HEADER ENDOCYTOSIS 30-SEP-14 4WJG
TITLE STRUCTURE OF T. BRUCEI HAPTOGLOBIN-HEMOGLOBIN RECEPTOR BINDING TO
TITLE 2 HUMAN HAPTOGLOBIN-HEMOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;
COMPND 3 CHAIN: A, F, K, P, U, Z;
COMPND 4 SYNONYM: ALPHA-GLOBIN,HEMOGLOBIN ALPHA CHAIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN SUBUNIT BETA;
COMPND 7 CHAIN: B, G, L, Q, V, 1;
COMPND 8 SYNONYM: BETA-GLOBIN,HEMOGLOBIN BETA CHAIN;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HAPTOGLOBIN;
COMPND 11 CHAIN: C, H, M, R, W, 2;
COMPND 12 SYNONYM: ZONULIN;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: IRON-REGULATED SURFACE DETERMINANT PROTEIN H;
COMPND 15 CHAIN: D, I, N, S, X, 3;
COMPND 16 SYNONYM: HAPTOGLOBIN RECEPTOR A,STAPHYLOCOCCUS AUREUS SURFACE PROTEIN
COMPND 17 I;
COMPND 18 ENGINEERED: YES;
COMPND 19 OTHER_DETAILS: FIRST NEAT DOMAIN;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: HAPTOGLOBIN-HEMOGLOBIN RECEPTOR;
COMPND 22 CHAIN: E, J, O, T, Y, 4;
COMPND 23 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS N315;
SOURCE 15 ORGANISM_TAXID: 158879;
SOURCE 16 GENE: ISDH, HARA, SASI, SA1552;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 20 MOL_ID: 5;
SOURCE 21 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;
SOURCE 22 ORGANISM_TAXID: 5702;
SOURCE 23 GENE: HPHBR;
SOURCE 24 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PPICZ ALPHA A
KEYWDS ENDOCYTOSIS, TRYPANOSOME, RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR K.STOEDKILDE,M.TORVUND-JENSEN,S.K.MOESTRUP,C.B.F.ANDERSEN
REVDAT 4 29-JUL-20 4WJG 1 COMPND SOURCE REMARK HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 28-FEB-18 4WJG 1 SOURCE
REVDAT 2 03-DEC-14 4WJG 1 JRNL
REVDAT 1 26-NOV-14 4WJG 0
JRNL AUTH K.STDKILDE,M.TORVUND-JENSEN,S.K.MOESTRUP,C.B.ANDERSEN
JRNL TITL STRUCTURAL BASIS FOR TRYPANOSOMAL HAEM ACQUISITION AND
JRNL TITL 2 SUSCEPTIBILITY TO THE HOST INNATE IMMUNE SYSTEM.
JRNL REF NAT COMMUN V. 5 5487 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25410714
JRNL DOI 10.1038/NCOMMS6487
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1702)
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 182377
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.255
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1750
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 28.9841 - 7.2538 0.91 13511 87 0.1822 0.1853
REMARK 3 2 7.2538 - 5.7725 0.96 13884 197 0.2329 0.2497
REMARK 3 3 5.7725 - 5.0472 0.96 13967 100 0.2350 0.2649
REMARK 3 4 5.0472 - 4.5877 0.96 13943 192 0.2205 0.2467
REMARK 3 5 4.5877 - 4.2599 0.97 14132 98 0.2236 0.2281
REMARK 3 6 4.2599 - 4.0095 0.97 14118 97 0.2420 0.2603
REMARK 3 7 4.0095 - 3.8091 0.95 13685 196 0.2659 0.2782
REMARK 3 8 3.8091 - 3.6436 0.96 13977 97 0.2783 0.2907
REMARK 3 9 3.6436 - 3.5036 0.97 14066 159 0.2967 0.3221
REMARK 3 10 3.5036 - 3.3829 0.97 14025 135 0.3152 0.3157
REMARK 3 11 3.3829 - 3.2773 0.97 14050 100 0.3405 0.4031
REMARK 3 12 3.2773 - 3.1837 0.97 13830 194 0.3757 0.3596
REMARK 3 13 3.1837 - 3.1000 0.97 14029 98 0.4074 0.4514
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.011 48930
REMARK 3 ANGLE : 1.552 66526
REMARK 3 CHIRALITY : 0.065 7487
REMARK 3 PLANARITY : 0.007 8482
REMARK 3 DIHEDRAL : 18.507 17611
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000203888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 184077
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.440
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 (%): 66.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% POLYETHYLENE GLYCOL (PEG) 1500,
REMARK 280 0.1M BIS-TRIS, PH 6.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 70.47500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: a, b, c
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: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, N, O, P, Q, R, S, T,
REMARK 350 AND CHAINS: d, e, f, g
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V, W, X, Y, Z, 1, 2, 3, 4,
REMARK 350 AND CHAINS: h, i, j
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO C 157A
REMARK 465 VAL C 157B
REMARK 465 GLN C 157C
REMARK 465 ARG C 157D
REMARK 465 ASN C 402
REMARK 465 GLY D 84
REMARK 465 SER D 85
REMARK 465 MET E 297
REMARK 465 LYS E 298
REMARK 465 ARG E 299
REMARK 465 ASN E 300
REMARK 465 GLY E 301
REMARK 465 ASN E 302
REMARK 465 PRO E 303
REMARK 465 ILE E 304
REMARK 465 GLU E 305
REMARK 465 ASN E 306
REMARK 465 GLU E 307
REMARK 465 SER E 308
REMARK 465 GLU E 309
REMARK 465 THR E 310
REMARK 465 ASN E 311
REMARK 465 SER E 312
REMARK 465 GLY E 313
REMARK 465 GLY E 314
REMARK 465 ASN E 315
REMARK 465 ALA E 316
REMARK 465 GLU E 317
REMARK 465 SER E 318
REMARK 465 GLN E 319
REMARK 465 GLY E 320
REMARK 465 ASN E 321
REMARK 465 GLY E 322
REMARK 465 ASP E 323
REMARK 465 ARG E 324
REMARK 465 GLU E 325
REMARK 465 ASP E 326
REMARK 465 LYS E 327
REMARK 465 ASN E 328
REMARK 465 ASP E 329
REMARK 465 GLU E 330
REMARK 465 GLN E 331
REMARK 465 GLN E 332
REMARK 465 GLN E 333
REMARK 465 VAL E 334
REMARK 465 ASP E 335
REMARK 465 GLU E 336
REMARK 465 GLU E 337
REMARK 465 GLU E 338
REMARK 465 THR E 339
REMARK 465 LYS E 340
REMARK 465 VAL E 341
REMARK 465 GLU E 342
REMARK 465 ASN E 343
REMARK 465 GLY E 344
REMARK 465 SER E 345
REMARK 465 SER E 346
REMARK 465 GLU E 347
REMARK 465 GLU E 348
REMARK 465 GLY E 349
REMARK 465 SER E 350
REMARK 465 CYS E 351
REMARK 465 CYS E 352
REMARK 465 GLY E 353
REMARK 465 ASN E 354
REMARK 465 GLU E 355
REMARK 465 SER E 356
REMARK 465 ASN E 357
REMARK 465 GLY E 358
REMARK 465 PRO E 359
REMARK 465 HIS E 360
REMARK 465 VAL E 361
REMARK 465 MET E 362
REMARK 465 LYS E 363
REMARK 465 LYS E 364
REMARK 465 ARG E 365
REMARK 465 HIS E 366
REMARK 465 GLY E 367
REMARK 465 VAL E 368
REMARK 465 GLU E 369
REMARK 465 GLY E 370
REMARK 465 PRO E 371
REMARK 465 ARG E 372
REMARK 465 PRO E 373
REMARK 465 VAL E 374
REMARK 465 ASP E 375
REMARK 465 VAL E 376
REMARK 465 VAL E 377
REMARK 465 SER E 378
REMARK 465 PRO H 157A
REMARK 465 VAL H 157B
REMARK 465 GLN H 157C
REMARK 465 ARG H 157D
REMARK 465 ASN H 402
REMARK 465 GLY I 84
REMARK 465 SER I 85
REMARK 465 MET J 297
REMARK 465 LYS J 298
REMARK 465 ARG J 299
REMARK 465 ASN J 300
REMARK 465 GLY J 301
REMARK 465 ASN J 302
REMARK 465 PRO J 303
REMARK 465 ILE J 304
REMARK 465 GLU J 305
REMARK 465 ASN J 306
REMARK 465 GLU J 307
REMARK 465 SER J 308
REMARK 465 GLU J 309
REMARK 465 THR J 310
REMARK 465 ASN J 311
REMARK 465 SER J 312
REMARK 465 GLY J 313
REMARK 465 GLY J 314
REMARK 465 ASN J 315
REMARK 465 ALA J 316
REMARK 465 GLU J 317
REMARK 465 SER J 318
REMARK 465 GLN J 319
REMARK 465 GLY J 320
REMARK 465 ASN J 321
REMARK 465 GLY J 322
REMARK 465 ASP J 323
REMARK 465 ARG J 324
REMARK 465 GLU J 325
REMARK 465 ASP J 326
REMARK 465 LYS J 327
REMARK 465 ASN J 328
REMARK 465 ASP J 329
REMARK 465 GLU J 330
REMARK 465 GLN J 331
REMARK 465 GLN J 332
REMARK 465 GLN J 333
REMARK 465 VAL J 334
REMARK 465 ASP J 335
REMARK 465 GLU J 336
REMARK 465 GLU J 337
REMARK 465 GLU J 338
REMARK 465 THR J 339
REMARK 465 LYS J 340
REMARK 465 VAL J 341
REMARK 465 GLU J 342
REMARK 465 ASN J 343
REMARK 465 GLY J 344
REMARK 465 SER J 345
REMARK 465 SER J 346
REMARK 465 GLU J 347
REMARK 465 GLU J 348
REMARK 465 GLY J 349
REMARK 465 SER J 350
REMARK 465 CYS J 351
REMARK 465 CYS J 352
REMARK 465 GLY J 353
REMARK 465 ASN J 354
REMARK 465 GLU J 355
REMARK 465 SER J 356
REMARK 465 ASN J 357
REMARK 465 GLY J 358
REMARK 465 PRO J 359
REMARK 465 HIS J 360
REMARK 465 VAL J 361
REMARK 465 MET J 362
REMARK 465 LYS J 363
REMARK 465 LYS J 364
REMARK 465 ARG J 365
REMARK 465 HIS J 366
REMARK 465 GLY J 367
REMARK 465 VAL J 368
REMARK 465 GLU J 369
REMARK 465 GLY J 370
REMARK 465 PRO J 371
REMARK 465 ARG J 372
REMARK 465 PRO J 373
REMARK 465 VAL J 374
REMARK 465 ASP J 375
REMARK 465 VAL J 376
REMARK 465 VAL J 377
REMARK 465 SER J 378
REMARK 465 PRO M 157A
REMARK 465 VAL M 157B
REMARK 465 GLN M 157C
REMARK 465 ARG M 157D
REMARK 465 ASN M 402
REMARK 465 GLY N 84
REMARK 465 SER N 85
REMARK 465 MET O 297
REMARK 465 LYS O 298
REMARK 465 ARG O 299
REMARK 465 ASN O 300
REMARK 465 GLY O 301
REMARK 465 ASN O 302
REMARK 465 PRO O 303
REMARK 465 ILE O 304
REMARK 465 GLU O 305
REMARK 465 ASN O 306
REMARK 465 GLU O 307
REMARK 465 SER O 308
REMARK 465 GLU O 309
REMARK 465 THR O 310
REMARK 465 ASN O 311
REMARK 465 SER O 312
REMARK 465 GLY O 313
REMARK 465 GLY O 314
REMARK 465 ASN O 315
REMARK 465 ALA O 316
REMARK 465 GLU O 317
REMARK 465 SER O 318
REMARK 465 GLN O 319
REMARK 465 GLY O 320
REMARK 465 ASN O 321
REMARK 465 GLY O 322
REMARK 465 ASP O 323
REMARK 465 ARG O 324
REMARK 465 GLU O 325
REMARK 465 ASP O 326
REMARK 465 LYS O 327
REMARK 465 ASN O 328
REMARK 465 ASP O 329
REMARK 465 GLU O 330
REMARK 465 GLN O 331
REMARK 465 GLN O 332
REMARK 465 GLN O 333
REMARK 465 VAL O 334
REMARK 465 ASP O 335
REMARK 465 GLU O 336
REMARK 465 GLU O 337
REMARK 465 GLU O 338
REMARK 465 THR O 339
REMARK 465 LYS O 340
REMARK 465 VAL O 341
REMARK 465 GLU O 342
REMARK 465 ASN O 343
REMARK 465 GLY O 344
REMARK 465 SER O 345
REMARK 465 SER O 346
REMARK 465 GLU O 347
REMARK 465 GLU O 348
REMARK 465 GLY O 349
REMARK 465 SER O 350
REMARK 465 CYS O 351
REMARK 465 CYS O 352
REMARK 465 GLY O 353
REMARK 465 ASN O 354
REMARK 465 GLU O 355
REMARK 465 SER O 356
REMARK 465 ASN O 357
REMARK 465 GLY O 358
REMARK 465 PRO O 359
REMARK 465 HIS O 360
REMARK 465 VAL O 361
REMARK 465 MET O 362
REMARK 465 LYS O 363
REMARK 465 LYS O 364
REMARK 465 ARG O 365
REMARK 465 HIS O 366
REMARK 465 GLY O 367
REMARK 465 VAL O 368
REMARK 465 GLU O 369
REMARK 465 GLY O 370
REMARK 465 PRO O 371
REMARK 465 ARG O 372
REMARK 465 PRO O 373
REMARK 465 VAL O 374
REMARK 465 ASP O 375
REMARK 465 VAL O 376
REMARK 465 VAL O 377
REMARK 465 SER O 378
REMARK 465 PRO R 157A
REMARK 465 VAL R 157B
REMARK 465 GLN R 157C
REMARK 465 ARG R 157D
REMARK 465 ASN R 402
REMARK 465 GLY S 84
REMARK 465 SER S 85
REMARK 465 MET T 297
REMARK 465 LYS T 298
REMARK 465 ARG T 299
REMARK 465 ASN T 300
REMARK 465 GLY T 301
REMARK 465 ASN T 302
REMARK 465 PRO T 303
REMARK 465 ILE T 304
REMARK 465 GLU T 305
REMARK 465 ASN T 306
REMARK 465 GLU T 307
REMARK 465 SER T 308
REMARK 465 GLU T 309
REMARK 465 THR T 310
REMARK 465 ASN T 311
REMARK 465 SER T 312
REMARK 465 GLY T 313
REMARK 465 GLY T 314
REMARK 465 ASN T 315
REMARK 465 ALA T 316
REMARK 465 GLU T 317
REMARK 465 SER T 318
REMARK 465 GLN T 319
REMARK 465 GLY T 320
REMARK 465 ASN T 321
REMARK 465 GLY T 322
REMARK 465 ASP T 323
REMARK 465 ARG T 324
REMARK 465 GLU T 325
REMARK 465 ASP T 326
REMARK 465 LYS T 327
REMARK 465 ASN T 328
REMARK 465 ASP T 329
REMARK 465 GLU T 330
REMARK 465 GLN T 331
REMARK 465 GLN T 332
REMARK 465 GLN T 333
REMARK 465 VAL T 334
REMARK 465 ASP T 335
REMARK 465 GLU T 336
REMARK 465 GLU T 337
REMARK 465 GLU T 338
REMARK 465 THR T 339
REMARK 465 LYS T 340
REMARK 465 VAL T 341
REMARK 465 GLU T 342
REMARK 465 ASN T 343
REMARK 465 GLY T 344
REMARK 465 SER T 345
REMARK 465 SER T 346
REMARK 465 GLU T 347
REMARK 465 GLU T 348
REMARK 465 GLY T 349
REMARK 465 SER T 350
REMARK 465 CYS T 351
REMARK 465 CYS T 352
REMARK 465 GLY T 353
REMARK 465 ASN T 354
REMARK 465 GLU T 355
REMARK 465 SER T 356
REMARK 465 ASN T 357
REMARK 465 GLY T 358
REMARK 465 PRO T 359
REMARK 465 HIS T 360
REMARK 465 VAL T 361
REMARK 465 MET T 362
REMARK 465 LYS T 363
REMARK 465 LYS T 364
REMARK 465 ARG T 365
REMARK 465 HIS T 366
REMARK 465 GLY T 367
REMARK 465 VAL T 368
REMARK 465 GLU T 369
REMARK 465 GLY T 370
REMARK 465 PRO T 371
REMARK 465 ARG T 372
REMARK 465 PRO T 373
REMARK 465 VAL T 374
REMARK 465 ASP T 375
REMARK 465 VAL T 376
REMARK 465 VAL T 377
REMARK 465 SER T 378
REMARK 465 PRO W 157A
REMARK 465 VAL W 157B
REMARK 465 GLN W 157C
REMARK 465 ARG W 157D
REMARK 465 ASN W 402
REMARK 465 GLY X 84
REMARK 465 SER X 85
REMARK 465 MET Y 297
REMARK 465 LYS Y 298
REMARK 465 ARG Y 299
REMARK 465 ASN Y 300
REMARK 465 GLY Y 301
REMARK 465 ASN Y 302
REMARK 465 PRO Y 303
REMARK 465 ILE Y 304
REMARK 465 GLU Y 305
REMARK 465 ASN Y 306
REMARK 465 GLU Y 307
REMARK 465 SER Y 308
REMARK 465 GLU Y 309
REMARK 465 THR Y 310
REMARK 465 ASN Y 311
REMARK 465 SER Y 312
REMARK 465 GLY Y 313
REMARK 465 GLY Y 314
REMARK 465 ASN Y 315
REMARK 465 ALA Y 316
REMARK 465 GLU Y 317
REMARK 465 SER Y 318
REMARK 465 GLN Y 319
REMARK 465 GLY Y 320
REMARK 465 ASN Y 321
REMARK 465 GLY Y 322
REMARK 465 ASP Y 323
REMARK 465 ARG Y 324
REMARK 465 GLU Y 325
REMARK 465 ASP Y 326
REMARK 465 LYS Y 327
REMARK 465 ASN Y 328
REMARK 465 ASP Y 329
REMARK 465 GLU Y 330
REMARK 465 GLN Y 331
REMARK 465 GLN Y 332
REMARK 465 GLN Y 333
REMARK 465 VAL Y 334
REMARK 465 ASP Y 335
REMARK 465 GLU Y 336
REMARK 465 GLU Y 337
REMARK 465 GLU Y 338
REMARK 465 THR Y 339
REMARK 465 LYS Y 340
REMARK 465 VAL Y 341
REMARK 465 GLU Y 342
REMARK 465 ASN Y 343
REMARK 465 GLY Y 344
REMARK 465 SER Y 345
REMARK 465 SER Y 346
REMARK 465 GLU Y 347
REMARK 465 GLU Y 348
REMARK 465 GLY Y 349
REMARK 465 SER Y 350
REMARK 465 CYS Y 351
REMARK 465 CYS Y 352
REMARK 465 GLY Y 353
REMARK 465 ASN Y 354
REMARK 465 GLU Y 355
REMARK 465 SER Y 356
REMARK 465 ASN Y 357
REMARK 465 GLY Y 358
REMARK 465 PRO Y 359
REMARK 465 HIS Y 360
REMARK 465 VAL Y 361
REMARK 465 MET Y 362
REMARK 465 LYS Y 363
REMARK 465 LYS Y 364
REMARK 465 ARG Y 365
REMARK 465 HIS Y 366
REMARK 465 GLY Y 367
REMARK 465 VAL Y 368
REMARK 465 GLU Y 369
REMARK 465 GLY Y 370
REMARK 465 PRO Y 371
REMARK 465 ARG Y 372
REMARK 465 PRO Y 373
REMARK 465 VAL Y 374
REMARK 465 ASP Y 375
REMARK 465 VAL Y 376
REMARK 465 VAL Y 377
REMARK 465 SER Y 378
REMARK 465 PRO 2 157A
REMARK 465 VAL 2 157B
REMARK 465 GLN 2 157C
REMARK 465 ARG 2 157D
REMARK 465 ASN 2 402
REMARK 465 GLY 3 84
REMARK 465 SER 3 85
REMARK 465 MET 4 297
REMARK 465 LYS 4 298
REMARK 465 ARG 4 299
REMARK 465 ASN 4 300
REMARK 465 GLY 4 301
REMARK 465 ASN 4 302
REMARK 465 PRO 4 303
REMARK 465 ILE 4 304
REMARK 465 GLU 4 305
REMARK 465 ASN 4 306
REMARK 465 GLU 4 307
REMARK 465 SER 4 308
REMARK 465 GLU 4 309
REMARK 465 THR 4 310
REMARK 465 ASN 4 311
REMARK 465 SER 4 312
REMARK 465 GLY 4 313
REMARK 465 GLY 4 314
REMARK 465 ASN 4 315
REMARK 465 ALA 4 316
REMARK 465 GLU 4 317
REMARK 465 SER 4 318
REMARK 465 GLN 4 319
REMARK 465 GLY 4 320
REMARK 465 ASN 4 321
REMARK 465 GLY 4 322
REMARK 465 ASP 4 323
REMARK 465 ARG 4 324
REMARK 465 GLU 4 325
REMARK 465 ASP 4 326
REMARK 465 LYS 4 327
REMARK 465 ASN 4 328
REMARK 465 ASP 4 329
REMARK 465 GLU 4 330
REMARK 465 GLN 4 331
REMARK 465 GLN 4 332
REMARK 465 GLN 4 333
REMARK 465 VAL 4 334
REMARK 465 ASP 4 335
REMARK 465 GLU 4 336
REMARK 465 GLU 4 337
REMARK 465 GLU 4 338
REMARK 465 THR 4 339
REMARK 465 LYS 4 340
REMARK 465 VAL 4 341
REMARK 465 GLU 4 342
REMARK 465 ASN 4 343
REMARK 465 GLY 4 344
REMARK 465 SER 4 345
REMARK 465 SER 4 346
REMARK 465 GLU 4 347
REMARK 465 GLU 4 348
REMARK 465 GLY 4 349
REMARK 465 SER 4 350
REMARK 465 CYS 4 351
REMARK 465 CYS 4 352
REMARK 465 GLY 4 353
REMARK 465 ASN 4 354
REMARK 465 GLU 4 355
REMARK 465 SER 4 356
REMARK 465 ASN 4 357
REMARK 465 GLY 4 358
REMARK 465 PRO 4 359
REMARK 465 HIS 4 360
REMARK 465 VAL 4 361
REMARK 465 MET 4 362
REMARK 465 LYS 4 363
REMARK 465 LYS 4 364
REMARK 465 ARG 4 365
REMARK 465 HIS 4 366
REMARK 465 GLY 4 367
REMARK 465 VAL 4 368
REMARK 465 GLU 4 369
REMARK 465 GLY 4 370
REMARK 465 PRO 4 371
REMARK 465 ARG 4 372
REMARK 465 PRO 4 373
REMARK 465 VAL 4 374
REMARK 465 ASP 4 375
REMARK 465 VAL 4 376
REMARK 465 VAL 4 377
REMARK 465 SER 4 378
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 OG1 THR M 196 OD1 ASN M 199 2.08
REMARK 500 OH TYR M 109 O PRO R 96 2.09
REMARK 500 ND2 ASN W 203 O5 NAG W 1002 2.09
REMARK 500 OG1 THR C 196 OD1 ASN C 199 2.10
REMARK 500 OG1 THR H 196 OD1 ASN H 199 2.10
REMARK 500 ND2 ASN M 203 O5 NAG d 1 2.13
REMARK 500 OG1 THR 2 196 OD1 ASN 2 199 2.14
REMARK 500 OG1 THR W 196 OD1 ASN W 199 2.14
REMARK 500 OD2 ASP E 43 CE LYS E 47 2.15
REMARK 500 O4 NAG e 1 C2 NAG e 2 2.16
REMARK 500 ND2 ASN R 203 O5 NAG f 1 2.16
REMARK 500 OH TYR C 109 O PRO H 96 2.16
REMARK 500 O ASN E 287 OG1 THR E 291 2.18
REMARK 500 ND2 ASN H 157 O THR J 68 2.18
REMARK 500 O ASN Y 287 OG1 THR Y 291 2.18
REMARK 500 O ASN J 287 OG1 THR J 291 2.18
REMARK 500 OD2 ASP J 147 NZ LYS J 151 2.18
REMARK 500 OD2 ASP Y 147 NZ LYS Y 151 2.19
REMARK 500 O ASN T 287 OG1 THR T 291 2.19
REMARK 500 OD2 ASP 4 147 NZ LYS 4 151 2.19
REMARK 500 O ASN O 287 OG1 THR O 291 2.19
REMARK 500 OG1 THR R 196 OD1 ASN R 199 2.19
REMARK 500 OD2 ASP T 147 NZ LYS T 151 2.19
REMARK 500 O ASN 4 287 OG1 THR 4 291 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 VAL F 1 CG1 - CB - CG2 ANGL. DEV. = 9.8 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 LEU A 2 76.14 55.83
REMARK 500 LYS A 16 -9.48 -55.19
REMARK 500 SER A 49 -176.82 -68.55
REMARK 500 HIS A 89 -63.40 -92.29
REMARK 500 ARG A 92 71.73 40.58
REMARK 500 PRO A 95 -18.83 -47.05
REMARK 500 GLU B 22 -57.38 -126.81
REMARK 500 PRO C 93 84.51 -65.86
REMARK 500 THR C 119 162.88 171.94
REMARK 500 HIS C 162 75.84 60.54
REMARK 500 HIS C 179 37.66 -95.28
REMARK 500 LYS C 223 -84.35 -89.51
REMARK 500 GLU C 230 -70.14 -87.79
REMARK 500 MET C 259 138.77 -175.39
REMARK 500 ASN C 283 -166.94 -122.84
REMARK 500 SER C 312 -74.06 -102.41
REMARK 500 THR C 313 -104.54 67.10
REMARK 500 CYS C 347 -167.36 -125.09
REMARK 500 SER C 372 -61.37 -92.77
REMARK 500 CYS C 377 -133.89 50.03
REMARK 500 LYS D 142 -74.19 -103.22
REMARK 500 LYS D 157 -73.74 -116.87
REMARK 500 VAL D 173 -60.58 -102.53
REMARK 500 GLU D 180 -62.61 -94.93
REMARK 500 GLN D 194 -57.55 -127.30
REMARK 500 ASP D 205 -119.85 54.44
REMARK 500 LEU E 39 176.53 167.43
REMARK 500 LYS E 40 -159.49 -172.89
REMARK 500 LYS E 42 -8.41 -57.69
REMARK 500 GLU E 109 -76.37 -99.62
REMARK 500 ASN E 114 65.32 36.52
REMARK 500 THR E 116 -105.05 61.27
REMARK 500 ALA E 118 -61.05 -93.02
REMARK 500 ASN E 185 -18.84 75.85
REMARK 500 ALA E 188 -18.19 65.60
REMARK 500 ALA E 194 -61.12 -95.48
REMARK 500 ASN E 219 -71.86 -55.85
REMARK 500 LEU E 223 -38.43 -39.25
REMARK 500 HIS E 289 -61.42 -100.81
REMARK 500 LYS E 292 -60.01 -99.96
REMARK 500 LEU F 2 76.77 58.13
REMARK 500 SER F 49 -175.90 -68.95
REMARK 500 HIS F 89 -64.82 -92.83
REMARK 500 ARG F 92 72.54 41.00
REMARK 500 PRO F 95 -19.46 -46.97
REMARK 500 THR F 118 150.80 -46.90
REMARK 500 ALA F 123 -70.42 -56.64
REMARK 500 GLU G 22 -56.70 -127.08
REMARK 500 ASN G 80 48.02 -97.16
REMARK 500 PRO H 93 85.26 -65.40
REMARK 500
REMARK 500 THIS ENTRY HAS 245 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 GLU C 120 GLY C 121 39.63
REMARK 500 GLY C 311 SER C 312 -137.42
REMARK 500 SER C 312 THR C 313 -129.66
REMARK 500 ALA C 378 VAL C 379 -149.85
REMARK 500 PRO D 177 VAL D 178 -140.00
REMARK 500 GLY E 38 LEU E 39 147.53
REMARK 500 GLU H 120 GLY H 121 39.26
REMARK 500 GLY H 311 SER H 312 -137.43
REMARK 500 SER H 312 THR H 313 -129.30
REMARK 500 PRO I 177 VAL I 178 -138.27
REMARK 500 GLY J 38 LEU J 39 147.96
REMARK 500 GLU M 120 GLY M 121 39.35
REMARK 500 GLY M 311 SER M 312 -137.00
REMARK 500 SER M 312 THR M 313 -131.28
REMARK 500 ALA M 378 VAL M 379 -149.89
REMARK 500 PRO N 177 VAL N 178 -139.72
REMARK 500 GLY O 38 LEU O 39 147.80
REMARK 500 GLU R 120 GLY R 121 38.90
REMARK 500 GLY R 311 SER R 312 -136.82
REMARK 500 SER R 312 THR R 313 -129.28
REMARK 500 PRO S 177 VAL S 178 -139.17
REMARK 500 GLY T 38 LEU T 39 147.63
REMARK 500 GLU W 120 GLY W 121 37.61
REMARK 500 GLY W 311 SER W 312 -137.71
REMARK 500 SER W 312 THR W 313 -129.89
REMARK 500 PRO X 177 VAL X 178 -139.75
REMARK 500 GLY Y 38 LEU Y 39 147.69
REMARK 500 GLU 2 120 GLY 2 121 38.31
REMARK 500 GLY 2 311 SER 2 312 -138.54
REMARK 500 SER 2 312 THR 2 313 -129.33
REMARK 500 PRO 3 177 VAL 3 178 -139.38
REMARK 500 GLY 4 38 LEU 4 39 148.43
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 HEM A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 87 NE2
REMARK 620 2 HEM A 201 NA 80.9
REMARK 620 3 HEM A 201 NB 91.9 94.1
REMARK 620 4 HEM A 201 NC 112.1 166.9 83.7
REMARK 620 5 HEM A 201 ND 102.4 85.7 165.5 93.2
REMARK 620 6 OXY A 202 O1 156.1 75.4 92.9 91.7 73.0
REMARK 620 7 OXY A 202 O2 169.3 101.5 98.3 66.1 67.6 27.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 92 NE2
REMARK 620 2 HEM B 201 NA 96.1
REMARK 620 3 HEM B 201 NB 78.0 94.3
REMARK 620 4 HEM B 201 NC 105.8 153.2 75.6
REMARK 620 5 HEM B 201 ND 128.5 79.5 153.1 98.1
REMARK 620 6 OXY B 202 O2 139.9 72.4 65.1 80.8 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 87 NE2
REMARK 620 2 HEM F 201 NA 83.4
REMARK 620 3 HEM F 201 NB 86.8 92.7
REMARK 620 4 HEM F 201 NC 109.9 166.8 88.1
REMARK 620 5 HEM F 201 ND 107.1 82.9 164.8 93.0
REMARK 620 6 OXY F 202 O1 157.2 76.0 84.6 90.9 80.2
REMARK 620 7 OXY F 202 O2 173.0 97.3 100.1 69.5 66.3 27.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM G 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 92 NE2
REMARK 620 2 HEM G 201 NA 94.7
REMARK 620 3 HEM G 201 NB 79.7 87.5
REMARK 620 4 HEM G 201 NC 109.2 151.8 82.3
REMARK 620 5 HEM G 201 ND 126.7 83.8 152.7 93.3
REMARK 620 6 OXY G 202 O1 145.9 71.9 68.8 79.9 83.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM K 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 87 NE2
REMARK 620 2 HEM K 201 NA 87.8
REMARK 620 3 HEM K 201 NB 93.4 95.5
REMARK 620 4 HEM K 201 NC 108.6 163.5 85.4
REMARK 620 5 HEM K 201 ND 105.3 82.7 161.1 91.1
REMARK 620 6 OXY K 202 O1 168.5 81.6 83.4 82.1 77.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM L 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 92 NE2
REMARK 620 2 HEM L 201 NA 92.7
REMARK 620 3 HEM L 201 NB 79.8 93.4
REMARK 620 4 HEM L 201 NC 110.1 150.7 73.7
REMARK 620 5 HEM L 201 ND 128.5 77.0 149.9 100.8
REMARK 620 6 OXY L 202 O1 143.4 69.0 70.4 81.8 79.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM P 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 87 NE2
REMARK 620 2 HEM P 201 NA 80.6
REMARK 620 3 HEM P 201 NB 85.3 94.8
REMARK 620 4 HEM P 201 NC 113.3 165.6 83.1
REMARK 620 5 HEM P 201 ND 108.3 78.8 163.5 99.3
REMARK 620 6 OXY P 202 O1 141.5 73.4 69.3 92.6 94.2
REMARK 620 7 OXY P 202 O2 167.6 87.3 92.8 78.6 71.8 29.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM Q 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 92 NE2
REMARK 620 2 HEM Q 201 NA 97.1
REMARK 620 3 HEM Q 201 NB 79.4 90.1
REMARK 620 4 HEM Q 201 NC 106.2 150.7 77.4
REMARK 620 5 HEM Q 201 ND 129.0 80.3 150.7 97.7
REMARK 620 6 OXY Q 202 O2 160.2 81.3 80.8 70.7 70.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM U 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS U 87 NE2
REMARK 620 2 HEM U 201 NA 71.2
REMARK 620 3 HEM U 201 NB 87.4 87.7
REMARK 620 4 HEM U 201 NC 114.1 174.2 90.2
REMARK 620 5 HEM U 201 ND 96.2 85.3 170.6 96.2
REMARK 620 6 OXY U 202 O2 162.6 91.5 94.1 83.3 79.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS V 92 NE2
REMARK 620 2 HEM V 201 NA 91.4
REMARK 620 3 HEM V 201 NB 76.8 88.0
REMARK 620 4 HEM V 201 NC 100.2 163.0 82.7
REMARK 620 5 HEM V 201 ND 119.8 89.8 163.3 95.1
REMARK 620 6 OXY V 202 O2 169.7 85.5 93.2 80.9 70.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM Z 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Z 87 NE2
REMARK 620 2 HEM Z 201 NA 83.8
REMARK 620 3 HEM Z 201 NB 93.5 90.0
REMARK 620 4 HEM Z 201 NC 107.7 168.4 87.8
REMARK 620 5 HEM Z 201 ND 99.0 86.2 166.4 93.3
REMARK 620 6 OXY Z 202 O1 151.5 67.7 88.3 100.8 78.2
REMARK 620 7 OXY Z 202 O2 177.4 94.4 88.3 74.2 79.1 26.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM 1 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS 1 92 NE2
REMARK 620 2 HEM 1 201 NA 87.8
REMARK 620 3 HEM 1 201 NB 76.5 94.0
REMARK 620 4 HEM 1 201 NC 106.2 162.5 79.5
REMARK 620 5 HEM 1 201 ND 121.5 82.8 161.4 98.2
REMARK 620 6 OXY 1 202 O1 137.8 69.2 70.7 93.3 91.1
REMARK 620 7 OXY 1 202 O2 165.4 83.6 92.4 80.5 69.0 27.6
REMARK 620 N 1 2 3 4 5 6
DBREF 4WJG A 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 4WJG B 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 4WJG C 92 402 UNP P00738 HPT_HUMAN 92 406
DBREF 4WJG D 86 229 UNP Q99TD3 ISDH_STAAN 86 229
DBREF 4WJG E 36 378 UNP I7BA80 I7BA80_TRYBB 36 378
DBREF 4WJG F 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 4WJG G 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 4WJG H 92 402 UNP P00738 HPT_HUMAN 92 406
DBREF 4WJG I 86 229 UNP Q99TD3 ISDH_STAAN 86 229
DBREF 4WJG J 36 378 UNP I7BA80 I7BA80_TRYBB 36 378
DBREF 4WJG K 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 4WJG L 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 4WJG M 92 402 UNP P00738 HPT_HUMAN 92 406
DBREF 4WJG N 86 229 UNP Q99TD3 ISDH_STAAN 86 229
DBREF 4WJG O 36 378 UNP I7BA80 I7BA80_TRYBB 36 378
DBREF 4WJG P 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 4WJG Q 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 4WJG R 92 402 UNP P00738 HPT_HUMAN 92 406
DBREF 4WJG S 86 229 UNP Q99TD3 ISDH_STAAN 86 229
DBREF 4WJG T 36 378 UNP I7BA80 I7BA80_TRYBB 36 378
DBREF 4WJG U 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 4WJG V 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 4WJG W 92 402 UNP P00738 HPT_HUMAN 92 406
DBREF 4WJG X 86 229 UNP Q99TD3 ISDH_STAAN 86 229
DBREF 4WJG Y 36 378 UNP I7BA80 I7BA80_TRYBB 36 378
DBREF 4WJG Z 1 141 UNP P69905 HBA_HUMAN 2 142
DBREF 4WJG 1 1 146 UNP P68871 HBB_HUMAN 2 147
DBREF 4WJG 2 92 402 UNP P00738 HPT_HUMAN 92 406
DBREF 4WJG 3 86 229 UNP Q99TD3 ISDH_STAAN 86 229
DBREF 4WJG 4 36 378 UNP I7BA80 I7BA80_TRYBB 36 378
SEQADV 4WJG GLY D 84 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG SER D 85 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG GLY I 84 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG SER I 85 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG GLY N 84 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG SER N 85 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG GLY S 84 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG SER S 85 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG GLY X 84 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG SER X 85 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG GLY 3 84 UNP Q99TD3 EXPRESSION TAG
SEQADV 4WJG SER 3 85 UNP Q99TD3 EXPRESSION TAG
SEQRES 1 A 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 A 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 A 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 A 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 A 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 B 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 B 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 B 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 B 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 B 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 B 146 LYS TYR HIS
SEQRES 1 C 315 CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU
SEQRES 2 C 315 HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU
SEQRES 3 C 315 ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU
SEQRES 4 C 315 LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO
SEQRES 5 C 315 GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA
SEQRES 6 C 315 ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA
SEQRES 7 C 315 LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS
SEQRES 8 C 315 HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN
SEQRES 9 C 315 TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS
SEQRES 10 C 315 SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU
SEQRES 11 C 315 THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU
SEQRES 12 C 315 LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE
SEQRES 13 C 315 GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU
SEQRES 14 C 315 ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA
SEQRES 15 C 315 GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG
SEQRES 16 C 315 ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL
SEQRES 17 C 315 MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS
SEQRES 18 C 315 TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS
SEQRES 19 C 315 SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR
SEQRES 20 C 315 PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS
SEQRES 21 C 315 TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU
SEQRES 22 C 315 GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE
SEQRES 23 C 315 ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL
SEQRES 24 C 315 LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE
SEQRES 25 C 315 ALA GLU ASN
SEQRES 1 D 146 GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP
SEQRES 2 D 146 PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG
SEQRES 3 D 146 GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU
SEQRES 4 D 146 THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA
SEQRES 5 D 146 ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU
SEQRES 6 D 146 ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL
SEQRES 7 D 146 TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER
SEQRES 8 D 146 TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE
SEQRES 9 D 146 PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER
SEQRES 10 D 146 SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP
SEQRES 11 D 146 TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP
SEQRES 12 D 146 PRO SER LEU
SEQRES 1 E 343 ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA
SEQRES 2 E 343 CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR
SEQRES 3 E 343 LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL
SEQRES 4 E 343 GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA
SEQRES 5 E 343 ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL
SEQRES 6 E 343 ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA
SEQRES 7 E 343 ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR
SEQRES 8 E 343 SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR
SEQRES 9 E 343 GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS
SEQRES 10 E 343 ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU
SEQRES 11 E 343 LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU
SEQRES 12 E 343 ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS
SEQRES 13 E 343 ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER
SEQRES 14 E 343 THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA
SEQRES 15 E 343 ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR
SEQRES 16 E 343 GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER
SEQRES 17 E 343 VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS
SEQRES 18 E 343 HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS
SEQRES 19 E 343 ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE
SEQRES 20 E 343 GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU
SEQRES 21 E 343 GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER
SEQRES 22 E 343 GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN
SEQRES 23 E 343 GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL
SEQRES 24 E 343 ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU
SEQRES 25 E 343 GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS
SEQRES 26 E 343 VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO
SEQRES 27 E 343 VAL ASP VAL VAL SER
SEQRES 1 F 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 F 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 F 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 F 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 F 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 F 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 F 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 F 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 F 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 F 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 F 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 G 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 G 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 G 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 G 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 G 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 G 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 G 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 G 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 G 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 G 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 G 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 G 146 LYS TYR HIS
SEQRES 1 H 315 CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU
SEQRES 2 H 315 HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU
SEQRES 3 H 315 ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU
SEQRES 4 H 315 LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO
SEQRES 5 H 315 GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA
SEQRES 6 H 315 ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA
SEQRES 7 H 315 LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS
SEQRES 8 H 315 HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN
SEQRES 9 H 315 TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS
SEQRES 10 H 315 SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU
SEQRES 11 H 315 THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU
SEQRES 12 H 315 LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE
SEQRES 13 H 315 GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU
SEQRES 14 H 315 ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA
SEQRES 15 H 315 GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG
SEQRES 16 H 315 ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL
SEQRES 17 H 315 MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS
SEQRES 18 H 315 TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS
SEQRES 19 H 315 SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR
SEQRES 20 H 315 PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS
SEQRES 21 H 315 TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU
SEQRES 22 H 315 GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE
SEQRES 23 H 315 ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL
SEQRES 24 H 315 LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE
SEQRES 25 H 315 ALA GLU ASN
SEQRES 1 I 146 GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP
SEQRES 2 I 146 PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG
SEQRES 3 I 146 GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU
SEQRES 4 I 146 THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA
SEQRES 5 I 146 ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU
SEQRES 6 I 146 ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL
SEQRES 7 I 146 TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER
SEQRES 8 I 146 TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE
SEQRES 9 I 146 PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER
SEQRES 10 I 146 SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP
SEQRES 11 I 146 TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP
SEQRES 12 I 146 PRO SER LEU
SEQRES 1 J 343 ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA
SEQRES 2 J 343 CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR
SEQRES 3 J 343 LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL
SEQRES 4 J 343 GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA
SEQRES 5 J 343 ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL
SEQRES 6 J 343 ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA
SEQRES 7 J 343 ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR
SEQRES 8 J 343 SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR
SEQRES 9 J 343 GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS
SEQRES 10 J 343 ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU
SEQRES 11 J 343 LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU
SEQRES 12 J 343 ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS
SEQRES 13 J 343 ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER
SEQRES 14 J 343 THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA
SEQRES 15 J 343 ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR
SEQRES 16 J 343 GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER
SEQRES 17 J 343 VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS
SEQRES 18 J 343 HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS
SEQRES 19 J 343 ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE
SEQRES 20 J 343 GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU
SEQRES 21 J 343 GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER
SEQRES 22 J 343 GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN
SEQRES 23 J 343 GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL
SEQRES 24 J 343 ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU
SEQRES 25 J 343 GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS
SEQRES 26 J 343 VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO
SEQRES 27 J 343 VAL ASP VAL VAL SER
SEQRES 1 K 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 K 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 K 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 K 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 K 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 K 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 K 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 K 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 K 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 K 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 K 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 L 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 L 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 L 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 L 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 L 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 L 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 L 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 L 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 L 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 L 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 L 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 L 146 LYS TYR HIS
SEQRES 1 M 315 CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU
SEQRES 2 M 315 HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU
SEQRES 3 M 315 ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU
SEQRES 4 M 315 LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO
SEQRES 5 M 315 GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA
SEQRES 6 M 315 ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA
SEQRES 7 M 315 LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS
SEQRES 8 M 315 HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN
SEQRES 9 M 315 TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS
SEQRES 10 M 315 SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU
SEQRES 11 M 315 THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU
SEQRES 12 M 315 LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE
SEQRES 13 M 315 GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU
SEQRES 14 M 315 ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA
SEQRES 15 M 315 GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG
SEQRES 16 M 315 ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL
SEQRES 17 M 315 MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS
SEQRES 18 M 315 TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS
SEQRES 19 M 315 SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR
SEQRES 20 M 315 PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS
SEQRES 21 M 315 TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU
SEQRES 22 M 315 GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE
SEQRES 23 M 315 ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL
SEQRES 24 M 315 LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE
SEQRES 25 M 315 ALA GLU ASN
SEQRES 1 N 146 GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP
SEQRES 2 N 146 PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG
SEQRES 3 N 146 GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU
SEQRES 4 N 146 THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA
SEQRES 5 N 146 ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU
SEQRES 6 N 146 ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL
SEQRES 7 N 146 TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER
SEQRES 8 N 146 TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE
SEQRES 9 N 146 PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER
SEQRES 10 N 146 SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP
SEQRES 11 N 146 TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP
SEQRES 12 N 146 PRO SER LEU
SEQRES 1 O 343 ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA
SEQRES 2 O 343 CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR
SEQRES 3 O 343 LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL
SEQRES 4 O 343 GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA
SEQRES 5 O 343 ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL
SEQRES 6 O 343 ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA
SEQRES 7 O 343 ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR
SEQRES 8 O 343 SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR
SEQRES 9 O 343 GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS
SEQRES 10 O 343 ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU
SEQRES 11 O 343 LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU
SEQRES 12 O 343 ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS
SEQRES 13 O 343 ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER
SEQRES 14 O 343 THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA
SEQRES 15 O 343 ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR
SEQRES 16 O 343 GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER
SEQRES 17 O 343 VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS
SEQRES 18 O 343 HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS
SEQRES 19 O 343 ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE
SEQRES 20 O 343 GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU
SEQRES 21 O 343 GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER
SEQRES 22 O 343 GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN
SEQRES 23 O 343 GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL
SEQRES 24 O 343 ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU
SEQRES 25 O 343 GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS
SEQRES 26 O 343 VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO
SEQRES 27 O 343 VAL ASP VAL VAL SER
SEQRES 1 P 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 P 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 P 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 P 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 P 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 P 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 P 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 P 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 P 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 P 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 P 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 Q 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 Q 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 Q 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 Q 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 Q 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 Q 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 Q 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 Q 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 Q 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 Q 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 Q 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 Q 146 LYS TYR HIS
SEQRES 1 R 315 CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU
SEQRES 2 R 315 HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU
SEQRES 3 R 315 ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU
SEQRES 4 R 315 LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO
SEQRES 5 R 315 GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA
SEQRES 6 R 315 ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA
SEQRES 7 R 315 LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS
SEQRES 8 R 315 HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN
SEQRES 9 R 315 TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS
SEQRES 10 R 315 SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU
SEQRES 11 R 315 THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU
SEQRES 12 R 315 LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE
SEQRES 13 R 315 GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU
SEQRES 14 R 315 ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA
SEQRES 15 R 315 GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG
SEQRES 16 R 315 ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL
SEQRES 17 R 315 MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS
SEQRES 18 R 315 TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS
SEQRES 19 R 315 SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR
SEQRES 20 R 315 PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS
SEQRES 21 R 315 TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU
SEQRES 22 R 315 GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE
SEQRES 23 R 315 ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL
SEQRES 24 R 315 LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE
SEQRES 25 R 315 ALA GLU ASN
SEQRES 1 S 146 GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP
SEQRES 2 S 146 PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG
SEQRES 3 S 146 GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU
SEQRES 4 S 146 THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA
SEQRES 5 S 146 ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU
SEQRES 6 S 146 ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL
SEQRES 7 S 146 TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER
SEQRES 8 S 146 TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE
SEQRES 9 S 146 PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER
SEQRES 10 S 146 SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP
SEQRES 11 S 146 TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP
SEQRES 12 S 146 PRO SER LEU
SEQRES 1 T 343 ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA
SEQRES 2 T 343 CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR
SEQRES 3 T 343 LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL
SEQRES 4 T 343 GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA
SEQRES 5 T 343 ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL
SEQRES 6 T 343 ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA
SEQRES 7 T 343 ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR
SEQRES 8 T 343 SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR
SEQRES 9 T 343 GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS
SEQRES 10 T 343 ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU
SEQRES 11 T 343 LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU
SEQRES 12 T 343 ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS
SEQRES 13 T 343 ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER
SEQRES 14 T 343 THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA
SEQRES 15 T 343 ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR
SEQRES 16 T 343 GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER
SEQRES 17 T 343 VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS
SEQRES 18 T 343 HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS
SEQRES 19 T 343 ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE
SEQRES 20 T 343 GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU
SEQRES 21 T 343 GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER
SEQRES 22 T 343 GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN
SEQRES 23 T 343 GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL
SEQRES 24 T 343 ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU
SEQRES 25 T 343 GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS
SEQRES 26 T 343 VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO
SEQRES 27 T 343 VAL ASP VAL VAL SER
SEQRES 1 U 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 U 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 U 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 U 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 U 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 U 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 U 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 U 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 U 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 U 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 U 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 V 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 V 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 V 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 V 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 V 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 V 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 V 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 V 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 V 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 V 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 V 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 V 146 LYS TYR HIS
SEQRES 1 W 315 CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU
SEQRES 2 W 315 HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU
SEQRES 3 W 315 ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU
SEQRES 4 W 315 LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO
SEQRES 5 W 315 GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA
SEQRES 6 W 315 ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA
SEQRES 7 W 315 LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS
SEQRES 8 W 315 HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN
SEQRES 9 W 315 TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS
SEQRES 10 W 315 SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU
SEQRES 11 W 315 THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU
SEQRES 12 W 315 LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE
SEQRES 13 W 315 GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU
SEQRES 14 W 315 ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA
SEQRES 15 W 315 GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG
SEQRES 16 W 315 ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL
SEQRES 17 W 315 MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS
SEQRES 18 W 315 TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS
SEQRES 19 W 315 SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR
SEQRES 20 W 315 PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS
SEQRES 21 W 315 TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU
SEQRES 22 W 315 GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE
SEQRES 23 W 315 ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL
SEQRES 24 W 315 LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE
SEQRES 25 W 315 ALA GLU ASN
SEQRES 1 X 146 GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP
SEQRES 2 X 146 PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG
SEQRES 3 X 146 GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU
SEQRES 4 X 146 THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA
SEQRES 5 X 146 ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU
SEQRES 6 X 146 ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL
SEQRES 7 X 146 TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER
SEQRES 8 X 146 TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE
SEQRES 9 X 146 PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER
SEQRES 10 X 146 SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP
SEQRES 11 X 146 TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP
SEQRES 12 X 146 PRO SER LEU
SEQRES 1 Y 343 ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA
SEQRES 2 Y 343 CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR
SEQRES 3 Y 343 LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL
SEQRES 4 Y 343 GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA
SEQRES 5 Y 343 ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL
SEQRES 6 Y 343 ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA
SEQRES 7 Y 343 ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR
SEQRES 8 Y 343 SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR
SEQRES 9 Y 343 GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS
SEQRES 10 Y 343 ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU
SEQRES 11 Y 343 LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU
SEQRES 12 Y 343 ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS
SEQRES 13 Y 343 ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER
SEQRES 14 Y 343 THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA
SEQRES 15 Y 343 ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR
SEQRES 16 Y 343 GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER
SEQRES 17 Y 343 VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS
SEQRES 18 Y 343 HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS
SEQRES 19 Y 343 ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE
SEQRES 20 Y 343 GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU
SEQRES 21 Y 343 GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER
SEQRES 22 Y 343 GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN
SEQRES 23 Y 343 GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL
SEQRES 24 Y 343 ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU
SEQRES 25 Y 343 GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS
SEQRES 26 Y 343 VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO
SEQRES 27 Y 343 VAL ASP VAL VAL SER
SEQRES 1 Z 141 VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA
SEQRES 2 Z 141 TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA
SEQRES 3 Z 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR
SEQRES 4 Z 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER
SEQRES 5 Z 141 ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA
SEQRES 6 Z 141 LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN
SEQRES 7 Z 141 ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU
SEQRES 8 Z 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS
SEQRES 9 Z 141 LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE
SEQRES 10 Z 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA
SEQRES 11 Z 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG
SEQRES 1 1 146 VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA
SEQRES 2 1 146 LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU
SEQRES 3 1 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN
SEQRES 4 1 146 ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP
SEQRES 5 1 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS
SEQRES 6 1 146 LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU
SEQRES 7 1 146 ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU
SEQRES 8 1 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG
SEQRES 9 1 146 LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS
SEQRES 10 1 146 PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR
SEQRES 11 1 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS
SEQRES 12 1 146 LYS TYR HIS
SEQRES 1 2 315 CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU
SEQRES 2 2 315 HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU
SEQRES 3 2 315 ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU
SEQRES 4 2 315 LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO
SEQRES 5 2 315 GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA
SEQRES 6 2 315 ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA
SEQRES 7 2 315 LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS
SEQRES 8 2 315 HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN
SEQRES 9 2 315 TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS
SEQRES 10 2 315 SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU
SEQRES 11 2 315 THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU
SEQRES 12 2 315 LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE
SEQRES 13 2 315 GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU
SEQRES 14 2 315 ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA
SEQRES 15 2 315 GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG
SEQRES 16 2 315 ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL
SEQRES 17 2 315 MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS
SEQRES 18 2 315 TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS
SEQRES 19 2 315 SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR
SEQRES 20 2 315 PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS
SEQRES 21 2 315 TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU
SEQRES 22 2 315 GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE
SEQRES 23 2 315 ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL
SEQRES 24 2 315 LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE
SEQRES 25 2 315 ALA GLU ASN
SEQRES 1 3 146 GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP
SEQRES 2 3 146 PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG
SEQRES 3 3 146 GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU
SEQRES 4 3 146 THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA
SEQRES 5 3 146 ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU
SEQRES 6 3 146 ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL
SEQRES 7 3 146 TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER
SEQRES 8 3 146 TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE
SEQRES 9 3 146 PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER
SEQRES 10 3 146 SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP
SEQRES 11 3 146 TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP
SEQRES 12 3 146 PRO SER LEU
SEQRES 1 4 343 ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA
SEQRES 2 4 343 CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR
SEQRES 3 4 343 LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL
SEQRES 4 4 343 GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA
SEQRES 5 4 343 ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL
SEQRES 6 4 343 ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA
SEQRES 7 4 343 ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR
SEQRES 8 4 343 SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR
SEQRES 9 4 343 GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS
SEQRES 10 4 343 ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU
SEQRES 11 4 343 LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU
SEQRES 12 4 343 ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS
SEQRES 13 4 343 ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER
SEQRES 14 4 343 THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA
SEQRES 15 4 343 ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR
SEQRES 16 4 343 GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER
SEQRES 17 4 343 VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS
SEQRES 18 4 343 HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS
SEQRES 19 4 343 ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE
SEQRES 20 4 343 GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU
SEQRES 21 4 343 GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER
SEQRES 22 4 343 GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN
SEQRES 23 4 343 GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL
SEQRES 24 4 343 ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU
SEQRES 25 4 343 GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS
SEQRES 26 4 343 VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO
SEQRES 27 4 343 VAL ASP VAL VAL SER
HET NAG a 1 14
HET NAG a 2 14
HET NAG b 1 14
HET NAG b 2 14
HET NAG c 1 14
HET NAG c 2 14
HET NAG d 1 14
HET NAG d 2 14
HET NAG e 1 14
HET NAG e 2 14
HET NAG f 1 14
HET NAG f 2 14
HET NAG g 1 14
HET NAG g 2 14
HET NAG h 1 14
HET NAG h 2 14
HET NAG i 1 14
HET NAG i 2 14
HET NAG j 1 14
HET NAG j 2 14
HET HEM A 201 43
HET OXY A 202 2
HET HEM B 201 43
HET OXY B 202 2
HET NAG C1001 14
HET NAG C1004 14
HET NAG E1001 14
HET NAG E1002 14
HET HEM F 201 43
HET OXY F 202 2
HET HEM G 201 43
HET OXY G 202 2
HET NAG H1001 14
HET NAG H1002 14
HET NAG J1001 14
HET NAG J1002 14
HET HEM K 201 43
HET OXY K 202 2
HET HEM L 201 43
HET OXY L 202 2
HET NAG M1001 14
HET NAG M1004 14
HET NAG O1001 14
HET NAG O1002 14
HET HEM P 201 43
HET OXY P 202 2
HET HEM Q 201 43
HET OXY Q 202 2
HET NAG R1001 14
HET NAG R1004 14
HET NAG T1001 14
HET NAG T1002 14
HET HEM U 201 43
HET OXY U 202 2
HET HEM V 201 43
HET OXY V 202 2
HET NAG W1001 14
HET NAG W1002 14
HET NAG Y1001 14
HET NAG Y1002 14
HET HEM Z 201 43
HET OXY Z 202 2
HET HEM 1 201 43
HET OXY 1 202 2
HET NAG 21001 14
HET NAG 41001 14
HET NAG 41002 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM OXY OXYGEN MOLECULE
HETSYN HEM HEME
FORMUL 31 NAG 43(C8 H15 N O6)
FORMUL 41 HEM 12(C34 H32 FE N4 O4)
FORMUL 42 OXY 12(O2)
HELIX 1 AA1 SER A 3 LYS A 16 1 14
HELIX 2 AA2 VAL A 17 ALA A 19 5 3
HELIX 3 AA3 HIS A 20 PHE A 36 1 17
HELIX 4 AA4 PRO A 37 PHE A 43 5 7
HELIX 5 AA5 SER A 52 HIS A 72 1 21
HELIX 6 AA6 ASP A 75 HIS A 89 1 15
HELIX 7 AA7 PRO A 95 LEU A 113 1 19
HELIX 8 AA8 PRO A 114 PHE A 117 5 4
HELIX 9 AA9 THR A 118 SER A 138 1 21
HELIX 10 AB1 THR B 4 VAL B 18 1 15
HELIX 11 AB2 GLU B 22 TYR B 35 1 14
HELIX 12 AB3 THR B 38 GLU B 43 1 6
HELIX 13 AB4 SER B 44 GLY B 46 5 3
HELIX 14 AB5 THR B 50 ASN B 57 1 8
HELIX 15 AB6 ASN B 57 HIS B 77 1 21
HELIX 16 AB7 ASN B 80 PHE B 85 1 6
HELIX 17 AB8 PHE B 85 ASP B 94 1 10
HELIX 18 AB9 PRO B 100 GLY B 119 1 20
HELIX 19 AC1 LYS B 120 PHE B 122 5 3
HELIX 20 AC2 THR B 123 ALA B 142 1 20
HELIX 21 AC3 HIS B 143 HIS B 146 5 4
HELIX 22 AC4 THR C 196 PHE C 201 1 6
HELIX 23 AC5 THR C 209 ALA C 214 1 6
HELIX 24 AC6 ASP C 301 GLU C 310 1 10
HELIX 25 AC7 ILE C 391 ALA C 400 1 10
HELIX 26 AC8 SER D 89 ILE D 94 1 6
HELIX 27 AC9 LYS D 95 GLU D 100 5 6
HELIX 28 AD1 GLN D 124 ILE D 131 1 8
HELIX 29 AD2 THR D 152 SER D 154 5 3
HELIX 30 AD3 THR E 41 THR E 69 1 29
HELIX 31 AD4 THR E 69 VAL E 90 1 22
HELIX 32 AD5 VAL E 90 ALA E 103 1 14
HELIX 33 AD6 GLN E 105 GLU E 109 5 5
HELIX 34 AD7 LYS E 120 ILE E 125 1 6
HELIX 35 AD8 ILE E 125 ALA E 181 1 57
HELIX 36 AD9 ALA E 188 LYS E 196 1 9
HELIX 37 AE1 SER E 206 ASN E 219 1 14
HELIX 38 AE2 HIS E 226 ALA E 271 1 46
HELIX 39 AE3 ALA E 271 ALA E 280 1 10
HELIX 40 AE4 GLU E 281 GLU E 283 5 3
HELIX 41 AE5 LYS E 286 GLN E 294 1 9
HELIX 42 AE6 SER F 3 LYS F 16 1 14
HELIX 43 AE7 VAL F 17 ALA F 19 5 3
HELIX 44 AE8 HIS F 20 PHE F 36 1 17
HELIX 45 AE9 PRO F 37 PHE F 43 5 7
HELIX 46 AF1 SER F 52 HIS F 72 1 21
HELIX 47 AF2 ASP F 75 HIS F 89 1 15
HELIX 48 AF3 PRO F 95 LEU F 113 1 19
HELIX 49 AF4 PRO F 114 PHE F 117 5 4
HELIX 50 AF5 THR F 118 SER F 138 1 21
HELIX 51 AF6 THR G 4 LYS G 17 1 14
HELIX 52 AF7 GLU G 22 TYR G 35 1 14
HELIX 53 AF8 THR G 38 GLU G 43 1 6
HELIX 54 AF9 SER G 44 GLY G 46 5 3
HELIX 55 AG1 THR G 50 ASN G 57 1 8
HELIX 56 AG2 ASN G 57 HIS G 77 1 21
HELIX 57 AG3 ASN G 80 PHE G 85 1 6
HELIX 58 AG4 PHE G 85 ASP G 94 1 10
HELIX 59 AG5 PRO G 100 GLY G 119 1 20
HELIX 60 AG6 LYS G 120 PHE G 122 5 3
HELIX 61 AG7 THR G 123 ALA G 142 1 20
HELIX 62 AG8 HIS G 143 HIS G 146 5 4
HELIX 63 AG9 THR H 196 PHE H 201 1 6
HELIX 64 AH1 THR H 209 ALA H 214 1 6
HELIX 65 AH2 PRO H 215 LEU H 217 5 3
HELIX 66 AH3 ASP H 301 GLU H 310 1 10
HELIX 67 AH4 ILE H 391 ALA H 400 1 10
HELIX 68 AH5 SER I 89 ILE I 94 1 6
HELIX 69 AH6 LYS I 95 GLU I 100 5 6
HELIX 70 AH7 GLN I 124 ILE I 131 1 8
HELIX 71 AH8 THR I 152 SER I 154 5 3
HELIX 72 AH9 ASP J 43 THR J 69 1 27
HELIX 73 AI1 THR J 69 VAL J 90 1 22
HELIX 74 AI2 VAL J 90 ALA J 103 1 14
HELIX 75 AI3 LYS J 120 ILE J 125 1 6
HELIX 76 AI4 ILE J 125 VAL J 174 1 50
HELIX 77 AI5 TRP J 175 ALA J 181 1 7
HELIX 78 AI6 ALA J 188 LYS J 196 1 9
HELIX 79 AI7 SER J 206 ASN J 219 1 14
HELIX 80 AI8 HIS J 226 ALA J 271 1 46
HELIX 81 AI9 ALA J 271 ALA J 280 1 10
HELIX 82 AJ1 GLU J 281 GLU J 283 5 3
HELIX 83 AJ2 LYS J 286 GLN J 294 1 9
HELIX 84 AJ3 SER K 3 LYS K 16 1 14
HELIX 85 AJ4 VAL K 17 ALA K 19 5 3
HELIX 86 AJ5 HIS K 20 PHE K 36 1 17
HELIX 87 AJ6 PRO K 37 PHE K 43 5 7
HELIX 88 AJ7 SER K 52 HIS K 72 1 21
HELIX 89 AJ8 ASP K 75 HIS K 89 1 15
HELIX 90 AJ9 PRO K 95 LEU K 113 1 19
HELIX 91 AK1 PRO K 114 PHE K 117 5 4
HELIX 92 AK2 THR K 118 SER K 138 1 21
HELIX 93 AK3 THR L 4 VAL L 18 1 15
HELIX 94 AK4 GLU L 22 TYR L 35 1 14
HELIX 95 AK5 THR L 38 GLU L 43 1 6
HELIX 96 AK6 SER L 44 GLY L 46 5 3
HELIX 97 AK7 THR L 50 ASN L 57 1 8
HELIX 98 AK8 ASN L 57 HIS L 77 1 21
HELIX 99 AK9 ASN L 80 PHE L 85 1 6
HELIX 100 AL1 PHE L 85 ASP L 94 1 10
HELIX 101 AL2 PRO L 100 GLY L 119 1 20
HELIX 102 AL3 LYS L 120 PHE L 122 5 3
HELIX 103 AL4 THR L 123 ALA L 142 1 20
HELIX 104 AL5 HIS L 143 HIS L 146 5 4
HELIX 105 AL6 THR M 196 PHE M 201 1 6
HELIX 106 AL7 THR M 209 ALA M 214 1 6
HELIX 107 AL8 ASP M 301 GLU M 310 1 10
HELIX 108 AL9 ILE M 391 ALA M 400 1 10
HELIX 109 AM1 SER N 89 ILE N 94 1 6
HELIX 110 AM2 LYS N 95 GLU N 100 5 6
HELIX 111 AM3 GLN N 124 ILE N 131 1 8
HELIX 112 AM4 THR N 152 SER N 154 5 3
HELIX 113 AM5 ASP O 43 THR O 69 1 27
HELIX 114 AM6 THR O 69 VAL O 90 1 22
HELIX 115 AM7 VAL O 90 ALA O 103 1 14
HELIX 116 AM8 GLN O 105 GLU O 109 5 5
HELIX 117 AM9 LYS O 120 ILE O 125 1 6
HELIX 118 AN1 ILE O 125 ALA O 181 1 57
HELIX 119 AN2 ALA O 188 LYS O 196 1 9
HELIX 120 AN3 SER O 206 ASN O 219 1 14
HELIX 121 AN4 HIS O 226 ALA O 271 1 46
HELIX 122 AN5 ALA O 271 ALA O 280 1 10
HELIX 123 AN6 GLU O 281 GLU O 283 5 3
HELIX 124 AN7 LYS O 286 GLN O 294 1 9
HELIX 125 AN8 SER P 3 LYS P 16 1 14
HELIX 126 AN9 VAL P 17 ALA P 19 5 3
HELIX 127 AO1 HIS P 20 PHE P 36 1 17
HELIX 128 AO2 PRO P 37 PHE P 43 5 7
HELIX 129 AO3 SER P 52 HIS P 72 1 21
HELIX 130 AO4 ASP P 75 LEU P 80 1 6
HELIX 131 AO5 LEU P 80 HIS P 89 1 10
HELIX 132 AO6 PRO P 95 LEU P 113 1 19
HELIX 133 AO7 PRO P 114 PHE P 117 5 4
HELIX 134 AO8 THR P 118 SER P 138 1 21
HELIX 135 AO9 THR Q 4 LYS Q 17 1 14
HELIX 136 AP1 GLU Q 22 TYR Q 35 1 14
HELIX 137 AP2 THR Q 38 GLU Q 43 1 6
HELIX 138 AP3 SER Q 44 GLY Q 46 5 3
HELIX 139 AP4 THR Q 50 ASN Q 57 1 8
HELIX 140 AP5 ASN Q 57 HIS Q 77 1 21
HELIX 141 AP6 ASN Q 80 PHE Q 85 1 6
HELIX 142 AP7 PHE Q 85 ASP Q 94 1 10
HELIX 143 AP8 PRO Q 100 GLY Q 119 1 20
HELIX 144 AP9 LYS Q 120 PHE Q 122 5 3
HELIX 145 AQ1 THR Q 123 ALA Q 142 1 20
HELIX 146 AQ2 HIS Q 143 HIS Q 146 5 4
HELIX 147 AQ3 THR R 196 PHE R 201 1 6
HELIX 148 AQ4 THR R 209 ALA R 214 1 6
HELIX 149 AQ5 ASP R 301 GLU R 310 1 10
HELIX 150 AQ6 ILE R 391 ALA R 400 1 10
HELIX 151 AQ7 SER S 89 ILE S 94 1 6
HELIX 152 AQ8 LYS S 95 GLU S 100 5 6
HELIX 153 AQ9 GLN S 124 ILE S 131 1 8
HELIX 154 AR1 THR S 152 SER S 154 5 3
HELIX 155 AR2 THR T 41 THR T 69 1 29
HELIX 156 AR3 THR T 69 VAL T 90 1 22
HELIX 157 AR4 VAL T 90 ALA T 103 1 14
HELIX 158 AR5 LYS T 120 ILE T 125 1 6
HELIX 159 AR6 ILE T 125 ALA T 181 1 57
HELIX 160 AR7 ALA T 188 LYS T 196 1 9
HELIX 161 AR8 SER T 206 ASN T 219 1 14
HELIX 162 AR9 HIS T 226 ALA T 271 1 46
HELIX 163 AS1 ALA T 271 ALA T 280 1 10
HELIX 164 AS2 GLU T 281 GLU T 283 5 3
HELIX 165 AS3 LYS T 286 GLN T 294 1 9
HELIX 166 AS4 SER U 3 LYS U 16 1 14
HELIX 167 AS5 VAL U 17 ALA U 19 5 3
HELIX 168 AS6 HIS U 20 PHE U 36 1 17
HELIX 169 AS7 PRO U 37 PHE U 43 5 7
HELIX 170 AS8 SER U 52 HIS U 72 1 21
HELIX 171 AS9 ASP U 75 LEU U 80 1 6
HELIX 172 AT1 LEU U 80 HIS U 89 1 10
HELIX 173 AT2 PRO U 95 LEU U 113 1 19
HELIX 174 AT3 PRO U 114 PHE U 117 5 4
HELIX 175 AT4 THR U 118 SER U 138 1 21
HELIX 176 AT5 THR V 4 VAL V 18 1 15
HELIX 177 AT6 GLU V 22 TYR V 35 1 14
HELIX 178 AT7 THR V 38 GLU V 43 1 6
HELIX 179 AT8 SER V 44 GLY V 46 5 3
HELIX 180 AT9 THR V 50 ASN V 57 1 8
HELIX 181 AU1 ASN V 57 HIS V 77 1 21
HELIX 182 AU2 ASN V 80 PHE V 85 1 6
HELIX 183 AU3 PHE V 85 ASP V 94 1 10
HELIX 184 AU4 PRO V 100 GLY V 119 1 20
HELIX 185 AU5 LYS V 120 PHE V 122 5 3
HELIX 186 AU6 THR V 123 ALA V 142 1 20
HELIX 187 AU7 HIS V 143 HIS V 146 5 4
HELIX 188 AU8 THR W 196 PHE W 201 1 6
HELIX 189 AU9 THR W 209 ALA W 214 1 6
HELIX 190 AV1 ASP W 301 GLU W 310 1 10
HELIX 191 AV2 ILE W 391 ALA W 400 1 10
HELIX 192 AV3 SER X 89 ILE X 94 1 6
HELIX 193 AV4 LYS X 95 GLU X 100 5 6
HELIX 194 AV5 GLN X 124 ILE X 131 1 8
HELIX 195 AV6 THR X 152 SER X 154 5 3
HELIX 196 AV7 THR Y 41 THR Y 69 1 29
HELIX 197 AV8 THR Y 69 VAL Y 90 1 22
HELIX 198 AV9 VAL Y 90 ALA Y 103 1 14
HELIX 199 AW1 LYS Y 120 ILE Y 125 1 6
HELIX 200 AW2 ILE Y 125 ALA Y 181 1 57
HELIX 201 AW3 ALA Y 188 LYS Y 196 1 9
HELIX 202 AW4 SER Y 206 ASN Y 219 1 14
HELIX 203 AW5 HIS Y 226 ALA Y 271 1 46
HELIX 204 AW6 ALA Y 271 ALA Y 280 1 10
HELIX 205 AW7 GLU Y 281 GLU Y 283 5 3
HELIX 206 AW8 LYS Y 286 GLN Y 294 1 9
HELIX 207 AW9 SER Z 3 LYS Z 16 1 14
HELIX 208 AX1 VAL Z 17 ALA Z 19 5 3
HELIX 209 AX2 HIS Z 20 PHE Z 36 1 17
HELIX 210 AX3 PRO Z 37 PHE Z 43 5 7
HELIX 211 AX4 SER Z 52 HIS Z 72 1 21
HELIX 212 AX5 ASP Z 75 HIS Z 89 1 15
HELIX 213 AX6 PRO Z 95 LEU Z 113 1 19
HELIX 214 AX7 PRO Z 114 PHE Z 117 5 4
HELIX 215 AX8 THR Z 118 SER Z 138 1 21
HELIX 216 AX9 THR 1 4 VAL 1 18 1 15
HELIX 217 AY1 GLU 1 22 TYR 1 35 1 14
HELIX 218 AY2 THR 1 38 GLU 1 43 1 6
HELIX 219 AY3 SER 1 44 GLY 1 46 5 3
HELIX 220 AY4 THR 1 50 ASN 1 57 1 8
HELIX 221 AY5 ASN 1 57 HIS 1 77 1 21
HELIX 222 AY6 ASN 1 80 PHE 1 85 1 6
HELIX 223 AY7 PHE 1 85 ASP 1 94 1 10
HELIX 224 AY8 PRO 1 100 GLY 1 119 1 20
HELIX 225 AY9 LYS 1 120 PHE 1 122 5 3
HELIX 226 AZ1 THR 1 123 ALA 1 142 1 20
HELIX 227 AZ2 HIS 1 143 HIS 1 146 5 4
HELIX 228 AZ3 THR 2 196 PHE 2 201 1 6
HELIX 229 AZ4 THR 2 209 ALA 2 214 1 6
HELIX 230 AZ5 ASP 2 301 GLU 2 310 1 10
HELIX 231 AZ6 ILE 2 391 ALA 2 400 1 10
HELIX 232 AZ7 SER 3 89 ILE 3 94 1 6
HELIX 233 AZ8 LYS 3 95 GLU 3 100 5 6
HELIX 234 AZ9 GLN 3 124 ILE 3 131 1 8
HELIX 235 BA1 THR 3 152 SER 3 154 5 3
HELIX 236 BA2 THR 4 41 THR 4 69 1 29
HELIX 237 BA3 THR 4 69 VAL 4 90 1 22
HELIX 238 BA4 VAL 4 90 ALA 4 103 1 14
HELIX 239 BA5 GLN 4 105 GLU 4 109 5 5
HELIX 240 BA6 LYS 4 120 ILE 4 125 1 6
HELIX 241 BA7 ILE 4 125 ALA 4 181 1 57
HELIX 242 BA8 ALA 4 188 LYS 4 196 1 9
HELIX 243 BA9 SER 4 206 ASN 4 219 1 14
HELIX 244 BB1 HIS 4 226 ALA 4 271 1 46
HELIX 245 BB2 ALA 4 271 ALA 4 280 1 10
HELIX 246 BB3 GLU 4 281 GLU 4 283 5 3
HELIX 247 BB4 LYS 4 286 GLN 4 294 1 9
SHEET 1 AA1 6 TRP C 133 ILE C 134 0
SHEET 2 AA1 6 VAL C 124 LEU C 127 -1 N THR C 126 O ILE C 134
SHEET 3 AA1 6 GLY C 101 CYS C 111 -1 N HIS C 105 O LEU C 127
SHEET 4 AA1 6 GLY H 101 CYS H 111 -1 O TYR H 102 N GLN C 110
SHEET 5 AA1 6 VAL H 124 LEU H 127 -1 O TYR H 125 N VAL H 107
SHEET 6 AA1 6 TRP H 133 ILE H 134 -1 O ILE H 134 N THR H 126
SHEET 1 AA2 2 TYR C 115 ARG C 118 0
SHEET 2 AA2 2 GLU C 144 ALA C 147 -1 O GLU C 146 N LYS C 116
SHEET 1 AA3 7 GLN C 225 LEU C 226 0
SHEET 2 AA3 7 THR C 218 VAL C 221 -1 N VAL C 221 O GLN C 225
SHEET 3 AA3 7 GLN C 172 VAL C 176 -1 N LYS C 174 O TYR C 220
SHEET 4 AA3 7 THR C 182 ASN C 189 -1 O THR C 183 N MET C 175
SHEET 5 AA3 7 TRP C 192 THR C 195 -1 O LEU C 194 N THR C 186
SHEET 6 AA3 7 GLY C 244 LEU C 248 -1 O GLY C 244 N THR C 195
SHEET 7 AA3 7 ILE C 229 LEU C 234 -1 N VAL C 233 O LEU C 245
SHEET 1 AA4 7 VAL C 274 GLY C 279 0
SHEET 2 AA4 7 LYS C 293 ALA C 300 -1 O VAL C 295 N VAL C 277
SHEET 3 AA4 7 THR C 334 ALA C 337 -1 O CYS C 336 N ALA C 300
SHEET 4 AA4 7 GLY C 383 LYS C 387 -1 O TYR C 385 N PHE C 335
SHEET 5 AA4 7 THR C 364 PHE C 373 -1 N SER C 372 O VAL C 384
SHEET 6 AA4 7 ALA C 354 ASP C 359 -1 N PHE C 355 O GLY C 369
SHEET 7 AA4 7 VAL C 274 GLY C 279 -1 N TYR C 276 O ALA C 356
SHEET 1 AA5 5 ARG D 109 VAL D 112 0
SHEET 2 AA5 5 ALA D 135 TYR D 138 -1 O VAL D 137 N GLU D 110
SHEET 3 AA5 5 ALA D 144 ILE D 150 -1 O GLU D 145 N TYR D 138
SHEET 4 AA5 5 HIS D 182 VAL D 189 -1 O ALA D 183 N ILE D 150
SHEET 5 AA5 5 ARG D 171 SER D 176 -1 N VAL D 173 O TYR D 184
SHEET 1 AA6 5 PHE D 114 LEU D 117 0
SHEET 2 AA6 5 LYS D 216 PHE D 219 -1 O LYS D 216 N LEU D 117
SHEET 3 AA6 5 GLU D 195 GLN D 203 -1 N LEU D 196 O LEU D 217
SHEET 4 AA6 5 TRP D 156 GLU D 163 -1 N TYR D 162 O LYS D 197
SHEET 5 AA6 5 GLN D 166 LYS D 167 -1 O GLN D 166 N GLU D 163
SHEET 1 AA7 4 PHE D 114 LEU D 117 0
SHEET 2 AA7 4 LYS D 216 PHE D 219 -1 O LYS D 216 N LEU D 117
SHEET 3 AA7 4 GLU D 195 GLN D 203 -1 N LEU D 196 O LEU D 217
SHEET 4 AA7 4 GLU D 209 TYR D 212 -1 O TYR D 212 N SER D 200
SHEET 1 AA8 2 TYR H 115 ARG H 118 0
SHEET 2 AA8 2 GLU H 144 ALA H 147 -1 O GLU H 146 N LYS H 116
SHEET 1 AA9 7 GLN H 225 VAL H 227 0
SHEET 2 AA9 7 THR H 218 VAL H 221 -1 N VAL H 221 O GLN H 225
SHEET 3 AA9 7 GLN H 172 VAL H 176 -1 N LYS H 174 O TYR H 220
SHEET 4 AA9 7 THR H 182 ASN H 189 -1 O THR H 183 N MET H 175
SHEET 5 AA9 7 TRP H 192 THR H 195 -1 O LEU H 194 N THR H 186
SHEET 6 AA9 7 GLY H 244 LEU H 248 -1 O ILE H 246 N LEU H 193
SHEET 7 AA9 7 ILE H 229 LEU H 234 -1 N VAL H 233 O LEU H 245
SHEET 1 AB1 7 VAL H 274 GLY H 279 0
SHEET 2 AB1 7 LYS H 293 ALA H 300 -1 O VAL H 295 N VAL H 277
SHEET 3 AB1 7 THR H 334 ALA H 337 -1 O CYS H 336 N ALA H 300
SHEET 4 AB1 7 GLY H 383 LYS H 387 -1 O TYR H 385 N PHE H 335
SHEET 5 AB1 7 THR H 364 PHE H 373 -1 N SER H 372 O VAL H 384
SHEET 6 AB1 7 ALA H 354 ASP H 359 -1 N PHE H 355 O GLY H 369
SHEET 7 AB1 7 VAL H 274 GLY H 279 -1 N TYR H 276 O ALA H 356
SHEET 1 AB2 5 ARG I 109 VAL I 112 0
SHEET 2 AB2 5 ALA I 135 TYR I 138 -1 O VAL I 137 N GLU I 110
SHEET 3 AB2 5 ALA I 144 ILE I 150 -1 O GLU I 145 N TYR I 138
SHEET 4 AB2 5 HIS I 182 VAL I 189 -1 O ALA I 183 N ILE I 150
SHEET 5 AB2 5 ARG I 171 SER I 176 -1 N VAL I 173 O TYR I 184
SHEET 1 AB3 5 PHE I 114 LEU I 117 0
SHEET 2 AB3 5 LYS I 216 PHE I 219 -1 O LYS I 216 N LEU I 117
SHEET 3 AB3 5 GLU I 195 GLN I 203 -1 N LEU I 196 O LEU I 217
SHEET 4 AB3 5 TRP I 156 GLU I 163 -1 N LYS I 157 O SER I 201
SHEET 5 AB3 5 GLN I 166 LYS I 167 -1 O GLN I 166 N GLU I 163
SHEET 1 AB4 4 PHE I 114 LEU I 117 0
SHEET 2 AB4 4 LYS I 216 PHE I 219 -1 O LYS I 216 N LEU I 117
SHEET 3 AB4 4 GLU I 195 GLN I 203 -1 N LEU I 196 O LEU I 217
SHEET 4 AB4 4 GLU I 209 TYR I 212 -1 O TYR I 212 N SER I 200
SHEET 1 AB5 6 TRP M 133 ILE M 134 0
SHEET 2 AB5 6 VAL M 124 LEU M 127 -1 N THR M 126 O ILE M 134
SHEET 3 AB5 6 GLY M 101 CYS M 111 -1 N VAL M 107 O TYR M 125
SHEET 4 AB5 6 GLY R 101 CYS R 111 -1 O TYR R 102 N GLN M 110
SHEET 5 AB5 6 VAL R 124 LEU R 127 -1 O TYR R 125 N VAL R 107
SHEET 6 AB5 6 TRP R 133 ILE R 134 -1 O ILE R 134 N THR R 126
SHEET 1 AB6 2 TYR M 115 ARG M 118 0
SHEET 2 AB6 2 GLU M 144 ALA M 147 -1 O GLU M 146 N LYS M 116
SHEET 1 AB7 7 GLN M 225 LEU M 226 0
SHEET 2 AB7 7 THR M 218 VAL M 221 -1 N VAL M 221 O GLN M 225
SHEET 3 AB7 7 GLN M 172 VAL M 176 -1 N VAL M 176 O THR M 218
SHEET 4 AB7 7 THR M 182 LEU M 187 -1 O THR M 183 N MET M 175
SHEET 5 AB7 7 TRP M 192 THR M 195 -1 O LEU M 194 N THR M 186
SHEET 6 AB7 7 GLY M 244 LEU M 248 -1 O GLY M 244 N THR M 195
SHEET 7 AB7 7 ILE M 229 LEU M 234 -1 N VAL M 233 O LEU M 245
SHEET 1 AB8 7 VAL M 274 GLY M 279 0
SHEET 2 AB8 7 LYS M 293 ALA M 300 -1 O VAL M 295 N VAL M 277
SHEET 3 AB8 7 THR M 334 ALA M 337 -1 O CYS M 336 N ALA M 300
SHEET 4 AB8 7 GLY M 383 LYS M 387 -1 O TYR M 385 N PHE M 335
SHEET 5 AB8 7 THR M 364 PHE M 373 -1 N SER M 372 O VAL M 384
SHEET 6 AB8 7 ALA M 354 ASP M 359 -1 N PHE M 355 O GLY M 369
SHEET 7 AB8 7 VAL M 274 GLY M 279 -1 N TYR M 276 O ALA M 356
SHEET 1 AB9 5 ARG N 109 VAL N 112 0
SHEET 2 AB9 5 ALA N 135 TYR N 138 -1 O VAL N 137 N GLU N 110
SHEET 3 AB9 5 ALA N 144 ILE N 150 -1 O GLU N 145 N TYR N 138
SHEET 4 AB9 5 HIS N 182 VAL N 189 -1 O ALA N 183 N ILE N 150
SHEET 5 AB9 5 ARG N 171 SER N 176 -1 N VAL N 173 O TYR N 184
SHEET 1 AC1 5 PHE N 114 LEU N 117 0
SHEET 2 AC1 5 GLU N 209 PHE N 219 -1 O LYS N 216 N LEU N 117
SHEET 3 AC1 5 GLU N 195 GLN N 203 -1 N LEU N 196 O LEU N 217
SHEET 4 AC1 5 TRP N 156 GLU N 163 -1 N LYS N 157 O SER N 201
SHEET 5 AC1 5 GLN N 166 LYS N 167 -1 O GLN N 166 N GLU N 163
SHEET 1 AC2 2 TYR R 115 ARG R 118 0
SHEET 2 AC2 2 GLU R 144 ALA R 147 -1 O GLU R 146 N LYS R 116
SHEET 1 AC3 7 GLN R 225 VAL R 227 0
SHEET 2 AC3 7 THR R 218 VAL R 221 -1 N VAL R 221 O GLN R 225
SHEET 3 AC3 7 GLN R 172 VAL R 176 -1 N LYS R 174 O TYR R 220
SHEET 4 AC3 7 THR R 182 LEU R 187 -1 O THR R 183 N MET R 175
SHEET 5 AC3 7 TRP R 192 THR R 195 -1 O LEU R 194 N THR R 186
SHEET 6 AC3 7 GLY R 244 LEU R 248 -1 O GLY R 244 N THR R 195
SHEET 7 AC3 7 ILE R 229 LEU R 234 -1 N VAL R 233 O LEU R 245
SHEET 1 AC4 7 VAL R 274 GLY R 279 0
SHEET 2 AC4 7 LYS R 293 ALA R 300 -1 O VAL R 295 N VAL R 277
SHEET 3 AC4 7 THR R 334 ALA R 337 -1 O CYS R 336 N ALA R 300
SHEET 4 AC4 7 GLY R 383 LYS R 387 -1 O TYR R 385 N PHE R 335
SHEET 5 AC4 7 THR R 364 PHE R 373 -1 N SER R 372 O VAL R 384
SHEET 6 AC4 7 ALA R 354 ASP R 359 -1 N PHE R 355 O GLY R 369
SHEET 7 AC4 7 VAL R 274 GLY R 279 -1 N TYR R 276 O ALA R 356
SHEET 1 AC5 5 ARG S 109 VAL S 112 0
SHEET 2 AC5 5 ALA S 135 TYR S 138 -1 O VAL S 137 N GLU S 110
SHEET 3 AC5 5 ALA S 144 ILE S 150 -1 O GLU S 145 N TYR S 138
SHEET 4 AC5 5 HIS S 182 VAL S 189 -1 O ALA S 183 N ILE S 150
SHEET 5 AC5 5 ARG S 171 SER S 176 -1 N VAL S 173 O TYR S 184
SHEET 1 AC6 5 PHE S 114 LEU S 117 0
SHEET 2 AC6 5 LYS S 216 PHE S 219 -1 O LYS S 216 N LEU S 117
SHEET 3 AC6 5 GLU S 195 GLN S 203 -1 N LEU S 196 O LEU S 217
SHEET 4 AC6 5 TRP S 156 GLU S 163 -1 N LYS S 157 O SER S 201
SHEET 5 AC6 5 GLN S 166 LYS S 167 -1 O GLN S 166 N GLU S 163
SHEET 1 AC7 4 PHE S 114 LEU S 117 0
SHEET 2 AC7 4 LYS S 216 PHE S 219 -1 O LYS S 216 N LEU S 117
SHEET 3 AC7 4 GLU S 195 GLN S 203 -1 N LEU S 196 O LEU S 217
SHEET 4 AC7 4 GLU S 209 TYR S 212 -1 O TYR S 212 N SER S 200
SHEET 1 AC8 6 TRP W 133 ILE W 134 0
SHEET 2 AC8 6 VAL W 124 LEU W 127 -1 N THR W 126 O ILE W 134
SHEET 3 AC8 6 GLY W 101 CYS W 111 -1 N VAL W 107 O TYR W 125
SHEET 4 AC8 6 GLY 2 101 CYS 2 111 -1 O TYR 2 102 N GLN W 110
SHEET 5 AC8 6 VAL 2 124 LEU 2 127 -1 O TYR 2 125 N VAL 2 107
SHEET 6 AC8 6 TRP 2 133 ILE 2 134 -1 O ILE 2 134 N THR 2 126
SHEET 1 AC9 2 TYR W 115 ARG W 118 0
SHEET 2 AC9 2 GLU W 144 ALA W 147 -1 O GLU W 146 N LYS W 116
SHEET 1 AD1 7 GLN W 225 LEU W 226 0
SHEET 2 AD1 7 THR W 218 VAL W 221 -1 N VAL W 221 O GLN W 225
SHEET 3 AD1 7 GLN W 172 VAL W 176 -1 N LYS W 174 O TYR W 220
SHEET 4 AD1 7 THR W 182 LEU W 187 -1 O THR W 183 N MET W 175
SHEET 5 AD1 7 TRP W 192 THR W 195 -1 O LEU W 194 N THR W 186
SHEET 6 AD1 7 GLY W 244 LEU W 248 -1 O GLY W 244 N THR W 195
SHEET 7 AD1 7 ILE W 229 LEU W 234 -1 N VAL W 233 O LEU W 245
SHEET 1 AD2 7 VAL W 274 GLY W 279 0
SHEET 2 AD2 7 LYS W 293 ALA W 300 -1 O VAL W 295 N VAL W 277
SHEET 3 AD2 7 THR W 334 ALA W 337 -1 O CYS W 336 N ALA W 300
SHEET 4 AD2 7 GLY W 383 LYS W 387 -1 O TYR W 385 N PHE W 335
SHEET 5 AD2 7 THR W 364 PHE W 373 -1 N SER W 372 O VAL W 384
SHEET 6 AD2 7 ALA W 354 ASP W 359 -1 N PHE W 355 O GLY W 369
SHEET 7 AD2 7 VAL W 274 GLY W 279 -1 N TYR W 276 O ALA W 356
SHEET 1 AD3 5 ARG X 109 VAL X 112 0
SHEET 2 AD3 5 ALA X 135 TYR X 138 -1 O VAL X 137 N GLU X 110
SHEET 3 AD3 5 ALA X 144 ILE X 150 -1 O GLU X 145 N TYR X 138
SHEET 4 AD3 5 HIS X 182 VAL X 189 -1 O ALA X 183 N ILE X 150
SHEET 5 AD3 5 ARG X 171 SER X 176 -1 N VAL X 173 O TYR X 184
SHEET 1 AD4 4 PHE X 114 LEU X 117 0
SHEET 2 AD4 4 LYS X 216 PHE X 219 -1 O LYS X 216 N LEU X 117
SHEET 3 AD4 4 GLU X 195 GLN X 203 -1 N LEU X 196 O LEU X 217
SHEET 4 AD4 4 TRP X 156 TYR X 162 -1 N LYS X 157 O SER X 201
SHEET 1 AD5 4 PHE X 114 LEU X 117 0
SHEET 2 AD5 4 LYS X 216 PHE X 219 -1 O LYS X 216 N LEU X 117
SHEET 3 AD5 4 GLU X 195 GLN X 203 -1 N LEU X 196 O LEU X 217
SHEET 4 AD5 4 GLU X 209 TYR X 212 -1 O TYR X 212 N SER X 200
SHEET 1 AD6 2 TYR 2 115 ARG 2 118 0
SHEET 2 AD6 2 GLU 2 144 ALA 2 147 -1 O GLU 2 146 N LYS 2 116
SHEET 1 AD7 7 GLN 2 225 VAL 2 227 0
SHEET 2 AD7 7 THR 2 218 VAL 2 221 -1 N VAL 2 221 O GLN 2 225
SHEET 3 AD7 7 GLN 2 172 VAL 2 176 -1 N LYS 2 174 O TYR 2 220
SHEET 4 AD7 7 THR 2 182 LEU 2 187 -1 O THR 2 183 N MET 2 175
SHEET 5 AD7 7 TRP 2 192 THR 2 195 -1 O LEU 2 194 N THR 2 186
SHEET 6 AD7 7 GLY 2 244 LEU 2 248 -1 O ILE 2 246 N LEU 2 193
SHEET 7 AD7 7 ILE 2 229 LEU 2 234 -1 N VAL 2 233 O LEU 2 245
SHEET 1 AD8 7 VAL 2 274 GLY 2 279 0
SHEET 2 AD8 7 LYS 2 293 ALA 2 300 -1 O VAL 2 295 N VAL 2 277
SHEET 3 AD8 7 THR 2 334 ALA 2 337 -1 O CYS 2 336 N ALA 2 300
SHEET 4 AD8 7 GLY 2 383 LYS 2 387 -1 O TYR 2 385 N PHE 2 335
SHEET 5 AD8 7 THR 2 364 PHE 2 373 -1 N SER 2 372 O VAL 2 384
SHEET 6 AD8 7 ALA 2 354 ASP 2 359 -1 N PHE 2 355 O GLY 2 369
SHEET 7 AD8 7 VAL 2 274 GLY 2 279 -1 N TYR 2 276 O ALA 2 356
SHEET 1 AD9 5 ARG 3 109 VAL 3 112 0
SHEET 2 AD9 5 ALA 3 135 TYR 3 138 -1 O VAL 3 137 N GLU 3 110
SHEET 3 AD9 5 ALA 3 144 ILE 3 150 -1 O GLU 3 145 N TYR 3 138
SHEET 4 AD9 5 HIS 3 182 VAL 3 189 -1 O ALA 3 183 N ILE 3 150
SHEET 5 AD9 5 ARG 3 171 SER 3 176 -1 N VAL 3 173 O TYR 3 184
SHEET 1 AE1 5 PHE 3 114 LEU 3 117 0
SHEET 2 AE1 5 GLU 3 209 PHE 3 219 -1 O LYS 3 216 N LEU 3 117
SHEET 3 AE1 5 GLU 3 195 GLN 3 203 -1 N LEU 3 196 O LEU 3 217
SHEET 4 AE1 5 TRP 3 156 GLU 3 163 -1 N LYS 3 157 O SER 3 201
SHEET 5 AE1 5 GLN 3 166 LYS 3 167 -1 O GLN 3 166 N GLU 3 163
SSBOND 1 CYS C 92 CYS H 92 1555 1555 2.07
SSBOND 2 CYS C 111 CYS C 145 1555 1555 2.03
SSBOND 3 CYS C 149 CYS C 262 1555 1555 2.05
SSBOND 4 CYS C 305 CYS C 336 1555 1555 2.03
SSBOND 5 CYS C 347 CYS C 377 1555 1555 2.05
SSBOND 6 CYS E 49 CYS E 197 1555 1555 2.05
SSBOND 7 CYS H 111 CYS H 145 1555 1555 2.04
SSBOND 8 CYS H 149 CYS H 262 1555 1555 2.05
SSBOND 9 CYS H 305 CYS H 336 1555 1555 2.04
SSBOND 10 CYS H 347 CYS H 377 1555 1555 2.03
SSBOND 11 CYS J 49 CYS J 197 1555 1555 2.04
SSBOND 12 CYS M 92 CYS R 92 1555 1555 2.07
SSBOND 13 CYS M 111 CYS M 145 1555 1555 2.04
SSBOND 14 CYS M 149 CYS M 262 1555 1555 2.06
SSBOND 15 CYS M 305 CYS M 336 1555 1555 2.05
SSBOND 16 CYS M 347 CYS M 377 1555 1555 2.03
SSBOND 17 CYS O 49 CYS O 197 1555 1555 2.04
SSBOND 18 CYS R 111 CYS R 145 1555 1555 2.04
SSBOND 19 CYS R 149 CYS R 262 1555 1555 2.04
SSBOND 20 CYS R 305 CYS R 336 1555 1555 2.03
SSBOND 21 CYS R 347 CYS R 377 1555 1555 2.04
SSBOND 22 CYS T 49 CYS T 197 1555 1555 2.04
SSBOND 23 CYS W 92 CYS 2 92 1555 1555 2.04
SSBOND 24 CYS W 111 CYS W 145 1555 1555 2.03
SSBOND 25 CYS W 149 CYS W 262 1555 1555 2.04
SSBOND 26 CYS W 305 CYS W 336 1555 1555 2.02
SSBOND 27 CYS W 347 CYS W 377 1555 1555 2.02
SSBOND 28 CYS Y 49 CYS Y 197 1555 1555 2.03
SSBOND 29 CYS 2 111 CYS 2 145 1555 1555 2.03
SSBOND 30 CYS 2 149 CYS 2 262 1555 1555 2.04
SSBOND 31 CYS 2 305 CYS 2 336 1555 1555 2.02
SSBOND 32 CYS 2 347 CYS 2 377 1555 1555 2.04
SSBOND 33 CYS 4 49 CYS 4 197 1555 1555 2.03
LINK ND2 ASN C 180 C1 NAG C1001 1555 1555 1.45
LINK ND2 ASN C 203 C1 NAG a 1 1555 1555 1.46
LINK ND2 ASN C 207 C1 NAG C1004 1555 1555 1.44
LINK ND2 ASN C 237 C1 NAG b 1 1555 1555 1.43
LINK ND2 ASN E 137 C1 NAG E1001 1555 1555 1.44
LINK ND2 ASN E 241 C1 NAG E1002 1555 1555 1.45
LINK ND2 ASN H 180 C1 NAG H1001 1555 1555 1.45
LINK ND2 ASN H 203 C1 NAG H1002 1555 1555 1.44
LINK ND2 ASN H 237 C1 NAG c 1 1555 1555 1.45
LINK ND2 ASN J 137 C1 NAG J1001 1555 1555 1.45
LINK ND2 ASN J 241 C1 NAG J1002 1555 1555 1.43
LINK ND2 ASN M 180 C1 NAG M1001 1555 1555 1.44
LINK ND2 ASN M 203 C1 NAG d 1 1555 1555 1.44
LINK ND2 ASN M 207 C1 NAG M1004 1555 1555 1.45
LINK ND2 ASN M 237 C1 NAG e 1 1555 1555 1.44
LINK ND2 ASN O 137 C1 NAG O1001 1555 1555 1.44
LINK ND2 ASN O 241 C1 NAG O1002 1555 1555 1.44
LINK ND2 ASN R 180 C1 NAG R1001 1555 1555 1.45
LINK ND2 ASN R 203 C1 NAG f 1 1555 1555 1.45
LINK ND2 ASN R 207 C1 NAG R1004 1555 1555 1.43
LINK ND2 ASN R 237 C1 NAG g 1 1555 1555 1.43
LINK ND2 ASN T 137 C1 NAG T1001 1555 1555 1.44
LINK ND2 ASN T 241 C1 NAG T1002 1555 1555 1.43
LINK ND2 ASN W 180 C1 NAG W1001 1555 1555 1.46
LINK ND2 ASN W 203 C1 NAG W1002 1555 1555 1.45
LINK ND2 ASN W 237 C1 NAG h 1 1555 1555 1.43
LINK ND2 ASN Y 137 C1 NAG Y1001 1555 1555 1.44
LINK ND2 ASN Y 241 C1 NAG Y1002 1555 1555 1.44
LINK ND2 ASN 2 180 C1 NAG 21001 1555 1555 1.45
LINK ND2 ASN 2 203 C1 NAG i 1 1555 1555 1.46
LINK ND2 ASN 2 237 C1 NAG j 1 1555 1555 1.43
LINK ND2 ASN 4 137 C1 NAG 41001 1555 1555 1.44
LINK ND2 ASN 4 241 C1 NAG 41002 1555 1555 1.44
LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.46
LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44
LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44
LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.47
LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.42
LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.47
LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.47
LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44
LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.46
LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.44
LINK NE2 HIS A 87 FE HEM A 201 1555 1555 2.38
LINK FE HEM A 201 O1 OXY A 202 1555 1555 2.39
LINK FE HEM A 201 O2 OXY A 202 1555 1555 2.67
LINK NE2 HIS B 92 FE HEM B 201 1555 1555 2.44
LINK FE HEM B 201 O2 OXY B 202 1555 1555 2.69
LINK NE2 HIS F 87 FE HEM F 201 1555 1555 2.43
LINK FE HEM F 201 O1 OXY F 202 1555 1555 2.49
LINK FE HEM F 201 O2 OXY F 202 1555 1555 2.66
LINK NE2 HIS G 92 FE HEM G 201 1555 1555 2.42
LINK FE HEM G 201 O1 OXY G 202 1555 1555 2.57
LINK NE2 HIS K 87 FE HEM K 201 1555 1555 2.37
LINK FE HEM K 201 O1 OXY K 202 1555 1555 2.34
LINK NE2 HIS L 92 FE HEM L 201 1555 1555 2.53
LINK FE HEM L 201 O1 OXY L 202 1555 1555 2.59
LINK NE2 HIS P 87 FE HEM P 201 1555 1555 2.37
LINK FE HEM P 201 O1 OXY P 202 1555 1555 2.43
LINK FE HEM P 201 O2 OXY P 202 1555 1555 2.41
LINK NE2 HIS Q 92 FE HEM Q 201 1555 1555 2.40
LINK FE HEM Q 201 O2 OXY Q 202 1555 1555 2.67
LINK NE2 HIS U 87 FE HEM U 201 1555 1555 2.47
LINK FE HEM U 201 O2 OXY U 202 1555 1555 2.64
LINK NE2 HIS V 92 FE HEM V 201 1555 1555 2.58
LINK FE HEM V 201 O2 OXY V 202 1555 1555 2.66
LINK NE2 HIS Z 87 FE HEM Z 201 1555 1555 2.42
LINK FE HEM Z 201 O1 OXY Z 202 1555 1555 2.70
LINK FE HEM Z 201 O2 OXY Z 202 1555 1555 2.50
LINK NE2 HIS 1 92 FE HEM 1 201 1555 1555 2.53
LINK FE HEM 1 201 O1 OXY 1 202 1555 1555 2.55
LINK FE HEM 1 201 O2 OXY 1 202 1555 1555 2.50
CISPEP 1 ASP D 133 PRO D 134 0 11.24
CISPEP 2 ASP I 133 PRO I 134 0 12.35
CISPEP 3 ASP N 133 PRO N 134 0 9.64
CISPEP 4 ASP S 133 PRO S 134 0 10.96
CISPEP 5 ASP X 133 PRO X 134 0 11.14
CISPEP 6 ASP 3 133 PRO 3 134 0 10.55
CRYST1 143.230 140.950 267.180 90.00 98.54 90.00 P 1 21 1 12
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 0.006982 0.000000 0.001049 0.00000
SCALE2 0.000000 0.007095 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003785 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
