HEADER DNA BINDING PROTEIN 25-FEB-18 5ZE0
TITLE HAIRPIN FORMING COMPLEX, RAG1/2-NICKED(WITH DIDEOXY) 12RSS/23RSS
TITLE 2 COMPLEX IN MG2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOUSE RAG1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 383-1008;
COMPND 5 SYNONYM: RAG-1;
COMPND 6 EC: 3.1.-.-,2.3.2.27;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: AFTER PRESICSSION CLEAVAGE, GP SEQUENCE REMAINS.;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MOUSE RAG2;
COMPND 11 CHAIN: B, D;
COMPND 12 FRAGMENT: UNP RESIDUES 1-387;
COMPND 13 SYNONYM: RAG-2;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES;
COMPND 16 OTHER_DETAILS: GP REMAINS AFTER PRESCISSION CLEAVAGE;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: HMGB1 A-B BOX;
COMPND 19 CHAIN: N;
COMPND 20 FRAGMENT: UNP RESIDUES 1-163;
COMPND 21 SYNONYM: HIGH MOBILITY GROUP PROTEIN 1,HMG-1;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 4;
COMPND 24 MOLECULE: DNA (45-MER);
COMPND 25 CHAIN: F;
COMPND 26 ENGINEERED: YES;
COMPND 27 MOL_ID: 5;
COMPND 28 MOLECULE: DNA (5'-D(*AP*AP*TP*CP*TP*GP*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-
COMPND 29 3');
COMPND 30 CHAIN: I;
COMPND 31 ENGINEERED: YES;
COMPND 32 MOL_ID: 6;
COMPND 33 MOLECULE: DNA (5'-D(*TP*AP*TP*CP*TP*GP*GP*CP*CP*TP*GP*TP*CP*TP*TP*A)-
COMPND 34 3');
COMPND 35 CHAIN: J;
COMPND 36 ENGINEERED: YES;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: DNA (54-MER);
COMPND 39 CHAIN: G;
COMPND 40 ENGINEERED: YES;
COMPND 41 MOL_ID: 8;
COMPND 42 MOLECULE: DNA (30-MER);
COMPND 43 CHAIN: L;
COMPND 44 ENGINEERED: YES;
COMPND 45 MOL_ID: 9;
COMPND 46 MOLECULE: DNA (39-MER);
COMPND 47 CHAIN: M;
COMPND 48 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RAG1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: RAG2, RAG-2;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HET293T;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 19 ORGANISM_COMMON: MOUSE;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 GENE: HMGB1, HMG-1, HMG1;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 MOL_ID: 4;
SOURCE 25 SYNTHETIC: YES;
SOURCE 26 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 27 ORGANISM_TAXID: 32630;
SOURCE 28 MOL_ID: 5;
SOURCE 29 SYNTHETIC: YES;
SOURCE 30 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 31 ORGANISM_TAXID: 32630;
SOURCE 32 MOL_ID: 6;
SOURCE 33 SYNTHETIC: YES;
SOURCE 34 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 35 ORGANISM_TAXID: 32630;
SOURCE 36 MOL_ID: 7;
SOURCE 37 SYNTHETIC: YES;
SOURCE 38 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 39 ORGANISM_TAXID: 32630;
SOURCE 40 MOL_ID: 8;
SOURCE 41 SYNTHETIC: YES;
SOURCE 42 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 43 ORGANISM_TAXID: 32630;
SOURCE 44 MOL_ID: 9;
SOURCE 45 SYNTHETIC: YES;
SOURCE 46 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 47 ORGANISM_TAXID: 32630
KEYWDS V(D)J RECOMBINATION, RAG1-2-12RSS-23RSS COMPLEX, HAIRPIN FORMING
KEYWDS 2 COMPLEX, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.KIM,W.CHUENCHOR,X.CHEN,M.GELLERT,W.YANG
REVDAT 3 27-MAR-24 5ZE0 1 LINK
REVDAT 2 02-MAY-18 5ZE0 1 JRNL
REVDAT 1 25-APR-18 5ZE0 0
JRNL AUTH M.S.KIM,W.CHUENCHOR,X.CHEN,Y.CUI,X.ZHANG,Z.H.ZHOU,M.GELLERT,
JRNL AUTH 2 W.YANG
JRNL TITL CRACKING THE DNA CODE FOR V(D)J RECOMBINATION
JRNL REF MOL. CELL V. 70 358 2018
JRNL REFN ISSN 1097-4164
JRNL PMID 29628308
JRNL DOI 10.1016/J.MOLCEL.2018.03.008
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 202142
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 10084
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 34.8000 - 8.5045 0.94 6207 330 0.1692 0.1873
REMARK 3 2 8.5045 - 6.7665 0.96 6331 341 0.1646 0.2110
REMARK 3 3 6.7665 - 5.9159 0.97 6350 338 0.1756 0.2219
REMARK 3 4 5.9159 - 5.3772 0.97 6363 345 0.1620 0.1981
REMARK 3 5 5.3772 - 4.9930 0.97 6410 326 0.1573 0.2088
REMARK 3 6 4.9930 - 4.6993 0.97 6365 344 0.1572 0.1861
REMARK 3 7 4.6993 - 4.4645 0.98 6418 341 0.1568 0.1748
REMARK 3 8 4.4645 - 4.2705 0.97 6338 329 0.1581 0.1673
REMARK 3 9 4.2705 - 4.1064 0.98 6497 336 0.1653 0.1786
REMARK 3 10 4.1064 - 3.9649 0.98 6405 331 0.1766 0.2067
REMARK 3 11 3.9649 - 3.8411 0.96 6334 331 0.1980 0.2383
REMARK 3 12 3.8411 - 3.7314 0.98 6371 339 0.2101 0.2630
REMARK 3 13 3.7314 - 3.6333 0.97 6387 328 0.2041 0.2400
REMARK 3 14 3.6333 - 3.5447 0.98 6522 324 0.2143 0.2581
REMARK 3 15 3.5447 - 3.4642 0.98 6447 325 0.2092 0.2433
REMARK 3 16 3.4642 - 3.3905 0.97 6339 329 0.2190 0.2802
REMARK 3 17 3.3905 - 3.3228 0.98 6444 337 0.2177 0.2653
REMARK 3 18 3.3228 - 3.2601 0.98 6474 341 0.2298 0.2591
REMARK 3 19 3.2601 - 3.2019 0.98 6372 339 0.2409 0.2867
REMARK 3 20 3.2019 - 3.1477 0.98 6499 334 0.2548 0.3285
REMARK 3 21 3.1477 - 3.0970 0.98 6457 329 0.2612 0.3039
REMARK 3 22 3.0970 - 3.0493 0.98 6408 347 0.2784 0.3133
REMARK 3 23 3.0493 - 3.0045 0.98 6459 336 0.2883 0.3519
REMARK 3 24 3.0045 - 2.9622 0.98 6422 347 0.2838 0.3243
REMARK 3 25 2.9622 - 2.9222 0.98 6465 333 0.2970 0.3247
REMARK 3 26 2.9222 - 2.8843 0.97 6409 344 0.3030 0.3457
REMARK 3 27 2.8843 - 2.8482 0.98 6437 335 0.3081 0.3317
REMARK 3 28 2.8482 - 2.8139 0.97 6313 354 0.3238 0.3838
REMARK 3 29 2.8139 - 2.7812 0.97 6390 338 0.3408 0.3425
REMARK 3 30 2.7812 - 2.7500 0.97 6425 333 0.3611 0.3880
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.440
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 : 0.012 21076
REMARK 3 ANGLE : 1.212 29311
REMARK 3 CHIRALITY : 0.171 3209
REMARK 3 PLANARITY : 0.007 3081
REMARK 3 DIHEDRAL : 21.147 11946
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 5ZE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 208782
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES (PH 6.8), 15% PEG 3350, 200
REMARK 280 MM POTASSIUM FORMATE., VAPOR DIFFUSION, HANGING 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 54.51500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, N, J, G, M
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, I, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 382
REMARK 465 PRO A 383
REMARK 465 VAL A 384
REMARK 465 HIS A 385
REMARK 465 ILE A 386
REMARK 465 ASN A 387
REMARK 465 LYS A 388
REMARK 465 GLY A 389
REMARK 465 GLY A 390
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 GLY B 82
REMARK 465 SER B 83
REMARK 465 ILE B 84
REMARK 465 ASP B 85
REMARK 465 SER B 86
REMARK 465 ASP B 87
REMARK 465 LYS B 336
REMARK 465 GLN B 337
REMARK 465 ALA B 338
REMARK 465 MET B 339
REMARK 465 SER B 351
REMARK 465 GLU B 352
REMARK 465 GLU B 353
REMARK 465 ASP B 354
REMARK 465 LEU B 355
REMARK 465 SER B 356
REMARK 465 GLU B 357
REMARK 465 ASP B 358
REMARK 465 GLN B 359
REMARK 465 LYS B 360
REMARK 465 ILE B 361
REMARK 465 VAL B 362
REMARK 465 SER B 363
REMARK 465 ASN B 364
REMARK 465 SER B 365
REMARK 465 GLN B 366
REMARK 465 THR B 367
REMARK 465 SER B 368
REMARK 465 THR B 369
REMARK 465 GLU B 370
REMARK 465 ASP B 371
REMARK 465 PRO B 372
REMARK 465 GLY B 373
REMARK 465 ASP B 374
REMARK 465 SER B 375
REMARK 465 THR B 376
REMARK 465 PRO B 377
REMARK 465 PHE B 378
REMARK 465 GLU B 379
REMARK 465 ASP B 380
REMARK 465 SER B 381
REMARK 465 GLU B 382
REMARK 465 GLU B 383
REMARK 465 PHE B 384
REMARK 465 CYS B 385
REMARK 465 PHE B 386
REMARK 465 SER B 387
REMARK 465 GLY C 382
REMARK 465 PRO C 383
REMARK 465 VAL C 384
REMARK 465 ALA C 1008
REMARK 465 GLY D -1
REMARK 465 PRO D 0
REMARK 465 GLY D 82
REMARK 465 SER D 83
REMARK 465 ILE D 84
REMARK 465 ASP D 85
REMARK 465 SER D 86
REMARK 465 ASP D 87
REMARK 465 LYS D 336
REMARK 465 GLN D 337
REMARK 465 ALA D 338
REMARK 465 MET D 339
REMARK 465 SER D 340
REMARK 465 GLU D 352
REMARK 465 GLU D 353
REMARK 465 ASP D 354
REMARK 465 LEU D 355
REMARK 465 SER D 356
REMARK 465 GLU D 357
REMARK 465 ASP D 358
REMARK 465 GLN D 359
REMARK 465 LYS D 360
REMARK 465 ILE D 361
REMARK 465 VAL D 362
REMARK 465 SER D 363
REMARK 465 ASN D 364
REMARK 465 SER D 365
REMARK 465 GLN D 366
REMARK 465 THR D 367
REMARK 465 SER D 368
REMARK 465 THR D 369
REMARK 465 GLU D 370
REMARK 465 ASP D 371
REMARK 465 PRO D 372
REMARK 465 GLY D 373
REMARK 465 ASP D 374
REMARK 465 SER D 375
REMARK 465 THR D 376
REMARK 465 PRO D 377
REMARK 465 PHE D 378
REMARK 465 GLU D 379
REMARK 465 ASP D 380
REMARK 465 SER D 381
REMARK 465 GLU D 382
REMARK 465 GLU D 383
REMARK 465 PHE D 384
REMARK 465 CYS D 385
REMARK 465 PHE D 386
REMARK 465 SER D 387
REMARK 465 MET N 1
REMARK 465 GLY N 2
REMARK 465 LYS N 3
REMARK 465 GLY N 4
REMARK 465 ASP N 5
REMARK 465 PRO N 6
REMARK 465 LYS N 7
REMARK 465 LYS N 8
REMARK 465 PRO N 9
REMARK 465 THR N 51
REMARK 465 MET N 52
REMARK 465 SER N 53
REMARK 465 THR N 77
REMARK 465 TYR N 78
REMARK 465 ILE N 79
REMARK 465 PRO N 80
REMARK 465 PRO N 81
REMARK 465 LYS N 82
REMARK 465 GLY N 83
REMARK 465 GLU N 84
REMARK 465 THR N 85
REMARK 465 LYS N 86
REMARK 465 LYS N 87
REMARK 465 LYS N 88
REMARK 465 PHE N 89
REMARK 465 LYS N 90
REMARK 465 ASP N 91
REMARK 465 PRO N 92
REMARK 465 ASN N 93
REMARK 465 ALA N 94
REMARK 465 PRO N 95
REMARK 465 LYS N 96
REMARK 465 HIS N 117
REMARK 465 PRO N 118
REMARK 465 GLY N 119
REMARK 465 LEU N 120
REMARK 465 SER N 121
REMARK 465 ALA N 137
REMARK 465 ALA N 138
REMARK 465 ASP N 158
REMARK 465 ILE N 159
REMARK 465 ALA N 160
REMARK 465 ALA N 161
REMARK 465 TYR N 162
REMARK 465 ARG N 163
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 393 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 458 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 81 CG CD CE NZ
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 ASN B 117 CG OD1 ND2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 ASN C1007 CG OD1 ND2
REMARK 470 LYS D 81 CG CD CE NZ
REMARK 470 LYS D 88 CG CD CE NZ
REMARK 470 ASN D 117 CG OD1 ND2
REMARK 470 LYS D 118 CG CD CE NZ
REMARK 470 SER D 351 OG
REMARK 470 ARG N 10 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS N 12 CG CD CE NZ
REMARK 470 ARG N 24 CG CD NE CZ NH1 NH2
REMARK 470 HIS N 31 CG ND1 CD2 CE1 NE2
REMARK 470 ASP N 33 CG OD1 OD2
REMARK 470 GLU N 40 CG CD OE1 OE2
REMARK 470 LYS N 50 CG CD CE NZ
REMARK 470 LYS N 55 CG CD CE NZ
REMARK 470 LYS N 57 CG CD CE NZ
REMARK 470 LYS N 68 CG CD CE NZ
REMARK 470 ARG N 70 CG CD NE CZ NH1 NH2
REMARK 470 TYR N 71 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU N 72 CG CD OE1 OE2
REMARK 470 GLU N 74 CG CD OE1 OE2
REMARK 470 LYS N 76 CG CD CE NZ
REMARK 470 ARG N 97 CG CD NE CZ NH1 NH2
REMARK 470 SER N 100 OG
REMARK 470 ARG N 110 CG CD NE CZ NH1 NH2
REMARK 470 PRO N 111 CG CD
REMARK 470 LYS N 114 CG CD CE NZ
REMARK 470 GLU N 116 CG CD OE1 OE2
REMARK 470 ILE N 122 CG1 CG2 CD1
REMARK 470 ASP N 124 CG OD1 OD2
REMARK 470 LYS N 128 CG CD CE NZ
REMARK 470 GLU N 131 CG CD OE1 OE2
REMARK 470 TRP N 133 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP N 133 CZ3 CH2
REMARK 470 ASN N 134 CG OD1 ND2
REMARK 470 ASP N 139 CG OD1 OD2
REMARK 470 LYS N 146 CG CD CE NZ
REMARK 470 LYS N 147 CG CD CE NZ
REMARK 470 LYS N 152 CG CD CE NZ
REMARK 470 GLU N 153 CG CD OE1 OE2
REMARK 470 LYS N 154 CG CD CE NZ
REMARK 470 GLU N 156 CG CD OE1 OE2
REMARK 470 LYS N 157 CG CD CE NZ
REMARK 470 DA I 16 O3'
REMARK 470 DA J 16 O3'
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT F 19 O3' DT F 19 C3' -0.049
REMARK 500 DG F 20 O3' DG F 20 C3' -0.043
REMARK 500 DC F 26 O3' DC F 26 C3' -0.036
REMARK 500 DT F 27 O3' DT F 27 C3' -0.079
REMARK 500 DG F 28 O3' DG F 28 C3' -0.060
REMARK 500 DC F 36 O5' DC F 36 C5' -0.178
REMARK 500 DC F 36 C5' DC F 36 C4' -0.067
REMARK 500 DC F 36 O3' DC F 36 C3' -0.074
REMARK 500 DC I 13 O3' DC I 13 C3' -0.054
REMARK 500 DT I 15 O3' DT I 15 C3' -0.041
REMARK 500 DC J 13 O3' DC J 13 C3' -0.052
REMARK 500 DT J 14 O3' DT J 14 C3' -0.037
REMARK 500 DT J 15 O3' DT J 15 C3' -0.041
REMARK 500 DT G 8 O3' DT G 8 C3' -0.040
REMARK 500 DG G 39 O3' DG G 39 C3' -0.037
REMARK 500 DC G 47 O3' DC G 47 C3' -0.042
REMARK 500 DC L 17 P DC L 17 OP3 -0.135
REMARK 500 DC L 17 O3' DC L 17 C3' -0.053
REMARK 500 DC L 19 O3' DC L 19 C3' -0.070
REMARK 500 DA L 20 O3' DA L 20 C3' -0.040
REMARK 500 DC M 17 P DC M 17 OP3 -0.122
REMARK 500 DC M 17 O3' DC M 17 C3' -0.046
REMARK 500 DG M 21 O3' DG M 21 C3' -0.079
REMARK 500 DT M 25 O3' DT M 25 C3' -0.041
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 PRO D 253 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 DG F 2 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT F 9 C1' - O4' - C4' ANGL. DEV. = -6.2 DEGREES
REMARK 500 DG F 10 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC F 26 O3' - P - OP2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 DC F 26 O3' - P - OP1 ANGL. DEV. = -13.2 DEGREES
REMARK 500 DC F 26 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DG F 28 O3' - P - OP2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 DG F 28 O5' - P - OP2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 DT F 29 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DG F 30 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DA F 33 O5' - P - OP1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DC F 36 OP1 - P - OP2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 DC F 36 O5' - P - OP1 ANGL. DEV. = -12.0 DEGREES
REMARK 500 DC F 36 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DT J 3 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT J 14 O5' - P - OP2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DT J 14 O4' - C4' - C3' ANGL. DEV. = -2.9 DEGREES
REMARK 500 DC G 19 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC G 37 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DT G 40 O5' - P - OP1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 DT G 40 O4' - C4' - C3' ANGL. DEV. = -2.7 DEGREES
REMARK 500 DG G 41 O5' - P - OP1 ANGL. DEV. = -7.7 DEGREES
REMARK 500 DC G 52 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC L 17 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC L 19 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC L 27 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC L 32 O4' - C4' - C3' ANGL. DEV. = -3.2 DEGREES
REMARK 500 DA L 36 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DC L 43 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC L 45 O5' - P - OP2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 DC M 17 O5' - P - OP1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 DC M 19 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG M 21 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA M 33 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA M 45 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA M 49 O4' - C1' - N9 ANGL. DEV. = 2.4 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 GLU A 444 60.92 -118.66
REMARK 500 PRO A 512 150.57 -42.74
REMARK 500 HIS A 609 -178.00 -63.72
REMARK 500 GLU A 617 42.60 -89.28
REMARK 500 LYS A 645 71.32 -115.92
REMARK 500 SER A 684 46.48 -101.92
REMARK 500 LEU A 741 -59.12 76.45
REMARK 500 PRO A 789 96.07 -68.46
REMARK 500 THR A 922 -71.54 -83.87
REMARK 500 ASN A 975 25.36 -140.80
REMARK 500 ASN B 11 45.47 -97.62
REMARK 500 CYS B 41 89.90 -151.07
REMARK 500 TYR B 68 78.93 -117.90
REMARK 500 LYS B 115 35.40 -141.82
REMARK 500 LYS B 118 18.19 53.73
REMARK 500 MET B 162 159.03 -47.25
REMARK 500 PRO B 180 29.90 -69.85
REMARK 500 ASN B 213 -121.06 58.41
REMARK 500 LEU B 240 74.46 -118.71
REMARK 500 SER C 477 154.51 -48.47
REMARK 500 PRO C 590 109.80 -46.63
REMARK 500 ASP C 604 46.06 70.87
REMARK 500 GLU C 617 50.64 -92.44
REMARK 500 LEU C 741 -51.08 80.44
REMARK 500 PHE C 743 57.63 -111.56
REMARK 500 GLU C 814 72.28 45.47
REMARK 500 CYS C 902 59.07 -142.73
REMARK 500 THR C 922 -78.78 -92.99
REMARK 500 ASN C 975 37.15 -145.08
REMARK 500 GLN C 978 59.86 -92.58
REMARK 500 ARG D 148 44.24 33.59
REMARK 500 PRO D 180 35.45 -74.09
REMARK 500 ASN D 213 -128.77 50.19
REMARK 500 ASN D 267 -129.48 53.18
REMARK 500 ASN D 324 45.65 -89.87
REMARK 500 PRO D 332 162.23 -49.31
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 K A2005 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 649 OE1
REMARK 620 2 SER A 963 OG 85.4
REMARK 620 3 HOH A2138 O 80.5 60.3
REMARK 620 4 DC L 19 O4' 105.8 124.3 172.0
REMARK 620 5 DC L 19 O2 136.5 135.3 104.5 67.6
REMARK 620 6 HOH L4104 O 82.6 134.4 74.3 101.3 58.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 727 SG
REMARK 620 2 CYS A 730 SG 104.1
REMARK 620 3 HIS A 937 NE2 111.4 103.0
REMARK 620 4 HIS A 942 NE2 105.6 116.8 115.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 600 OD1
REMARK 620 2 GLY C 601 O 65.4
REMARK 620 3 GLU C 962 OE1 75.4 132.2
REMARK 620 4 DG G 41 O3' 157.6 131.3 82.5
REMARK 620 5 DT G 42 OP2 123.6 89.4 90.4 52.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C2003 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 649 OE1
REMARK 620 2 SER C 963 OG 81.3
REMARK 620 3 HOH C2104 O 81.7 52.6
REMARK 620 4 HOH G 107 O 89.8 61.8 114.4
REMARK 620 5 DC M 19 O4' 104.5 122.9 71.8 165.3
REMARK 620 6 DC M 19 O2 137.2 140.3 127.4 101.6 65.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C2002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 727 SG
REMARK 620 2 CYS C 730 SG 109.9
REMARK 620 3 HIS C 937 NE2 108.2 98.8
REMARK 620 4 HIS C 942 NE2 111.7 116.8 110.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K C 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 2004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WWX RELATED DB: PDB
REMARK 900 RELATED ID: 5ZDZ RELATED DB: PDB
REMARK 900 RELATED ID: 5ZE1 RELATED DB: PDB
REMARK 900 RELATED ID: 5EZ2 RELATED DB: PDB
REMARK 900 RELATED ID: 6CIM RELATED DB: PDB
REMARK 900 RELATED ID: 6CIL RELATED DB: PDB
REMARK 900 RELATED ID: 6CIK RELATED DB: PDB
REMARK 900 RELATED ID: 6CG0 RELATED DB: PDB
REMARK 900 RELATED ID: 6CIJ RELATED DB: PDB
DBREF 5ZE0 A 384 1008 UNP P15919 RAG1_MOUSE 384 1008
DBREF 5ZE0 B 1 387 UNP P21784 RAG2_MOUSE 1 387
DBREF 5ZE0 C 384 1008 UNP P15919 RAG1_MOUSE 384 1008
DBREF 5ZE0 D 1 387 UNP P21784 RAG2_MOUSE 1 387
DBREF 5ZE0 N 1 163 UNP P63158 HMGB1_MOUSE 1 163
DBREF 5ZE0 F 1 45 PDB 5ZE0 5ZE0 1 45
DBREF 5ZE0 I 1 16 PDB 5ZE0 5ZE0 1 16
DBREF 5ZE0 J 1 16 PDB 5ZE0 5ZE0 1 16
DBREF 5ZE0 G 3 56 PDB 5ZE0 5ZE0 3 56
DBREF 5ZE0 L 17 46 PDB 5ZE0 5ZE0 17 46
DBREF 5ZE0 M 17 55 PDB 5ZE0 5ZE0 17 55
SEQADV 5ZE0 GLY A 382 UNP P15919 CLONING ARTIFACT
SEQADV 5ZE0 PRO A 383 UNP P15919 CLONING ARTIFACT
SEQADV 5ZE0 GLY B -1 UNP P21784 CLONING ARTIFACT
SEQADV 5ZE0 PRO B 0 UNP P21784 CLONING ARTIFACT
SEQADV 5ZE0 VAL B 1 UNP P21784 MET 1 ENGINEERED MUTATION
SEQADV 5ZE0 GLY C 382 UNP P15919 CLONING ARTIFACT
SEQADV 5ZE0 PRO C 383 UNP P15919 CLONING ARTIFACT
SEQADV 5ZE0 GLY D -1 UNP P21784 CLONING ARTIFACT
SEQADV 5ZE0 PRO D 0 UNP P21784 CLONING ARTIFACT
SEQADV 5ZE0 VAL D 1 UNP P21784 MET 1 ENGINEERED MUTATION
SEQRES 1 A 627 GLY PRO VAL HIS ILE ASN LYS GLY GLY ARG PRO ARG GLN
SEQRES 2 A 627 HIS LEU LEU SER LEU THR ARG ARG ALA GLN LYS HIS ARG
SEQRES 3 A 627 LEU ARG GLU LEU LYS ILE GLN VAL LYS GLU PHE ALA ASP
SEQRES 4 A 627 LYS GLU GLU GLY GLY ASP VAL LYS ALA VAL CYS LEU THR
SEQRES 5 A 627 LEU PHE LEU LEU ALA LEU ARG ALA ARG ASN GLU HIS ARG
SEQRES 6 A 627 GLN ALA ASP GLU LEU GLU ALA ILE MET GLN GLY ARG GLY
SEQRES 7 A 627 SER GLY LEU GLN PRO ALA VAL CYS LEU ALA ILE ARG VAL
SEQRES 8 A 627 ASN THR PHE LEU SER CYS SER GLN TYR HIS LYS MET TYR
SEQRES 9 A 627 ARG THR VAL LYS ALA ILE THR GLY ARG GLN ILE PHE GLN
SEQRES 10 A 627 PRO LEU HIS ALA LEU ARG ASN ALA GLU LYS VAL LEU LEU
SEQRES 11 A 627 PRO GLY TYR HIS PRO PHE GLU TRP GLN PRO PRO LEU LYS
SEQRES 12 A 627 ASN VAL SER SER ARG THR ASP VAL GLY ILE ILE ASP GLY
SEQRES 13 A 627 LEU SER GLY LEU ALA SER SER VAL ASP GLU TYR PRO VAL
SEQRES 14 A 627 ASP THR ILE ALA LYS ARG PHE ARG TYR ASP SER ALA LEU
SEQRES 15 A 627 VAL SER ALA LEU MET ASP MET GLU GLU ASP ILE LEU GLU
SEQRES 16 A 627 GLY MET ARG SER GLN ASP LEU ASP ASP TYR LEU ASN GLY
SEQRES 17 A 627 PRO PHE THR VAL VAL VAL LYS GLU SER CYS ASP GLY MET
SEQRES 18 A 627 GLY ASP VAL SER GLU LYS HIS GLY SER GLY PRO ALA VAL
SEQRES 19 A 627 PRO GLU LYS ALA VAL ARG PHE SER PHE THR VAL MET ARG
SEQRES 20 A 627 ILE THR ILE GLU HIS GLY SER GLN ASN VAL LYS VAL PHE
SEQRES 21 A 627 GLU GLU PRO LYS PRO ASN SER GLU LEU CYS CYS LYS PRO
SEQRES 22 A 627 LEU CYS LEU MET LEU ALA ASP GLU SER ASP HIS GLU THR
SEQRES 23 A 627 LEU THR ALA ILE LEU SER PRO LEU ILE ALA GLU ARG GLU
SEQRES 24 A 627 ALA MET LYS SER SER GLU LEU THR LEU GLU MET GLY GLY
SEQRES 25 A 627 ILE PRO ARG THR PHE LYS PHE ILE PHE ARG GLY THR GLY
SEQRES 26 A 627 TYR ASP GLU LYS LEU VAL ARG GLU VAL GLU GLY LEU GLU
SEQRES 27 A 627 ALA SER GLY SER VAL TYR ILE CYS THR LEU CYS ASP THR
SEQRES 28 A 627 THR ARG LEU GLU ALA SER GLN ASN LEU VAL PHE HIS SER
SEQRES 29 A 627 ILE THR ARG SER HIS ALA GLU ASN LEU GLN ARG TYR GLU
SEQRES 30 A 627 VAL TRP ARG SER ASN PRO TYR HIS GLU SER VAL GLU GLU
SEQRES 31 A 627 LEU ARG ASP ARG VAL LYS GLY VAL SER ALA LYS PRO PHE
SEQRES 32 A 627 ILE GLU THR VAL PRO SER ILE ASP ALA LEU HIS CYS ASP
SEQRES 33 A 627 ILE GLY ASN ALA ALA GLU PHE TYR LYS ILE PHE GLN LEU
SEQRES 34 A 627 GLU ILE GLY GLU VAL TYR LYS HIS PRO ASN ALA SER LYS
SEQRES 35 A 627 GLU GLU ARG LYS ARG TRP GLN ALA THR LEU ASP LYS HIS
SEQRES 36 A 627 LEU ARG LYS ARG MET ASN LEU LYS PRO ILE MET ARG MET
SEQRES 37 A 627 ASN GLY ASN PHE ALA ARG LYS LEU MET THR GLN GLU THR
SEQRES 38 A 627 VAL ASP ALA VAL CYS GLU LEU ILE PRO SER GLU GLU ARG
SEQRES 39 A 627 HIS GLU ALA LEU ARG GLU LEU MET ASP LEU TYR LEU LYS
SEQRES 40 A 627 MET LYS PRO VAL TRP ARG SER SER CYS PRO ALA LYS GLU
SEQRES 41 A 627 CYS PRO GLU SER LEU CYS GLN TYR SER PHE ASN SER GLN
SEQRES 42 A 627 ARG PHE ALA GLU LEU LEU SER THR LYS PHE LYS TYR ARG
SEQRES 43 A 627 TYR GLU GLY LYS ILE THR ASN TYR PHE HIS LYS THR LEU
SEQRES 44 A 627 ALA HIS VAL PRO GLU ILE ILE GLU ARG ASP GLY SER ILE
SEQRES 45 A 627 GLY ALA TRP ALA SER GLU GLY ASN GLU SER GLY ASN LYS
SEQRES 46 A 627 LEU PHE ARG ARG PHE ARG LYS MET ASN ALA ARG GLN SER
SEQRES 47 A 627 LYS CYS TYR GLU MET GLU ASP VAL LEU LYS HIS HIS TRP
SEQRES 48 A 627 LEU TYR THR SER LYS TYR LEU GLN LYS PHE MET ASN ALA
SEQRES 49 A 627 HIS ASN ALA
SEQRES 1 B 389 GLY PRO VAL SER LEU GLN MET VAL THR VAL GLY HIS ASN
SEQRES 2 B 389 ILE ALA LEU ILE GLN PRO GLY PHE SER LEU MET ASN PHE
SEQRES 3 B 389 ASP GLY GLN VAL PHE PHE PHE GLY GLN LYS GLY TRP PRO
SEQRES 4 B 389 LYS ARG SER CYS PRO THR GLY VAL PHE HIS PHE ASP ILE
SEQRES 5 B 389 LYS GLN ASN HIS LEU LYS LEU LYS PRO ALA ILE PHE SER
SEQRES 6 B 389 LYS ASP SER CYS TYR LEU PRO PRO LEU ARG TYR PRO ALA
SEQRES 7 B 389 THR CYS SER TYR LYS GLY SER ILE ASP SER ASP LYS HIS
SEQRES 8 B 389 GLN TYR ILE ILE HIS GLY GLY LYS THR PRO ASN ASN GLU
SEQRES 9 B 389 LEU SER ASP LYS ILE TYR ILE MET SER VAL ALA CYS LYS
SEQRES 10 B 389 ASN ASN LYS LYS VAL THR PHE ARG CYS THR GLU LYS ASP
SEQRES 11 B 389 LEU VAL GLY ASP VAL PRO GLU PRO ARG TYR GLY HIS SER
SEQRES 12 B 389 ILE ASP VAL VAL TYR SER ARG GLY LYS SER MET GLY VAL
SEQRES 13 B 389 LEU PHE GLY GLY ARG SER TYR MET PRO SER THR GLN ARG
SEQRES 14 B 389 THR THR GLU LYS TRP ASN SER VAL ALA ASP CYS LEU PRO
SEQRES 15 B 389 HIS VAL PHE LEU ILE ASP PHE GLU PHE GLY CYS ALA THR
SEQRES 16 B 389 SER TYR ILE LEU PRO GLU LEU GLN ASP GLY LEU SER PHE
SEQRES 17 B 389 HIS VAL SER ILE ALA ARG ASN ASP THR VAL TYR ILE LEU
SEQRES 18 B 389 GLY GLY HIS SER LEU ALA SER ASN ILE ARG PRO ALA ASN
SEQRES 19 B 389 LEU TYR ARG ILE ARG VAL ASP LEU PRO LEU GLY THR PRO
SEQRES 20 B 389 ALA VAL ASN CYS THR VAL LEU PRO GLY GLY ILE SER VAL
SEQRES 21 B 389 SER SER ALA ILE LEU THR GLN THR ASN ASN ASP GLU PHE
SEQRES 22 B 389 VAL ILE VAL GLY GLY TYR GLN LEU GLU ASN GLN LYS ARG
SEQRES 23 B 389 MET VAL CYS SER LEU VAL SER LEU GLY ASP ASN THR ILE
SEQRES 24 B 389 GLU ILE SER GLU MET GLU THR PRO ASP TRP THR SER ASP
SEQRES 25 B 389 ILE LYS HIS SER LYS ILE TRP PHE GLY SER ASN MET GLY
SEQRES 26 B 389 ASN GLY THR ILE PHE LEU GLY ILE PRO GLY ASP ASN LYS
SEQRES 27 B 389 GLN ALA MET SER GLU ALA PHE TYR PHE TYR THR LEU ARG
SEQRES 28 B 389 CYS SER GLU GLU ASP LEU SER GLU ASP GLN LYS ILE VAL
SEQRES 29 B 389 SER ASN SER GLN THR SER THR GLU ASP PRO GLY ASP SER
SEQRES 30 B 389 THR PRO PHE GLU ASP SER GLU GLU PHE CYS PHE SER
SEQRES 1 C 627 GLY PRO VAL HIS ILE ASN LYS GLY GLY ARG PRO ARG GLN
SEQRES 2 C 627 HIS LEU LEU SER LEU THR ARG ARG ALA GLN LYS HIS ARG
SEQRES 3 C 627 LEU ARG GLU LEU LYS ILE GLN VAL LYS GLU PHE ALA ASP
SEQRES 4 C 627 LYS GLU GLU GLY GLY ASP VAL LYS ALA VAL CYS LEU THR
SEQRES 5 C 627 LEU PHE LEU LEU ALA LEU ARG ALA ARG ASN GLU HIS ARG
SEQRES 6 C 627 GLN ALA ASP GLU LEU GLU ALA ILE MET GLN GLY ARG GLY
SEQRES 7 C 627 SER GLY LEU GLN PRO ALA VAL CYS LEU ALA ILE ARG VAL
SEQRES 8 C 627 ASN THR PHE LEU SER CYS SER GLN TYR HIS LYS MET TYR
SEQRES 9 C 627 ARG THR VAL LYS ALA ILE THR GLY ARG GLN ILE PHE GLN
SEQRES 10 C 627 PRO LEU HIS ALA LEU ARG ASN ALA GLU LYS VAL LEU LEU
SEQRES 11 C 627 PRO GLY TYR HIS PRO PHE GLU TRP GLN PRO PRO LEU LYS
SEQRES 12 C 627 ASN VAL SER SER ARG THR ASP VAL GLY ILE ILE ASP GLY
SEQRES 13 C 627 LEU SER GLY LEU ALA SER SER VAL ASP GLU TYR PRO VAL
SEQRES 14 C 627 ASP THR ILE ALA LYS ARG PHE ARG TYR ASP SER ALA LEU
SEQRES 15 C 627 VAL SER ALA LEU MET ASP MET GLU GLU ASP ILE LEU GLU
SEQRES 16 C 627 GLY MET ARG SER GLN ASP LEU ASP ASP TYR LEU ASN GLY
SEQRES 17 C 627 PRO PHE THR VAL VAL VAL LYS GLU SER CYS ASP GLY MET
SEQRES 18 C 627 GLY ASP VAL SER GLU LYS HIS GLY SER GLY PRO ALA VAL
SEQRES 19 C 627 PRO GLU LYS ALA VAL ARG PHE SER PHE THR VAL MET ARG
SEQRES 20 C 627 ILE THR ILE GLU HIS GLY SER GLN ASN VAL LYS VAL PHE
SEQRES 21 C 627 GLU GLU PRO LYS PRO ASN SER GLU LEU CYS CYS LYS PRO
SEQRES 22 C 627 LEU CYS LEU MET LEU ALA ASP GLU SER ASP HIS GLU THR
SEQRES 23 C 627 LEU THR ALA ILE LEU SER PRO LEU ILE ALA GLU ARG GLU
SEQRES 24 C 627 ALA MET LYS SER SER GLU LEU THR LEU GLU MET GLY GLY
SEQRES 25 C 627 ILE PRO ARG THR PHE LYS PHE ILE PHE ARG GLY THR GLY
SEQRES 26 C 627 TYR ASP GLU LYS LEU VAL ARG GLU VAL GLU GLY LEU GLU
SEQRES 27 C 627 ALA SER GLY SER VAL TYR ILE CYS THR LEU CYS ASP THR
SEQRES 28 C 627 THR ARG LEU GLU ALA SER GLN ASN LEU VAL PHE HIS SER
SEQRES 29 C 627 ILE THR ARG SER HIS ALA GLU ASN LEU GLN ARG TYR GLU
SEQRES 30 C 627 VAL TRP ARG SER ASN PRO TYR HIS GLU SER VAL GLU GLU
SEQRES 31 C 627 LEU ARG ASP ARG VAL LYS GLY VAL SER ALA LYS PRO PHE
SEQRES 32 C 627 ILE GLU THR VAL PRO SER ILE ASP ALA LEU HIS CYS ASP
SEQRES 33 C 627 ILE GLY ASN ALA ALA GLU PHE TYR LYS ILE PHE GLN LEU
SEQRES 34 C 627 GLU ILE GLY GLU VAL TYR LYS HIS PRO ASN ALA SER LYS
SEQRES 35 C 627 GLU GLU ARG LYS ARG TRP GLN ALA THR LEU ASP LYS HIS
SEQRES 36 C 627 LEU ARG LYS ARG MET ASN LEU LYS PRO ILE MET ARG MET
SEQRES 37 C 627 ASN GLY ASN PHE ALA ARG LYS LEU MET THR GLN GLU THR
SEQRES 38 C 627 VAL ASP ALA VAL CYS GLU LEU ILE PRO SER GLU GLU ARG
SEQRES 39 C 627 HIS GLU ALA LEU ARG GLU LEU MET ASP LEU TYR LEU LYS
SEQRES 40 C 627 MET LYS PRO VAL TRP ARG SER SER CYS PRO ALA LYS GLU
SEQRES 41 C 627 CYS PRO GLU SER LEU CYS GLN TYR SER PHE ASN SER GLN
SEQRES 42 C 627 ARG PHE ALA GLU LEU LEU SER THR LYS PHE LYS TYR ARG
SEQRES 43 C 627 TYR GLU GLY LYS ILE THR ASN TYR PHE HIS LYS THR LEU
SEQRES 44 C 627 ALA HIS VAL PRO GLU ILE ILE GLU ARG ASP GLY SER ILE
SEQRES 45 C 627 GLY ALA TRP ALA SER GLU GLY ASN GLU SER GLY ASN LYS
SEQRES 46 C 627 LEU PHE ARG ARG PHE ARG LYS MET ASN ALA ARG GLN SER
SEQRES 47 C 627 LYS CYS TYR GLU MET GLU ASP VAL LEU LYS HIS HIS TRP
SEQRES 48 C 627 LEU TYR THR SER LYS TYR LEU GLN LYS PHE MET ASN ALA
SEQRES 49 C 627 HIS ASN ALA
SEQRES 1 D 389 GLY PRO VAL SER LEU GLN MET VAL THR VAL GLY HIS ASN
SEQRES 2 D 389 ILE ALA LEU ILE GLN PRO GLY PHE SER LEU MET ASN PHE
SEQRES 3 D 389 ASP GLY GLN VAL PHE PHE PHE GLY GLN LYS GLY TRP PRO
SEQRES 4 D 389 LYS ARG SER CYS PRO THR GLY VAL PHE HIS PHE ASP ILE
SEQRES 5 D 389 LYS GLN ASN HIS LEU LYS LEU LYS PRO ALA ILE PHE SER
SEQRES 6 D 389 LYS ASP SER CYS TYR LEU PRO PRO LEU ARG TYR PRO ALA
SEQRES 7 D 389 THR CYS SER TYR LYS GLY SER ILE ASP SER ASP LYS HIS
SEQRES 8 D 389 GLN TYR ILE ILE HIS GLY GLY LYS THR PRO ASN ASN GLU
SEQRES 9 D 389 LEU SER ASP LYS ILE TYR ILE MET SER VAL ALA CYS LYS
SEQRES 10 D 389 ASN ASN LYS LYS VAL THR PHE ARG CYS THR GLU LYS ASP
SEQRES 11 D 389 LEU VAL GLY ASP VAL PRO GLU PRO ARG TYR GLY HIS SER
SEQRES 12 D 389 ILE ASP VAL VAL TYR SER ARG GLY LYS SER MET GLY VAL
SEQRES 13 D 389 LEU PHE GLY GLY ARG SER TYR MET PRO SER THR GLN ARG
SEQRES 14 D 389 THR THR GLU LYS TRP ASN SER VAL ALA ASP CYS LEU PRO
SEQRES 15 D 389 HIS VAL PHE LEU ILE ASP PHE GLU PHE GLY CYS ALA THR
SEQRES 16 D 389 SER TYR ILE LEU PRO GLU LEU GLN ASP GLY LEU SER PHE
SEQRES 17 D 389 HIS VAL SER ILE ALA ARG ASN ASP THR VAL TYR ILE LEU
SEQRES 18 D 389 GLY GLY HIS SER LEU ALA SER ASN ILE ARG PRO ALA ASN
SEQRES 19 D 389 LEU TYR ARG ILE ARG VAL ASP LEU PRO LEU GLY THR PRO
SEQRES 20 D 389 ALA VAL ASN CYS THR VAL LEU PRO GLY GLY ILE SER VAL
SEQRES 21 D 389 SER SER ALA ILE LEU THR GLN THR ASN ASN ASP GLU PHE
SEQRES 22 D 389 VAL ILE VAL GLY GLY TYR GLN LEU GLU ASN GLN LYS ARG
SEQRES 23 D 389 MET VAL CYS SER LEU VAL SER LEU GLY ASP ASN THR ILE
SEQRES 24 D 389 GLU ILE SER GLU MET GLU THR PRO ASP TRP THR SER ASP
SEQRES 25 D 389 ILE LYS HIS SER LYS ILE TRP PHE GLY SER ASN MET GLY
SEQRES 26 D 389 ASN GLY THR ILE PHE LEU GLY ILE PRO GLY ASP ASN LYS
SEQRES 27 D 389 GLN ALA MET SER GLU ALA PHE TYR PHE TYR THR LEU ARG
SEQRES 28 D 389 CYS SER GLU GLU ASP LEU SER GLU ASP GLN LYS ILE VAL
SEQRES 29 D 389 SER ASN SER GLN THR SER THR GLU ASP PRO GLY ASP SER
SEQRES 30 D 389 THR PRO PHE GLU ASP SER GLU GLU PHE CYS PHE SER
SEQRES 1 N 163 MET GLY LYS GLY ASP PRO LYS LYS PRO ARG GLY LYS MET
SEQRES 2 N 163 SER SER TYR ALA PHE PHE VAL GLN THR CYS ARG GLU GLU
SEQRES 3 N 163 HIS LYS LYS LYS HIS PRO ASP ALA SER VAL ASN PHE SER
SEQRES 4 N 163 GLU PHE SER LYS LYS CYS SER GLU ARG TRP LYS THR MET
SEQRES 5 N 163 SER ALA LYS GLU LYS GLY LYS PHE GLU ASP MET ALA LYS
SEQRES 6 N 163 ALA ASP LYS ALA ARG TYR GLU ARG GLU MET LYS THR TYR
SEQRES 7 N 163 ILE PRO PRO LYS GLY GLU THR LYS LYS LYS PHE LYS ASP
SEQRES 8 N 163 PRO ASN ALA PRO LYS ARG PRO PRO SER ALA PHE PHE LEU
SEQRES 9 N 163 PHE CYS SER GLU TYR ARG PRO LYS ILE LYS GLY GLU HIS
SEQRES 10 N 163 PRO GLY LEU SER ILE GLY ASP VAL ALA LYS LYS LEU GLY
SEQRES 11 N 163 GLU MET TRP ASN ASN THR ALA ALA ASP ASP LYS GLN PRO
SEQRES 12 N 163 TYR GLU LYS LYS ALA ALA LYS LEU LYS GLU LYS TYR GLU
SEQRES 13 N 163 LYS ASP ILE ALA ALA TYR ARG
SEQRES 1 F 45 DC DG DG DG DT DT DT DT DT DG DT DT DA
SEQRES 2 F 45 DA DG DG DG DC DT DG DT DA DT DC DA DC
SEQRES 3 F 45 DT DG DT DG DT DA DA DG DA DC DA DG DG
SEQRES 4 F 45 DC DC DA DG DA DT
SEQRES 1 I 16 DA DA DT DC DT DG DG DC DC DT DG DT DC
SEQRES 2 I 16 DT DT DA
SEQRES 1 J 16 DT DA DT DC DT DG DG DC DC DT DG DT DC
SEQRES 2 J 16 DT DT DA
SEQRES 1 G 54 DG DG DT DT DT DT DT DG DT DC DT DG DG
SEQRES 2 G 54 DC DT DT DC DA DC DA DC DT DT DG DA DT
SEQRES 3 G 54 DT DT DG DC DA DT DC DA DC DT DG DT DG
SEQRES 4 G 54 DT DA DA DG DA DC DA DG DG DC DC DA DG
SEQRES 5 G 54 DA DT
SEQRES 1 L 30 DC DA DC DA DG DT DG DA DT DA DC DA DG
SEQRES 2 L 30 DC DC DC DT DT DA DA DC DA DA DA DA DA
SEQRES 3 L 30 DC DC DC DG
SEQRES 1 M 39 DC DA DC DA DG DT DG DA DT DG DC DA DA
SEQRES 2 M 39 DA DT DC DA DA DG DT DG DT DG DA DA DG
SEQRES 3 M 39 DC DC DA DG DA DC DA DA DA DA DA DC DC
HET MG A2001 1
HET ZN A2002 1
HET EDO A2003 4
HET EDO A2004 4
HET K A2005 1
HET MG C2001 1
HET ZN C2002 1
HET K C2003 1
HET EDO C2004 4
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM K POTASSIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 12 MG 2(MG 2+)
FORMUL 13 ZN 2(ZN 2+)
FORMUL 14 EDO 3(C2 H6 O2)
FORMUL 16 K 2(K 1+)
FORMUL 21 HOH *169(H2 O)
HELIX 1 AA1 THR A 400 GLU A 423 1 24
HELIX 2 AA2 ASP A 426 ARG A 442 1 17
HELIX 3 AA3 GLU A 444 GLN A 456 1 13
HELIX 4 AA4 GLN A 463 PHE A 475 1 13
HELIX 5 AA5 SER A 477 GLY A 493 1 17
HELIX 6 AA6 PRO A 499 LEU A 511 1 13
HELIX 7 AA7 ARG A 558 MET A 570 1 13
HELIX 8 AA8 MET A 570 GLN A 581 1 12
HELIX 9 AA9 SER A 648 CYS A 652 5 5
HELIX 10 AB1 ASP A 664 SER A 684 1 21
HELIX 11 AB2 ASP A 708 GLU A 716 1 9
HELIX 12 AB3 THR A 733 ASN A 740 1 8
HELIX 13 AB4 SER A 749 ASN A 763 1 15
HELIX 14 AB5 SER A 768 LYS A 777 1 10
HELIX 15 AB6 ASP A 792 GLY A 813 1 22
HELIX 16 AB7 SER A 822 ASN A 842 1 21
HELIX 17 AB8 ASN A 850 MET A 858 1 9
HELIX 18 AB9 THR A 859 GLU A 868 1 10
HELIX 19 AC1 SER A 872 SER A 895 1 24
HELIX 20 AC2 CYS A 897 CYS A 902 1 6
HELIX 21 AC3 CYS A 902 LYS A 923 1 22
HELIX 22 AC4 PHE A 924 GLU A 929 1 6
HELIX 23 AC5 THR A 933 HIS A 942 1 10
HELIX 24 AC6 HIS A 942 GLY A 951 1 10
HELIX 25 AC7 ILE A 953 ALA A 957 5 5
HELIX 26 AC8 SER A 958 ASN A 975 1 18
HELIX 27 AC9 TYR A 982 THR A 995 1 14
HELIX 28 AD1 SER A 996 PHE A 1002 1 7
HELIX 29 AD2 MET A 1003 ALA A 1005 5 3
HELIX 30 AD3 ASN B 11 ILE B 15 5 5
HELIX 31 AD4 LYS B 115 LYS B 119 5 5
HELIX 32 AD5 THR B 168 TRP B 172 5 5
HELIX 33 AD6 THR B 308 SER B 314 1 7
HELIX 34 AD7 HIS C 395 LEU C 399 5 5
HELIX 35 AD8 THR C 400 GLY C 424 1 25
HELIX 36 AD9 ASP C 426 ARG C 442 1 17
HELIX 37 AE1 GLU C 444 MET C 455 1 12
HELIX 38 AE2 GLN C 463 THR C 474 1 12
HELIX 39 AE3 SER C 477 GLY C 493 1 17
HELIX 40 AE4 PRO C 499 LEU C 511 1 13
HELIX 41 AE5 ARG C 558 MET C 570 1 13
HELIX 42 AE6 MET C 570 GLN C 581 1 12
HELIX 43 AE7 ASP C 664 SER C 684 1 21
HELIX 44 AE8 ASP C 708 GLU C 716 1 9
HELIX 45 AE9 THR C 733 LEU C 741 1 9
HELIX 46 AF1 SER C 749 ASN C 763 1 15
HELIX 47 AF2 SER C 768 LYS C 777 1 10
HELIX 48 AF3 ASP C 792 GLU C 814 1 23
HELIX 49 AF4 VAL C 815 HIS C 818 5 4
HELIX 50 AF5 SER C 822 ASN C 842 1 21
HELIX 51 AF6 ASN C 850 MET C 858 1 9
HELIX 52 AF7 THR C 859 GLU C 868 1 10
HELIX 53 AF8 SER C 872 SER C 895 1 24
HELIX 54 AF9 CYS C 897 CYS C 902 1 6
HELIX 55 AG1 CYS C 902 GLN C 908 1 7
HELIX 56 AG2 GLN C 908 LYS C 923 1 16
HELIX 57 AG3 PHE C 924 GLU C 929 1 6
HELIX 58 AG4 THR C 933 HIS C 942 1 10
HELIX 59 AG5 HIS C 942 GLY C 951 1 10
HELIX 60 AG6 ILE C 953 ALA C 957 5 5
HELIX 61 AG7 SER C 958 ASN C 975 1 18
HELIX 62 AG8 TYR C 982 THR C 995 1 14
HELIX 63 AG9 SER C 996 MET C 1003 1 8
HELIX 64 AH1 ASN D 11 ILE D 15 5 5
HELIX 65 AH2 THR D 168 TRP D 172 5 5
HELIX 66 AH3 THR D 308 SER D 314 1 7
HELIX 67 AH4 SER N 14 HIS N 31 1 18
HELIX 68 AH5 ASN N 37 LYS N 50 1 14
HELIX 69 AH6 LYS N 57 LYS N 76 1 20
HELIX 70 AH7 SER N 100 GLU N 116 1 17
HELIX 71 AH8 GLY N 123 THR N 136 1 14
HELIX 72 AH9 LYS N 141 LYS N 157 1 17
SHEET 1 AA1 8 PHE A 517 GLN A 520 0
SHEET 2 AA1 8 GLU A 686 MET A 691 -1 O THR A 688 N GLU A 518
SHEET 3 AA1 8 ILE A 694 GLY A 706 -1 O ARG A 696 N LEU A 689
SHEET 4 AA1 8 PRO A 590 MET A 602 1 N GLU A 597 O ARG A 703
SHEET 5 AA1 8 ALA A 619 GLU A 632 -1 O ALA A 619 N MET A 602
SHEET 6 AA1 8 LYS A 653 LEU A 659 -1 O LYS A 653 N PHE A 624
SHEET 7 AA1 8 ILE A 553 PHE A 557 -1 N ILE A 553 O LEU A 659
SHEET 8 AA1 8 ILE A 534 ASP A 536 -1 N ILE A 535 O ARG A 556
SHEET 1 AA2 6 PHE A 517 GLN A 520 0
SHEET 2 AA2 6 GLU A 686 MET A 691 -1 O THR A 688 N GLU A 518
SHEET 3 AA2 6 ILE A 694 GLY A 706 -1 O ARG A 696 N LEU A 689
SHEET 4 AA2 6 PRO A 590 MET A 602 1 N GLU A 597 O ARG A 703
SHEET 5 AA2 6 ALA A 619 GLU A 632 -1 O ALA A 619 N MET A 602
SHEET 6 AA2 6 ASN A 637 GLU A 642 -1 O VAL A 638 N ILE A 631
SHEET 1 AA3 8 SER B 20 PHE B 24 0
SHEET 2 AA3 8 GLN B 27 PHE B 31 -1 O PHE B 31 N SER B 20
SHEET 3 AA3 8 PHE B 46 LYS B 51 -1 O PHE B 46 N PHE B 30
SHEET 4 AA3 8 HIS B 54 PRO B 59 -1 O LYS B 58 N HIS B 47
SHEET 5 AA3 8 LEU B 3 VAL B 8 1 N THR B 7 O LEU B 55
SHEET 6 AA3 8 PHE B 343 LEU B 348 -1 O THR B 347 N GLN B 4
SHEET 7 AA3 8 ILE B 327 PRO B 332 -1 N LEU B 329 O TYR B 346
SHEET 8 AA3 8 PHE B 318 ASN B 321 -1 N PHE B 318 O GLY B 330
SHEET 1 AA4 5 ILE B 61 PHE B 62 0
SHEET 2 AA4 5 THR B 121 LYS B 127 1 O PHE B 122 N ILE B 61
SHEET 3 AA4 5 ILE B 107 CYS B 114 -1 N ALA B 113 O THR B 121
SHEET 4 AA4 5 GLN B 90 HIS B 94 -1 N TYR B 91 O MET B 110
SHEET 5 AA4 5 ALA B 76 TYR B 80 -1 N ALA B 76 O HIS B 94
SHEET 1 AA5 5 VAL B 130 GLY B 131 0
SHEET 2 AA5 5 CYS B 191 TYR B 195 1 O ALA B 192 N VAL B 130
SHEET 3 AA5 5 VAL B 182 ASP B 186 -1 N LEU B 184 O THR B 193
SHEET 4 AA5 5 SER B 151 PHE B 156 -1 N GLY B 153 O ILE B 185
SHEET 5 AA5 5 SER B 141 TYR B 146 -1 N ASP B 143 O VAL B 154
SHEET 1 AA6 2 ARG B 159 TYR B 161 0
SHEET 2 AA6 2 VAL B 175 ASP B 177 -1 O ALA B 176 N SER B 160
SHEET 1 AA7 4 VAL B 208 ARG B 212 0
SHEET 2 AA7 4 THR B 215 LEU B 219 -1 O TYR B 217 N ILE B 210
SHEET 3 AA7 4 LEU B 233 ASP B 239 -1 O ILE B 236 N VAL B 216
SHEET 4 AA7 4 ALA B 246 LEU B 252 -1 O THR B 250 N ARG B 235
SHEET 1 AA8 4 ILE B 262 ASN B 267 0
SHEET 2 AA8 4 GLU B 270 VAL B 274 -1 O VAL B 272 N THR B 264
SHEET 3 AA8 4 CYS B 287 LEU B 292 -1 O VAL B 290 N PHE B 271
SHEET 4 AA8 4 ILE B 297 MET B 302 -1 O GLU B 298 N SER B 291
SHEET 1 AA9 2 TYR B 277 LEU B 279 0
SHEET 2 AA9 2 GLN B 282 LYS B 283 -1 O GLN B 282 N LEU B 279
SHEET 1 AB1 8 GLU C 518 GLN C 520 0
SHEET 2 AB1 8 GLU C 686 MET C 691 -1 O THR C 688 N GLU C 518
SHEET 3 AB1 8 ILE C 694 GLY C 706 -1 O ARG C 696 N LEU C 689
SHEET 4 AB1 8 PHE C 591 GLY C 603 1 N PHE C 591 O THR C 697
SHEET 5 AB1 8 LYS C 618 GLU C 632 -1 O THR C 630 N THR C 592
SHEET 6 AB1 8 LYS C 653 LEU C 659 -1 O MET C 658 N VAL C 620
SHEET 7 AB1 8 ILE C 553 ARG C 556 -1 N LYS C 555 O LEU C 657
SHEET 8 AB1 8 ILE C 535 ASP C 536 -1 N ILE C 535 O ARG C 556
SHEET 1 AB2 6 GLU C 518 GLN C 520 0
SHEET 2 AB2 6 GLU C 686 MET C 691 -1 O THR C 688 N GLU C 518
SHEET 3 AB2 6 ILE C 694 GLY C 706 -1 O ARG C 696 N LEU C 689
SHEET 4 AB2 6 PHE C 591 GLY C 603 1 N PHE C 591 O THR C 697
SHEET 5 AB2 6 LYS C 618 GLU C 632 -1 O THR C 630 N THR C 592
SHEET 6 AB2 6 ASN C 637 GLU C 642 -1 O PHE C 641 N ILE C 629
SHEET 1 AB3 5 THR D 7 VAL D 8 0
SHEET 2 AB3 5 HIS D 54 PRO D 59 1 O LEU D 55 N THR D 7
SHEET 3 AB3 5 VAL D 45 LYS D 51 -1 N HIS D 47 O LYS D 58
SHEET 4 AB3 5 GLN D 27 PHE D 31 -1 N PHE D 30 O PHE D 46
SHEET 5 AB3 5 SER D 20 PHE D 24 -1 N PHE D 24 O GLN D 27
SHEET 1 AB4 5 ILE D 61 PHE D 62 0
SHEET 2 AB4 5 LYS D 119 LYS D 127 1 O PHE D 122 N ILE D 61
SHEET 3 AB4 5 ILE D 107 ASN D 116 -1 N SER D 111 O ARG D 123
SHEET 4 AB4 5 GLN D 90 HIS D 94 -1 N ILE D 93 O TYR D 108
SHEET 5 AB4 5 ALA D 76 TYR D 80 -1 N TYR D 80 O GLN D 90
SHEET 1 AB5 5 VAL D 130 GLY D 131 0
SHEET 2 AB5 5 CYS D 191 TYR D 195 1 O ALA D 192 N VAL D 130
SHEET 3 AB5 5 VAL D 182 ASP D 186 -1 N LEU D 184 O THR D 193
SHEET 4 AB5 5 LYS D 150 PHE D 156 -1 N GLY D 153 O ILE D 185
SHEET 5 AB5 5 SER D 141 SER D 147 -1 N ASP D 143 O VAL D 154
SHEET 1 AB6 2 ARG D 159 TYR D 161 0
SHEET 2 AB6 2 VAL D 175 ASP D 177 -1 O ALA D 176 N SER D 160
SHEET 1 AB7 2 VAL D 208 ARG D 212 0
SHEET 2 AB7 2 THR D 215 LEU D 219 -1 O LEU D 219 N VAL D 208
SHEET 1 AB8 2 LEU D 233 ASP D 239 0
SHEET 2 AB8 2 ALA D 246 LEU D 252 -1 O ASN D 248 N ARG D 237
SHEET 1 AB9 4 ILE D 262 THR D 266 0
SHEET 2 AB9 4 GLU D 270 VAL D 274 -1 O GLU D 270 N THR D 266
SHEET 3 AB9 4 CYS D 287 LEU D 292 -1 O VAL D 290 N PHE D 271
SHEET 4 AB9 4 ILE D 297 MET D 302 -1 O SER D 300 N LEU D 289
SHEET 1 AC1 3 PHE D 318 ASN D 321 0
SHEET 2 AC1 3 ILE D 327 PRO D 332 -1 O GLY D 330 N PHE D 318
SHEET 3 AC1 3 PHE D 343 TYR D 346 -1 O TYR D 344 N ILE D 331
LINK O GLY A 601 MG MG A2001 1555 1555 2.66
LINK OE1 GLU A 649 K K A2005 1555 1555 2.72
LINK SG CYS A 727 ZN ZN A2002 1555 1555 2.19
LINK SG CYS A 730 ZN ZN A2002 1555 1555 2.20
LINK NE2 HIS A 937 ZN ZN A2002 1555 1555 2.30
LINK NE2 HIS A 942 ZN ZN A2002 1555 1555 1.93
LINK OG SER A 963 K K A2005 1555 1555 3.42
LINK K K A2005 O HOH A2138 1555 1555 2.90
LINK K K A2005 O4' DC L 19 1555 1555 2.90
LINK K K A2005 O2 DC L 19 1555 1555 2.86
LINK K K A2005 O HOH L4104 1555 1555 2.55
LINK OD1 ASP C 600 MG MG C2001 1555 1555 2.61
LINK O GLY C 601 MG MG C2001 1555 1555 2.87
LINK OE1 GLU C 649 K K C2003 1555 1555 2.73
LINK SG CYS C 727 ZN ZN C2002 1555 1555 2.24
LINK SG CYS C 730 ZN ZN C2002 1555 1555 2.21
LINK NE2 HIS C 937 ZN ZN C2002 1555 1555 2.06
LINK NE2 HIS C 942 ZN ZN C2002 1555 1555 1.93
LINK OE1 GLU C 962 MG MG C2001 1555 1555 2.98
LINK OG SER C 963 K K C2003 1555 1555 3.18
LINK MG MG C2001 O3' DG G 41 1555 1555 2.94
LINK MG MG C2001 OP2 DT G 42 1555 1555 2.82
LINK K K C2003 O HOH C2104 1555 1555 2.65
LINK K K C2003 O HOH G 107 1555 1555 2.64
LINK K K C2003 O4' DC M 19 1555 1555 3.10
LINK K K C2003 O2 DC M 19 1555 1555 2.69
CISPEP 1 GLN A 520 PRO A 521 0 0.15
CISPEP 2 GLN C 520 PRO C 521 0 -1.15
SITE 1 AC1 6 ASP A 600 GLY A 601 GLU A 962 ASN A 965
SITE 2 AC1 6 DG F 30 DT F 31
SITE 1 AC2 4 CYS A 727 CYS A 730 HIS A 937 HIS A 942
SITE 1 AC3 6 VAL A 545 ASP A 546 GLU A 547 TYR B 74
SITE 2 AC3 6 TYR B 277 TRP B 317
SITE 1 AC4 5 LEU A 718 THR A 728 ASN A 753 THR A 787
SITE 2 AC4 5 PRO A 789
SITE 1 AC5 6 GLU A 649 SER A 963 HOH A2138 DA L 18
SITE 2 AC5 6 DC L 19 HOH L4104
SITE 1 AC6 7 ASP C 600 GLY C 601 GLU C 962 ASN C 965
SITE 2 AC6 7 DG G 41 DT G 42 HOH G 102
SITE 1 AC7 4 CYS C 727 CYS C 730 HIS C 937 HIS C 942
SITE 1 AC8 7 GLU C 649 SER C 963 HOH C2104 DG G 39
SITE 2 AC8 7 HOH G 107 DA M 18 DC M 19
SITE 1 AC9 2 ARG C 628 TRP C 956
CRYST1 132.440 109.030 156.850 90.00 114.43 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007551 0.000000 0.003429 0.00000
SCALE2 0.000000 0.009172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007002 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
