAL J 882 -1 O VAL J 882 N ILE J 820
SHEET 1 CH 3 ILE J 958 SER J 961 0
SHEET 2 CH 3 GLU J 981 ILE J 985 -1 O LYS J 983 N LYS J 959
SHEET 3 CH 3 THR J 991 LYS J 996 -1 O TYR J 995 N LEU J 982
SHEET 1 CI 4 SER J 965 VAL J 967 0
SHEET 2 CI 4 LEU J 973 ILE J 975 -1 O VAL J 974 N VAL J 966
SHEET 3 CI 4 VAL J1002 LEU J1003 -1 O LEU J1003 N LEU J 973
SHEET 4 CI 4 ALA J1018 ASN J1019 -1 O ASN J1019 N VAL J1002
SHEET 1 CJ 3 MET J1025 PRO J1026 0
SHEET 2 CJ 3 ALA J1122 ILE J1124 -1 O ILE J1124 N MET J1025
SHEET 3 CJ 3 ILE J1106 VAL J1107 -1 N ILE J1106 O ARG J1123
SHEET 1 CK 4 GLN J1098 PHE J1100 0
SHEET 2 CK 4 ALA J1077 VAL J1081 -1 N LEU J1078 O TYR J1099
SHEET 3 CK 4 GLY J1033 THR J1038 -1 N PHE J1034 O VAL J1081
SHEET 4 CK 4 GLN J1114 ILE J1115 -1 O ILE J1115 N GLY J1033
SHEET 1 CL 2 ILE J1046 GLN J1049 0
SHEET 2 CL 2 SER J1058 VAL J1061 -1 O VAL J1060 N THR J1047
SHEET 1 CM 3 ILE J1162 PHE J1165 0
SHEET 2 CM 3 ARG J1173 THR J1178 -1 O VAL J1176 N SER J1164
SHEET 3 CM 3 GLU J1187 ILE J1190 -1 O GLU J1188 N LEU J1175
SHEET 1 CN 2 LYS J1263 THR J1265 0
SHEET 2 CN 2 GLY J1277 GLN J1279 -1 O GLU J1278 N ALA J1264
SHEET 1 CO 2 ILE L 162 PHE L 165 0
SHEET 2 CO 2 PHE L 259 LEU L 261 -1 O ARG L 260 N THR L 163
LINK SG CYS D 70 ZN ZN D1502 1555 1555 2.36
LINK SG CYS D 72 ZN ZN D1502 1555 1555 2.26
LINK SG CYS D 85 ZN ZN D1502 1555 1555 2.36
LINK SG CYS D 814 ZN ZN D1503 1555 1555 2.41
LINK SG CYS D 888 ZN ZN D1503 1555 1555 2.36
LINK SG CYS D 895 ZN ZN D1503 1555 1555 2.51
LINK SG CYS D 898 ZN ZN D1503 1555 1555 2.29
LINK SG CYS J 70 ZN ZN J1502 1555 1555 2.35
LINK SG CYS J 72 ZN ZN J1502 1555 1555 2.26
LINK SG CYS J 85 ZN ZN J1502 1555 1555 2.34
LINK SG CYS J 814 ZN ZN J1503 1555 1555 2.40
LINK SG CYS J 888 ZN ZN J1503 1555 1555 2.38
LINK SG CYS J 895 ZN ZN J1503 1555 1555 2.50
LINK SG CYS J 898 ZN ZN J1503 1555 1555 2.47
CISPEP 1 GLU B 29 PRO B 30 0 -12.93
CISPEP 2 PHE C 57 PRO C 58 0 -11.67
CISPEP 3 ARG C 107 GLU C 108 0 11.65
CISPEP 4 ALA C 543 GLY C 544 0 20.95
CISPEP 5 ASP C 1160 LEU C 1161 0 19.87
CISPEP 6 ARG D 53 ASP D 54 0 -7.97
CISPEP 7 GLY D 336 ARG D 337 0 3.10
CISPEP 8 GLU H 29 PRO H 30 0 -12.85
CISPEP 9 PHE I 57 PRO I 58 0 -11.83
CISPEP 10 ARG I 107 GLU I 108 0 14.55
CISPEP 11 ALA I 543 GLY I 544 0 20.84
CISPEP 12 ASP I 1160 LEU I 1161 0 17.14
CISPEP 13 ARG J 53 ASP J 54 0 -8.05
SITE 1 AC1 3 ASP D 460 ASP D 462 ASP D 464
SITE 1 AC2 4 CYS D 70 CYS D 72 CYS D 85 CYS D 88
SITE 1 AC3 4 CYS D 814 CYS D 888 CYS D 895 CYS D 898
SITE 1 AC4 3 ASP J 460 ASP J 462 ASP J 464
SITE 1 AC5 4 CYS J 70 CYS J 72 CYS J 85 CYS J 88
SITE 1 AC6 4 CYS J 814 CYS J 888 CYS J 895 CYS J 898
CRYST1 186.366 206.740 309.190 90.00 90.00 90.00 P 21 21 21 16
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 0.005366 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003234 0.00000
MTRIX1 1 -0.408742 -0.005560 -0.912633 -69.40560 1
MTRIX2 1 -0.041692 -0.998824 0.024758 -221.11900 1
MTRIX3 1 -0.911697 0.048170 0.408030 -39.81770 1
MTRIX1 2 -0.474270 0.039090 -0.879511 -65.79100 1
MTRIX2 2 -0.068330 -0.997635 -0.007494 -225.45700 1
MTRIX3 2 -0.877724 0.056543 0.475819 -30.82610 1
MTRIX1 3 -0.359519 0.079142 -0.929776 -55.68390 1
MTRIX2 3 -0.078513 -0.995429 -0.054371 -230.02100 1
MTRIX3 3 -0.929829 0.053452 0.364089 -44.07620 1
MTRIX1 4 -0.347840 0.097627 -0.932457 -52.90580 1
MTRIX2 4 -0.098377 -0.992874 -0.067254 -231.97600 1
MTRIX3 4 -0.932378 0.068338 0.354966 -43.12830 1
MTRIX1 5 -0.406474 -0.007603 -0.913631 -69.54780 1
MTRIX2 5 -0.038281 -0.998946 0.025344 -220.61500 1
MTRIX3 5 -0.912860 0.045276 0.405754 -40.46500 1
MTRIX1 6 -0.442476 -0.005077 -0.896766 -70.24980 1
MTRIX2 6 0.004265 -0.999985 0.003557 -218.97000 1
MTRIX3 6 -0.896770 -0.002250 0.442491 -45.41570 1
MTRIX1 7 -0.407374 0.013507 -0.913162 -66.34290 1
MTRIX2 7 -0.046727 -0.998889 0.006071 -222.72700 1
MTRIX3 7 -0.912065 0.045143 0.407552 -40.53860 1
MTRIX1 8 -0.417008 0.010430 -0.908843 -67.18090 1
MTRIX2 8 -0.032129 -0.999478 0.003271 -221.82899 1
MTRIX3 8 -0.908335 0.030564 0.417126 -41.87860 1
MTRIX1 9 -0.394229 0.036166 -0.918301 -63.39520 1
MTRIX2 9 0.047285 -0.997104 -0.059569 -225.61800 1
MTRIX3 9 -0.917795 -0.066906 0.391377 -61.41470 1
MTRIX1 10 -0.424555 -0.012268 -0.905319 -71.02730 1
MTRIX2 10 -0.009445 -0.999794 0.017977 -219.96201 1
MTRIX3 10 -0.905353 0.016183 0.424351 -43.58110 1
MTRIX1 11 -0.408943 -0.000910 -0.912560 -68.69800 1
MTRIX2 11 -0.043457 -0.998846 0.020470 -221.34399 1
MTRIX3 11 -0.911525 0.048028 0.408431 -39.76380 1
MTRIX1 12 -0.411506 -0.030633 -0.910892 -72.67960 1
MTRIX2 12 -0.029289 -0.998474 0.046810 -219.18300 1
MTRIX3 12 -0.910936 0.045942 0.409981 -40.09210 1
(ATOM LINES ARE NOT SHOWN.)
END
