HEADER LIGASE 02-JAN-12 3VBB
TITLE CRYSTAL STRUCTURE OF SERYL-TRNA SYNTHETASE FROM HUMAN AT 2.9 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERYL-TRNA SYNTHETASE, CYTOPLASMIC;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: SERINE--TRNA LIGASE, SERRS, SERYL-TRNA(SER/SEC) SYNTHETASE;
COMPND 5 EC: 6.1.1.11;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SARS, SERS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: E.COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B
KEYWDS COILED-COIL, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.L.XU,X.-L.YANG
REVDAT 3 13-SEP-23 3VBB 1 REMARK SEQADV
REVDAT 2 21-MAR-12 3VBB 1 JRNL
REVDAT 1 29-FEB-12 3VBB 0
JRNL AUTH X.XU,Y.SHI,H.M.ZHANG,E.C.SWINDELL,A.G.MARSHALL,M.GUO,
JRNL AUTH 2 S.KISHI,X.L.YANG
JRNL TITL UNIQUE DOMAIN APPENDED TO VERTEBRATE TRNA SYNTHETASE IS
JRNL TITL 2 ESSENTIAL FOR VASCULAR DEVELOPMENT.
JRNL REF NAT COMMUN V. 3 681 2012
JRNL REFN ESSN 2041-1723
JRNL PMID 22353712
JRNL DOI 10.1038/NCOMMS1686
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 108801
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5461
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 48.5998 - 8.9653 0.99 3821 230 0.1920 0.2291
REMARK 3 2 8.9653 - 7.1233 1.00 3743 207 0.1638 0.2035
REMARK 3 3 7.1233 - 6.2249 1.00 3719 177 0.1907 0.2307
REMARK 3 4 6.2249 - 5.6567 1.00 3684 197 0.2138 0.2980
REMARK 3 5 5.6567 - 5.2518 1.00 3639 209 0.2028 0.2562
REMARK 3 6 5.2518 - 4.9425 1.00 3639 205 0.1751 0.2160
REMARK 3 7 4.9425 - 4.6951 1.00 3649 175 0.1474 0.2109
REMARK 3 8 4.6951 - 4.4909 1.00 3652 180 0.1447 0.2043
REMARK 3 9 4.4909 - 4.3181 1.00 3640 189 0.1615 0.2282
REMARK 3 10 4.3181 - 4.1692 1.00 3602 185 0.1689 0.2312
REMARK 3 11 4.1692 - 4.0389 0.99 3613 191 0.1690 0.2206
REMARK 3 12 4.0389 - 3.9235 0.99 3624 177 0.1682 0.2213
REMARK 3 13 3.9235 - 3.8203 0.99 3577 202 0.1823 0.2299
REMARK 3 14 3.8203 - 3.7271 0.99 3577 183 0.1902 0.2454
REMARK 3 15 3.7271 - 3.6424 0.99 3543 193 0.1921 0.2403
REMARK 3 16 3.6424 - 3.5649 0.99 3638 167 0.1949 0.2518
REMARK 3 17 3.5649 - 3.4936 0.98 3505 179 0.2090 0.2503
REMARK 3 18 3.4936 - 3.4277 0.97 3503 198 0.2211 0.3066
REMARK 3 19 3.4277 - 3.3665 0.97 3480 210 0.2149 0.2988
REMARK 3 20 3.3665 - 3.3095 0.96 3475 179 0.2359 0.2765
REMARK 3 21 3.3095 - 3.2561 0.96 3501 160 0.2320 0.2711
REMARK 3 22 3.2561 - 3.2060 0.95 3370 195 0.2345 0.3438
REMARK 3 23 3.2060 - 3.1589 0.93 3359 170 0.2430 0.3305
REMARK 3 24 3.1589 - 3.1144 0.92 3302 196 0.2668 0.3281
REMARK 3 25 3.1144 - 3.0723 0.90 3240 170 0.2876 0.3995
REMARK 3 26 3.0723 - 3.0324 0.87 3191 157 0.3035 0.4222
REMARK 3 27 3.0324 - 2.9945 0.86 3039 151 0.3178 0.3453
REMARK 3 28 2.9945 - 2.9584 0.81 2942 149 0.2969 0.3188
REMARK 3 29 2.9584 - 2.9240 0.77 2755 150 0.2896 0.3514
REMARK 3 30 2.9240 - 2.8910 0.65 2318 130 0.3107 0.3369
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 48.66
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.100
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) : 9.09040
REMARK 3 B22 (A**2) : -18.17120
REMARK 3 B33 (A**2) : 9.08080
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.009 21776
REMARK 3 ANGLE : 1.305 29394
REMARK 3 CHIRALITY : 0.092 3264
REMARK 3 PLANARITY : 0.006 3785
REMARK 3 DIHEDRAL : 16.472 8135
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 3VBB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069829.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113515
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.891
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : 0.45600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2ZR3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M TRI-SODIUM CITRATE
REMARK 280 PH 7.0, 5MM ATP, 10MM MGCL2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 58.40000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.29450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 94.70850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.29450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 58.40000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 94.70850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 73
REMARK 465 VAL A 74
REMARK 465 GLY A 75
REMARK 465 ASP A 76
REMARK 465 GLN A 242
REMARK 465 GLY A 252
REMARK 465 LYS A 253
REMARK 465 GLY A 254
REMARK 465 SER A 255
REMARK 465 GLU A 256
REMARK 465 LYS A 257
REMARK 465 SER A 258
REMARK 465 ASP A 259
REMARK 465 ASP A 260
REMARK 465 ASN A 261
REMARK 465 SER A 262
REMARK 465 TYR A 263
REMARK 465 HIS A 308
REMARK 465 GLY A 309
REMARK 465 ARG A 310
REMARK 465 ASP A 311
REMARK 465 LYS A 414
REMARK 465 LYS A 415
REMARK 465 MET A 416
REMARK 465 GLU A 477
REMARK 465 GLN A 478
REMARK 465 GLU A 479
REMARK 465 PRO A 480
REMARK 465 SER A 481
REMARK 465 LYS A 482
REMARK 465 LYS A 483
REMARK 465 GLN A 484
REMARK 465 LYS A 485
REMARK 465 LYS A 486
REMARK 465 GLN A 487
REMARK 465 HIS A 488
REMARK 465 GLU A 489
REMARK 465 GLY A 490
REMARK 465 SER A 491
REMARK 465 LYS A 492
REMARK 465 LYS A 493
REMARK 465 LYS A 494
REMARK 465 ALA A 495
REMARK 465 ALA A 496
REMARK 465 ALA A 497
REMARK 465 ARG A 498
REMARK 465 ASP A 499
REMARK 465 VAL A 500
REMARK 465 THR A 501
REMARK 465 LEU A 502
REMARK 465 GLU A 503
REMARK 465 ASN A 504
REMARK 465 ARG A 505
REMARK 465 LEU A 506
REMARK 465 GLN A 507
REMARK 465 ASN A 508
REMARK 465 MET A 509
REMARK 465 GLU A 510
REMARK 465 VAL A 511
REMARK 465 THR A 512
REMARK 465 ASP A 513
REMARK 465 ALA A 514
REMARK 465 LEU A 515
REMARK 465 GLU A 516
REMARK 465 HIS A 517
REMARK 465 HIS A 518
REMARK 465 HIS A 519
REMARK 465 HIS A 520
REMARK 465 HIS A 521
REMARK 465 HIS A 522
REMARK 465 MET B 1
REMARK 465 LYS B 71
REMARK 465 GLU B 72
REMARK 465 PRO B 73
REMARK 465 VAL B 74
REMARK 465 GLY B 75
REMARK 465 ASP B 76
REMARK 465 GLY B 252
REMARK 465 LYS B 253
REMARK 465 GLY B 254
REMARK 465 SER B 255
REMARK 465 GLU B 256
REMARK 465 LYS B 257
REMARK 465 SER B 258
REMARK 465 ASP B 259
REMARK 465 ASP B 260
REMARK 465 ASN B 261
REMARK 465 SER B 262
REMARK 465 TYR B 263
REMARK 465 ARG B 310
REMARK 465 ASP B 311
REMARK 465 ILE B 476
REMARK 465 GLU B 477
REMARK 465 GLN B 478
REMARK 465 GLU B 479
REMARK 465 PRO B 480
REMARK 465 SER B 481
REMARK 465 LYS B 482
REMARK 465 LYS B 483
REMARK 465 GLN B 484
REMARK 465 LYS B 485
REMARK 465 LYS B 486
REMARK 465 GLN B 487
REMARK 465 HIS B 488
REMARK 465 GLU B 489
REMARK 465 GLY B 490
REMARK 465 SER B 491
REMARK 465 LYS B 492
REMARK 465 LYS B 493
REMARK 465 LYS B 494
REMARK 465 ALA B 495
REMARK 465 ALA B 496
REMARK 465 ALA B 497
REMARK 465 ARG B 498
REMARK 465 ASP B 499
REMARK 465 VAL B 500
REMARK 465 THR B 501
REMARK 465 LEU B 502
REMARK 465 GLU B 503
REMARK 465 ASN B 504
REMARK 465 ARG B 505
REMARK 465 LEU B 506
REMARK 465 GLN B 507
REMARK 465 ASN B 508
REMARK 465 MET B 509
REMARK 465 GLU B 510
REMARK 465 VAL B 511
REMARK 465 THR B 512
REMARK 465 ASP B 513
REMARK 465 ALA B 514
REMARK 465 LEU B 515
REMARK 465 GLU B 516
REMARK 465 HIS B 517
REMARK 465 HIS B 518
REMARK 465 HIS B 519
REMARK 465 HIS B 520
REMARK 465 HIS B 521
REMARK 465 HIS B 522
REMARK 465 MET C 1
REMARK 465 VAL C 74
REMARK 465 GLY C 75
REMARK 465 ASP C 76
REMARK 465 GLY C 254
REMARK 465 SER C 255
REMARK 465 GLU C 256
REMARK 465 LYS C 257
REMARK 465 SER C 258
REMARK 465 ASP C 259
REMARK 465 ASP C 260
REMARK 465 ASN C 261
REMARK 465 SER C 262
REMARK 465 VAL C 305
REMARK 465 GLY C 306
REMARK 465 SER C 307
REMARK 465 HIS C 308
REMARK 465 GLY C 309
REMARK 465 ARG C 310
REMARK 465 ILE C 476
REMARK 465 GLU C 477
REMARK 465 GLN C 478
REMARK 465 GLU C 479
REMARK 465 PRO C 480
REMARK 465 SER C 481
REMARK 465 LYS C 482
REMARK 465 LYS C 483
REMARK 465 GLN C 484
REMARK 465 LYS C 485
REMARK 465 LYS C 486
REMARK 465 GLN C 487
REMARK 465 HIS C 488
REMARK 465 GLU C 489
REMARK 465 GLY C 490
REMARK 465 SER C 491
REMARK 465 LYS C 492
REMARK 465 LYS C 493
REMARK 465 LYS C 494
REMARK 465 ALA C 495
REMARK 465 ALA C 496
REMARK 465 ALA C 497
REMARK 465 ARG C 498
REMARK 465 ASP C 499
REMARK 465 VAL C 500
REMARK 465 THR C 501
REMARK 465 LEU C 502
REMARK 465 GLU C 503
REMARK 465 ASN C 504
REMARK 465 ARG C 505
REMARK 465 LEU C 506
REMARK 465 GLN C 507
REMARK 465 ASN C 508
REMARK 465 MET C 509
REMARK 465 GLU C 510
REMARK 465 VAL C 511
REMARK 465 THR C 512
REMARK 465 ASP C 513
REMARK 465 ALA C 514
REMARK 465 LEU C 515
REMARK 465 GLU C 516
REMARK 465 HIS C 517
REMARK 465 HIS C 518
REMARK 465 HIS C 519
REMARK 465 HIS C 520
REMARK 465 HIS C 521
REMARK 465 HIS C 522
REMARK 465 MET D 1
REMARK 465 PRO D 73
REMARK 465 VAL D 74
REMARK 465 SER D 79
REMARK 465 VAL D 80
REMARK 465 PRO D 81
REMARK 465 GLN D 242
REMARK 465 GLY D 254
REMARK 465 SER D 255
REMARK 465 GLU D 256
REMARK 465 LYS D 257
REMARK 465 SER D 258
REMARK 465 ASP D 259
REMARK 465 ASP D 260
REMARK 465 ASN D 261
REMARK 465 SER D 262
REMARK 465 TYR D 263
REMARK 465 GLY D 306
REMARK 465 SER D 307
REMARK 465 HIS D 308
REMARK 465 GLY D 309
REMARK 465 ARG D 310
REMARK 465 ASP D 311
REMARK 465 THR D 413
REMARK 465 LYS D 414
REMARK 465 LYS D 415
REMARK 465 GLU D 477
REMARK 465 GLN D 478
REMARK 465 GLU D 479
REMARK 465 PRO D 480
REMARK 465 SER D 481
REMARK 465 LYS D 482
REMARK 465 LYS D 483
REMARK 465 GLN D 484
REMARK 465 LYS D 485
REMARK 465 LYS D 486
REMARK 465 GLN D 487
REMARK 465 HIS D 488
REMARK 465 GLU D 489
REMARK 465 GLY D 490
REMARK 465 SER D 491
REMARK 465 LYS D 492
REMARK 465 LYS D 493
REMARK 465 LYS D 494
REMARK 465 ALA D 495
REMARK 465 ALA D 496
REMARK 465 ALA D 497
REMARK 465 ARG D 498
REMARK 465 ASP D 499
REMARK 465 VAL D 500
REMARK 465 THR D 501
REMARK 465 LEU D 502
REMARK 465 GLU D 503
REMARK 465 ASN D 504
REMARK 465 ARG D 505
REMARK 465 LEU D 506
REMARK 465 GLN D 507
REMARK 465 ASN D 508
REMARK 465 MET D 509
REMARK 465 GLU D 510
REMARK 465 VAL D 511
REMARK 465 THR D 512
REMARK 465 ASP D 513
REMARK 465 ALA D 514
REMARK 465 LEU D 515
REMARK 465 GLU D 516
REMARK 465 HIS D 517
REMARK 465 HIS D 518
REMARK 465 HIS D 519
REMARK 465 HIS D 520
REMARK 465 HIS D 521
REMARK 465 HIS D 522
REMARK 465 MET E 1
REMARK 465 MET E 68
REMARK 465 LYS E 69
REMARK 465 LYS E 70
REMARK 465 LYS E 71
REMARK 465 GLU E 72
REMARK 465 PRO E 73
REMARK 465 VAL E 74
REMARK 465 GLY E 75
REMARK 465 ASP E 76
REMARK 465 ASP E 77
REMARK 465 GLU E 78
REMARK 465 SER E 79
REMARK 465 VAL E 80
REMARK 465 PRO E 81
REMARK 465 GLU E 82
REMARK 465 ASN E 83
REMARK 465 SER E 241
REMARK 465 GLN E 242
REMARK 465 PHE E 243
REMARK 465 ASP E 244
REMARK 465 GLU E 245
REMARK 465 GLY E 254
REMARK 465 SER E 255
REMARK 465 GLU E 256
REMARK 465 LYS E 257
REMARK 465 SER E 258
REMARK 465 ASP E 259
REMARK 465 ASP E 260
REMARK 465 ASN E 261
REMARK 465 SER E 262
REMARK 465 HIS E 308
REMARK 465 GLY E 309
REMARK 465 ARG E 310
REMARK 465 ASP E 311
REMARK 465 THR E 312
REMARK 465 GLU E 477
REMARK 465 GLN E 478
REMARK 465 GLU E 479
REMARK 465 PRO E 480
REMARK 465 SER E 481
REMARK 465 LYS E 482
REMARK 465 LYS E 483
REMARK 465 GLN E 484
REMARK 465 LYS E 485
REMARK 465 LYS E 486
REMARK 465 GLN E 487
REMARK 465 HIS E 488
REMARK 465 GLU E 489
REMARK 465 GLY E 490
REMARK 465 SER E 491
REMARK 465 LYS E 492
REMARK 465 LYS E 493
REMARK 465 LYS E 494
REMARK 465 ALA E 495
REMARK 465 ALA E 496
REMARK 465 ALA E 497
REMARK 465 ARG E 498
REMARK 465 ASP E 499
REMARK 465 VAL E 500
REMARK 465 THR E 501
REMARK 465 LEU E 502
REMARK 465 GLU E 503
REMARK 465 ASN E 504
REMARK 465 ARG E 505
REMARK 465 LEU E 506
REMARK 465 GLN E 507
REMARK 465 ASN E 508
REMARK 465 MET E 509
REMARK 465 GLU E 510
REMARK 465 VAL E 511
REMARK 465 THR E 512
REMARK 465 ASP E 513
REMARK 465 ALA E 514
REMARK 465 LEU E 515
REMARK 465 GLU E 516
REMARK 465 HIS E 517
REMARK 465 HIS E 518
REMARK 465 HIS E 519
REMARK 465 HIS E 520
REMARK 465 HIS E 521
REMARK 465 HIS E 522
REMARK 465 MET F 1
REMARK 465 VAL F 74
REMARK 465 GLY F 75
REMARK 465 ASP F 76
REMARK 465 ASP F 77
REMARK 465 GLU F 78
REMARK 465 SER F 79
REMARK 465 LYS F 99
REMARK 465 LEU F 240
REMARK 465 SER F 241
REMARK 465 GLN F 242
REMARK 465 PHE F 243
REMARK 465 ASP F 244
REMARK 465 LYS F 253
REMARK 465 GLY F 254
REMARK 465 SER F 255
REMARK 465 GLU F 256
REMARK 465 LYS F 257
REMARK 465 SER F 258
REMARK 465 ASP F 259
REMARK 465 ASP F 260
REMARK 465 ASN F 261
REMARK 465 GLY F 306
REMARK 465 SER F 307
REMARK 465 HIS F 308
REMARK 465 GLY F 309
REMARK 465 ARG F 310
REMARK 465 ASP F 311
REMARK 465 THR F 413
REMARK 465 LYS F 414
REMARK 465 LYS F 415
REMARK 465 MET F 416
REMARK 465 MET F 417
REMARK 465 GLU F 477
REMARK 465 GLN F 478
REMARK 465 GLU F 479
REMARK 465 PRO F 480
REMARK 465 SER F 481
REMARK 465 LYS F 482
REMARK 465 LYS F 483
REMARK 465 GLN F 484
REMARK 465 LYS F 485
REMARK 465 LYS F 486
REMARK 465 GLN F 487
REMARK 465 HIS F 488
REMARK 465 GLU F 489
REMARK 465 GLY F 490
REMARK 465 SER F 491
REMARK 465 LYS F 492
REMARK 465 LYS F 493
REMARK 465 LYS F 494
REMARK 465 ALA F 495
REMARK 465 ALA F 496
REMARK 465 ALA F 497
REMARK 465 ARG F 498
REMARK 465 ASP F 499
REMARK 465 VAL F 500
REMARK 465 THR F 501
REMARK 465 LEU F 502
REMARK 465 GLU F 503
REMARK 465 ASN F 504
REMARK 465 ARG F 505
REMARK 465 LEU F 506
REMARK 465 GLN F 507
REMARK 465 ASN F 508
REMARK 465 MET F 509
REMARK 465 GLU F 510
REMARK 465 VAL F 511
REMARK 465 THR F 512
REMARK 465 ASP F 513
REMARK 465 ALA F 514
REMARK 465 LEU F 515
REMARK 465 GLU F 516
REMARK 465 HIS F 517
REMARK 465 HIS F 518
REMARK 465 HIS F 519
REMARK 465 HIS F 520
REMARK 465 HIS F 521
REMARK 465 HIS F 522
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 ASP A 51 CG OD1 OD2
REMARK 470 LYS A 67 CG CD CE NZ
REMARK 470 VAL A 80 CG1 CG2
REMARK 470 LEU A 98 CG CD1 CD2
REMARK 470 ASP A 111 CG OD1 OD2
REMARK 470 LYS A 231 CG CD CE NZ
REMARK 470 GLU A 232 CG CD OE1 OE2
REMARK 470 ASP A 264 CB CG OD1 OD2
REMARK 470 GLU A 265 CG CD OE1 OE2
REMARK 470 VAL A 305 CG1 CG2
REMARK 470 SER A 307 OG
REMARK 470 MET A 417 CG SD CE
REMARK 470 LEU B 59 CG CD1 CD2
REMARK 470 SER B 79 OG
REMARK 470 VAL B 80 CG1 CG2
REMARK 470 PRO B 81 CG CD
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 ASN B 83 CG OD1 ND2
REMARK 470 VAL B 84 CG1 CG2
REMARK 470 LYS B 231 CG CD CE NZ
REMARK 470 GLN B 242 CG CD OE1 NE2
REMARK 470 GLU B 246 CG CD OE1 OE2
REMARK 470 ASP B 264 CB CG OD1 OD2
REMARK 470 VAL B 305 CG1 CG2
REMARK 470 SER B 307 OG
REMARK 470 HIS B 308 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 67 CG CD CE NZ
REMARK 470 PRO C 73 CG CD
REMARK 470 ASP C 77 CG OD1 OD2
REMARK 470 GLU C 78 CG CD OE1 OE2
REMARK 470 ASP C 93 CG OD1 OD2
REMARK 470 LEU C 98 CG CD1 CD2
REMARK 470 LYS C 99 CG CD CE NZ
REMARK 470 LYS C 105 CG CD CE NZ
REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 183 CG CD OE1 OE2
REMARK 470 ARG C 192 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 231 CG CD CE NZ
REMARK 470 GLU C 232 CG CD OE1 OE2
REMARK 470 GLU C 246 CG CD OE1 OE2
REMARK 470 LYS C 253 CG CD CE NZ
REMARK 470 TYR C 263 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 265 CG CD OE1 OE2
REMARK 470 THR C 271 OG1 CG2
REMARK 470 ARG C 313 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 317 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 412 CG CD OE1 NE2
REMARK 470 THR C 413 OG1 CG2
REMARK 470 LYS C 414 CG CD CE NZ
REMARK 470 LYS C 415 CG CD CE NZ
REMARK 470 MET C 416 CG SD CE
REMARK 470 LYS C 419 CG CD CE NZ
REMARK 470 ASP D 51 CG OD1 OD2
REMARK 470 MET D 68 CG SD CE
REMARK 470 LYS D 70 CG CD CE NZ
REMARK 470 GLU D 72 CG CD OE1 OE2
REMARK 470 ASP D 76 CG OD1 OD2
REMARK 470 ASP D 77 CG OD1 OD2
REMARK 470 GLU D 78 CG CD OE1 OE2
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 ASN D 83 CG OD1 ND2
REMARK 470 VAL D 84 CG1 CG2
REMARK 470 ASP D 93 CG OD1 OD2
REMARK 470 ASN D 97 CG OD1 ND2
REMARK 470 GLU D 183 CG CD OE1 OE2
REMARK 470 SER D 191 OG
REMARK 470 ARG D 192 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 230 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 232 CG CD OE1 OE2
REMARK 470 PHE D 243 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 253 CG CD CE NZ
REMARK 470 ASP D 264 CG OD1 OD2
REMARK 470 GLU D 265 CG CD OE1 OE2
REMARK 470 ARG D 286 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 304 CG CD OE1 OE2
REMARK 470 VAL D 305 CG1 CG2
REMARK 470 THR D 312 OG1 CG2
REMARK 470 ARG D 313 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 317 CG CD NE CZ NH1 NH2
REMARK 470 MET D 416 CG SD CE
REMARK 470 LEU E 59 CG CD1 CD2
REMARK 470 LYS E 67 CG CD CE NZ
REMARK 470 VAL E 84 CG1 CG2
REMARK 470 LEU E 95 CG CD1 CD2
REMARK 470 GLU E 183 CG CD OE1 OE2
REMARK 470 ARG E 230 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 231 CG CD CE NZ
REMARK 470 GLU E 232 CG CD OE1 OE2
REMARK 470 LEU E 240 CG CD1 CD2
REMARK 470 GLU E 246 CG CD OE1 OE2
REMARK 470 VAL E 250 CG1 CG2
REMARK 470 LYS E 253 CG CD CE NZ
REMARK 470 TYR E 263 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU E 265 CG CD OE1 OE2
REMARK 470 ARG E 302 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 304 CG CD OE1 OE2
REMARK 470 VAL E 305 CG1 CG2
REMARK 470 SER E 307 OG
REMARK 470 ARG E 313 CG CD NE CZ NH1 NH2
REMARK 470 ILE E 315 CG1 CG2 CD1
REMARK 470 THR E 413 OG1 CG2
REMARK 470 GLU E 447 CG CD OE1 OE2
REMARK 470 LYS E 448 CG CD CE NZ
REMARK 470 LYS F 57 CG CD CE NZ
REMARK 470 LEU F 59 CG CD1 CD2
REMARK 470 GLU F 66 CG CD OE1 OE2
REMARK 470 LYS F 67 CG CD CE NZ
REMARK 470 LYS F 69 CG CD CE NZ
REMARK 470 PRO F 73 CG CD
REMARK 470 VAL F 80 CG1 CG2
REMARK 470 GLU F 82 CG CD OE1 OE2
REMARK 470 ASN F 83 CG OD1 ND2
REMARK 470 VAL F 84 CG1 CG2
REMARK 470 ASP F 88 CG OD1 OD2
REMARK 470 LEU F 90 CG CD1 CD2
REMARK 470 LEU F 95 CG CD1 CD2
REMARK 470 ASN F 97 CG OD1 ND2
REMARK 470 ARG F 192 CG CD NE CZ NH1 NH2
REMARK 470 ILE F 251 CG1 CG2 CD1
REMARK 470 GLU F 265 CG CD OE1 OE2
REMARK 470 THR F 312 OG1 CG2
REMARK 470 GLU F 466 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 236 CB CG CD OE1 OE2
REMARK 480 LYS C 167 CD CE NZ
REMARK 480 LYS D 123 CD CE NZ
REMARK 480 GLU D 130 OE1 OE2
REMARK 480 GLU D 421 OE1 OE2
REMARK 480 GLU E 156 CD
REMARK 480 ARG F 47 CD NE CZ NH1 NH2
REMARK 480 LYS F 55 CG CD CE NZ
REMARK 480 THR F 63 CA C
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 PHE A 27 -0.99 76.59
REMARK 500 LYS A 71 174.32 176.27
REMARK 500 SER A 86 163.06 173.55
REMARK 500 LYS A 99 -133.44 61.65
REMARK 500 SER A 101 -12.45 69.01
REMARK 500 GLN A 102 -62.68 -90.05
REMARK 500 ARG A 192 -2.34 71.37
REMARK 500 ASP A 244 -71.64 -56.54
REMARK 500 LEU A 247 -137.00 50.91
REMARK 500 GLU A 265 67.91 60.80
REMARK 500 GLU A 304 71.78 63.46
REMARK 500 ASP A 334 -137.85 56.73
REMARK 500 THR A 399 -132.11 46.48
REMARK 500 PHE B 87 -17.11 79.53
REMARK 500 ARG B 192 -3.97 75.44
REMARK 500 ASP B 244 -71.84 -104.46
REMARK 500 GLU B 245 -70.39 -49.62
REMARK 500 ASP B 334 3.08 81.54
REMARK 500 THR B 399 -131.89 44.62
REMARK 500 THR B 446 -89.31 -126.15
REMARK 500 GLU B 447 -66.79 -137.42
REMARK 500 GLU B 466 -111.08 58.95
REMARK 500 LYS C 71 -125.92 59.68
REMARK 500 GLU C 78 -66.00 -129.03
REMARK 500 LEU C 98 -7.52 85.64
REMARK 500 LYS C 99 -139.38 50.04
REMARK 500 GLU C 149 -15.96 76.99
REMARK 500 ARG C 192 -3.27 81.55
REMARK 500 LEU C 240 -137.24 56.21
REMARK 500 GLU C 246 71.08 61.77
REMARK 500 GLU C 265 70.03 44.31
REMARK 500 ALA C 270 -60.65 -104.27
REMARK 500 SER C 272 -4.47 68.17
REMARK 500 THR C 399 -135.25 45.42
REMARK 500 MET C 416 73.26 62.10
REMARK 500 MET C 417 -2.52 89.44
REMARK 500 ASP C 418 66.99 63.11
REMARK 500 VAL C 420 72.54 59.98
REMARK 500 GLU C 466 -19.46 76.17
REMARK 500 LEU C 467 155.56 179.84
REMARK 500 LEU D 7 -14.92 85.78
REMARK 500 GLU D 66 -63.74 -128.52
REMARK 500 VAL D 84 -7.39 85.41
REMARK 500 LEU D 85 -131.33 47.13
REMARK 500 LEU D 90 -73.81 -100.06
REMARK 500 THR D 91 72.66 46.15
REMARK 500 ARG D 192 -3.15 85.14
REMARK 500 ALA D 238 -122.26 61.40
REMARK 500 ASN D 335 19.45 59.34
REMARK 500 THR D 399 -135.83 47.74
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 601
DBREF 3VBB A 1 514 UNP P49591 SYSC_HUMAN 1 514
DBREF 3VBB B 1 514 UNP P49591 SYSC_HUMAN 1 514
DBREF 3VBB C 1 514 UNP P49591 SYSC_HUMAN 1 514
DBREF 3VBB D 1 514 UNP P49591 SYSC_HUMAN 1 514
DBREF 3VBB E 1 514 UNP P49591 SYSC_HUMAN 1 514
DBREF 3VBB F 1 514 UNP P49591 SYSC_HUMAN 1 514
SEQADV 3VBB LEU A 515 UNP P49591 EXPRESSION TAG
SEQADV 3VBB GLU A 516 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS A 517 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS A 518 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS A 519 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS A 520 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS A 521 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS A 522 UNP P49591 EXPRESSION TAG
SEQADV 3VBB LEU B 515 UNP P49591 EXPRESSION TAG
SEQADV 3VBB GLU B 516 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS B 517 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS B 518 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS B 519 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS B 520 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS B 521 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS B 522 UNP P49591 EXPRESSION TAG
SEQADV 3VBB LEU C 515 UNP P49591 EXPRESSION TAG
SEQADV 3VBB GLU C 516 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS C 517 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS C 518 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS C 519 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS C 520 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS C 521 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS C 522 UNP P49591 EXPRESSION TAG
SEQADV 3VBB LEU D 515 UNP P49591 EXPRESSION TAG
SEQADV 3VBB GLU D 516 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS D 517 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS D 518 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS D 519 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS D 520 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS D 521 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS D 522 UNP P49591 EXPRESSION TAG
SEQADV 3VBB LEU E 515 UNP P49591 EXPRESSION TAG
SEQADV 3VBB GLU E 516 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS E 517 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS E 518 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS E 519 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS E 520 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS E 521 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS E 522 UNP P49591 EXPRESSION TAG
SEQADV 3VBB LEU F 515 UNP P49591 EXPRESSION TAG
SEQADV 3VBB GLU F 516 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS F 517 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS F 518 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS F 519 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS F 520 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS F 521 UNP P49591 EXPRESSION TAG
SEQADV 3VBB HIS F 522 UNP P49591 EXPRESSION TAG
SEQRES 1 A 522 MET VAL LEU ASP LEU ASP LEU PHE ARG VAL ASP LYS GLY
SEQRES 2 A 522 GLY ASP PRO ALA LEU ILE ARG GLU THR GLN GLU LYS ARG
SEQRES 3 A 522 PHE LYS ASP PRO GLY LEU VAL ASP GLN LEU VAL LYS ALA
SEQRES 4 A 522 ASP SER GLU TRP ARG ARG CYS ARG PHE ARG ALA ASP ASN
SEQRES 5 A 522 LEU ASN LYS LEU LYS ASN LEU CYS SER LYS THR ILE GLY
SEQRES 6 A 522 GLU LYS MET LYS LYS LYS GLU PRO VAL GLY ASP ASP GLU
SEQRES 7 A 522 SER VAL PRO GLU ASN VAL LEU SER PHE ASP ASP LEU THR
SEQRES 8 A 522 ALA ASP ALA LEU ALA ASN LEU LYS VAL SER GLN ILE LYS
SEQRES 9 A 522 LYS VAL ARG LEU LEU ILE ASP GLU ALA ILE LEU LYS CYS
SEQRES 10 A 522 ASP ALA GLU ARG ILE LYS LEU GLU ALA GLU ARG PHE GLU
SEQRES 11 A 522 ASN LEU ARG GLU ILE GLY ASN LEU LEU HIS PRO SER VAL
SEQRES 12 A 522 PRO ILE SER ASN ASP GLU ASP VAL ASP ASN LYS VAL GLU
SEQRES 13 A 522 ARG ILE TRP GLY ASP CYS THR VAL ARG LYS LYS TYR SER
SEQRES 14 A 522 HIS VAL ASP LEU VAL VAL MET VAL ASP GLY PHE GLU GLY
SEQRES 15 A 522 GLU LYS GLY ALA VAL VAL ALA GLY SER ARG GLY TYR PHE
SEQRES 16 A 522 LEU LYS GLY VAL LEU VAL PHE LEU GLU GLN ALA LEU ILE
SEQRES 17 A 522 GLN TYR ALA LEU ARG THR LEU GLY SER ARG GLY TYR ILE
SEQRES 18 A 522 PRO ILE TYR THR PRO PHE PHE MET ARG LYS GLU VAL MET
SEQRES 19 A 522 GLN GLU VAL ALA GLN LEU SER GLN PHE ASP GLU GLU LEU
SEQRES 20 A 522 TYR LYS VAL ILE GLY LYS GLY SER GLU LYS SER ASP ASP
SEQRES 21 A 522 ASN SER TYR ASP GLU LYS TYR LEU ILE ALA THR SER GLU
SEQRES 22 A 522 GLN PRO ILE ALA ALA LEU HIS ARG ASP GLU TRP LEU ARG
SEQRES 23 A 522 PRO GLU ASP LEU PRO ILE LYS TYR ALA GLY LEU SER THR
SEQRES 24 A 522 CYS PHE ARG GLN GLU VAL GLY SER HIS GLY ARG ASP THR
SEQRES 25 A 522 ARG GLY ILE PHE ARG VAL HIS GLN PHE GLU LYS ILE GLU
SEQRES 26 A 522 GLN PHE VAL TYR SER SER PRO HIS ASP ASN LYS SER TRP
SEQRES 27 A 522 GLU MET PHE GLU GLU MET ILE THR THR ALA GLU GLU PHE
SEQRES 28 A 522 TYR GLN SER LEU GLY ILE PRO TYR HIS ILE VAL ASN ILE
SEQRES 29 A 522 VAL SER GLY SER LEU ASN HIS ALA ALA SER LYS LYS LEU
SEQRES 30 A 522 ASP LEU GLU ALA TRP PHE PRO GLY SER GLY ALA PHE ARG
SEQRES 31 A 522 GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN ALA
SEQRES 32 A 522 ARG ARG LEU ARG ILE ARG TYR GLY GLN THR LYS LYS MET
SEQRES 33 A 522 MET ASP LYS VAL GLU PHE VAL HIS MET LEU ASN ALA THR
SEQRES 34 A 522 MET CYS ALA THR THR ARG THR ILE CYS ALA ILE LEU GLU
SEQRES 35 A 522 ASN TYR GLN THR GLU LYS GLY ILE THR VAL PRO GLU LYS
SEQRES 36 A 522 LEU LYS GLU PHE MET PRO PRO GLY LEU GLN GLU LEU ILE
SEQRES 37 A 522 PRO PHE VAL LYS PRO ALA PRO ILE GLU GLN GLU PRO SER
SEQRES 38 A 522 LYS LYS GLN LYS LYS GLN HIS GLU GLY SER LYS LYS LYS
SEQRES 39 A 522 ALA ALA ALA ARG ASP VAL THR LEU GLU ASN ARG LEU GLN
SEQRES 40 A 522 ASN MET GLU VAL THR ASP ALA LEU GLU HIS HIS HIS HIS
SEQRES 41 A 522 HIS HIS
SEQRES 1 B 522 MET VAL LEU ASP LEU ASP LEU PHE ARG VAL ASP LYS GLY
SEQRES 2 B 522 GLY ASP PRO ALA LEU ILE ARG GLU THR GLN GLU LYS ARG
SEQRES 3 B 522 PHE LYS ASP PRO GLY LEU VAL ASP GLN LEU VAL LYS ALA
SEQRES 4 B 522 ASP SER GLU TRP ARG ARG CYS ARG PHE ARG ALA ASP ASN
SEQRES 5 B 522 LEU ASN LYS LEU LYS ASN LEU CYS SER LYS THR ILE GLY
SEQRES 6 B 522 GLU LYS MET LYS LYS LYS GLU PRO VAL GLY ASP ASP GLU
SEQRES 7 B 522 SER VAL PRO GLU ASN VAL LEU SER PHE ASP ASP LEU THR
SEQRES 8 B 522 ALA ASP ALA LEU ALA ASN LEU LYS VAL SER GLN ILE LYS
SEQRES 9 B 522 LYS VAL ARG LEU LEU ILE ASP GLU ALA ILE LEU LYS CYS
SEQRES 10 B 522 ASP ALA GLU ARG ILE LYS LEU GLU ALA GLU ARG PHE GLU
SEQRES 11 B 522 ASN LEU ARG GLU ILE GLY ASN LEU LEU HIS PRO SER VAL
SEQRES 12 B 522 PRO ILE SER ASN ASP GLU ASP VAL ASP ASN LYS VAL GLU
SEQRES 13 B 522 ARG ILE TRP GLY ASP CYS THR VAL ARG LYS LYS TYR SER
SEQRES 14 B 522 HIS VAL ASP LEU VAL VAL MET VAL ASP GLY PHE GLU GLY
SEQRES 15 B 522 GLU LYS GLY ALA VAL VAL ALA GLY SER ARG GLY TYR PHE
SEQRES 16 B 522 LEU LYS GLY VAL LEU VAL PHE LEU GLU GLN ALA LEU ILE
SEQRES 17 B 522 GLN TYR ALA LEU ARG THR LEU GLY SER ARG GLY TYR ILE
SEQRES 18 B 522 PRO ILE TYR THR PRO PHE PHE MET ARG LYS GLU VAL MET
SEQRES 19 B 522 GLN GLU VAL ALA GLN LEU SER GLN PHE ASP GLU GLU LEU
SEQRES 20 B 522 TYR LYS VAL ILE GLY LYS GLY SER GLU LYS SER ASP ASP
SEQRES 21 B 522 ASN SER TYR ASP GLU LYS TYR LEU ILE ALA THR SER GLU
SEQRES 22 B 522 GLN PRO ILE ALA ALA LEU HIS ARG ASP GLU TRP LEU ARG
SEQRES 23 B 522 PRO GLU ASP LEU PRO ILE LYS TYR ALA GLY LEU SER THR
SEQRES 24 B 522 CYS PHE ARG GLN GLU VAL GLY SER HIS GLY ARG ASP THR
SEQRES 25 B 522 ARG GLY ILE PHE ARG VAL HIS GLN PHE GLU LYS ILE GLU
SEQRES 26 B 522 GLN PHE VAL TYR SER SER PRO HIS ASP ASN LYS SER TRP
SEQRES 27 B 522 GLU MET PHE GLU GLU MET ILE THR THR ALA GLU GLU PHE
SEQRES 28 B 522 TYR GLN SER LEU GLY ILE PRO TYR HIS ILE VAL ASN ILE
SEQRES 29 B 522 VAL SER GLY SER LEU ASN HIS ALA ALA SER LYS LYS LEU
SEQRES 30 B 522 ASP LEU GLU ALA TRP PHE PRO GLY SER GLY ALA PHE ARG
SEQRES 31 B 522 GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN ALA
SEQRES 32 B 522 ARG ARG LEU ARG ILE ARG TYR GLY GLN THR LYS LYS MET
SEQRES 33 B 522 MET ASP LYS VAL GLU PHE VAL HIS MET LEU ASN ALA THR
SEQRES 34 B 522 MET CYS ALA THR THR ARG THR ILE CYS ALA ILE LEU GLU
SEQRES 35 B 522 ASN TYR GLN THR GLU LYS GLY ILE THR VAL PRO GLU LYS
SEQRES 36 B 522 LEU LYS GLU PHE MET PRO PRO GLY LEU GLN GLU LEU ILE
SEQRES 37 B 522 PRO PHE VAL LYS PRO ALA PRO ILE GLU GLN GLU PRO SER
SEQRES 38 B 522 LYS LYS GLN LYS LYS GLN HIS GLU GLY SER LYS LYS LYS
SEQRES 39 B 522 ALA ALA ALA ARG ASP VAL THR LEU GLU ASN ARG LEU GLN
SEQRES 40 B 522 ASN MET GLU VAL THR ASP ALA LEU GLU HIS HIS HIS HIS
SEQRES 41 B 522 HIS HIS
SEQRES 1 C 522 MET VAL LEU ASP LEU ASP LEU PHE ARG VAL ASP LYS GLY
SEQRES 2 C 522 GLY ASP PRO ALA LEU ILE ARG GLU THR GLN GLU LYS ARG
SEQRES 3 C 522 PHE LYS ASP PRO GLY LEU VAL ASP GLN LEU VAL LYS ALA
SEQRES 4 C 522 ASP SER GLU TRP ARG ARG CYS ARG PHE ARG ALA ASP ASN
SEQRES 5 C 522 LEU ASN LYS LEU LYS ASN LEU CYS SER LYS THR ILE GLY
SEQRES 6 C 522 GLU LYS MET LYS LYS LYS GLU PRO VAL GLY ASP ASP GLU
SEQRES 7 C 522 SER VAL PRO GLU ASN VAL LEU SER PHE ASP ASP LEU THR
SEQRES 8 C 522 ALA ASP ALA LEU ALA ASN LEU LYS VAL SER GLN ILE LYS
SEQRES 9 C 522 LYS VAL ARG LEU LEU ILE ASP GLU ALA ILE LEU LYS CYS
SEQRES 10 C 522 ASP ALA GLU ARG ILE LYS LEU GLU ALA GLU ARG PHE GLU
SEQRES 11 C 522 ASN LEU ARG GLU ILE GLY ASN LEU LEU HIS PRO SER VAL
SEQRES 12 C 522 PRO ILE SER ASN ASP GLU ASP VAL ASP ASN LYS VAL GLU
SEQRES 13 C 522 ARG ILE TRP GLY ASP CYS THR VAL ARG LYS LYS TYR SER
SEQRES 14 C 522 HIS VAL ASP LEU VAL VAL MET VAL ASP GLY PHE GLU GLY
SEQRES 15 C 522 GLU LYS GLY ALA VAL VAL ALA GLY SER ARG GLY TYR PHE
SEQRES 16 C 522 LEU LYS GLY VAL LEU VAL PHE LEU GLU GLN ALA LEU ILE
SEQRES 17 C 522 GLN TYR ALA LEU ARG THR LEU GLY SER ARG GLY TYR ILE
SEQRES 18 C 522 PRO ILE TYR THR PRO PHE PHE MET ARG LYS GLU VAL MET
SEQRES 19 C 522 GLN GLU VAL ALA GLN LEU SER GLN PHE ASP GLU GLU LEU
SEQRES 20 C 522 TYR LYS VAL ILE GLY LYS GLY SER GLU LYS SER ASP ASP
SEQRES 21 C 522 ASN SER TYR ASP GLU LYS TYR LEU ILE ALA THR SER GLU
SEQRES 22 C 522 GLN PRO ILE ALA ALA LEU HIS ARG ASP GLU TRP LEU ARG
SEQRES 23 C 522 PRO GLU ASP LEU PRO ILE LYS TYR ALA GLY LEU SER THR
SEQRES 24 C 522 CYS PHE ARG GLN GLU VAL GLY SER HIS GLY ARG ASP THR
SEQRES 25 C 522 ARG GLY ILE PHE ARG VAL HIS GLN PHE GLU LYS ILE GLU
SEQRES 26 C 522 GLN PHE VAL TYR SER SER PRO HIS ASP ASN LYS SER TRP
SEQRES 27 C 522 GLU MET PHE GLU GLU MET ILE THR THR ALA GLU GLU PHE
SEQRES 28 C 522 TYR GLN SER LEU GLY ILE PRO TYR HIS ILE VAL ASN ILE
SEQRES 29 C 522 VAL SER GLY SER LEU ASN HIS ALA ALA SER LYS LYS LEU
SEQRES 30 C 522 ASP LEU GLU ALA TRP PHE PRO GLY SER GLY ALA PHE ARG
SEQRES 31 C 522 GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN ALA
SEQRES 32 C 522 ARG ARG LEU ARG ILE ARG TYR GLY GLN THR LYS LYS MET
SEQRES 33 C 522 MET ASP LYS VAL GLU PHE VAL HIS MET LEU ASN ALA THR
SEQRES 34 C 522 MET CYS ALA THR THR ARG THR ILE CYS ALA ILE LEU GLU
SEQRES 35 C 522 ASN TYR GLN THR GLU LYS GLY ILE THR VAL PRO GLU LYS
SEQRES 36 C 522 LEU LYS GLU PHE MET PRO PRO GLY LEU GLN GLU LEU ILE
SEQRES 37 C 522 PRO PHE VAL LYS PRO ALA PRO ILE GLU GLN GLU PRO SER
SEQRES 38 C 522 LYS LYS GLN LYS LYS GLN HIS GLU GLY SER LYS LYS LYS
SEQRES 39 C 522 ALA ALA ALA ARG ASP VAL THR LEU GLU ASN ARG LEU GLN
SEQRES 40 C 522 ASN MET GLU VAL THR ASP ALA LEU GLU HIS HIS HIS HIS
SEQRES 41 C 522 HIS HIS
SEQRES 1 D 522 MET VAL LEU ASP LEU ASP LEU PHE ARG VAL ASP LYS GLY
SEQRES 2 D 522 GLY ASP PRO ALA LEU ILE ARG GLU THR GLN GLU LYS ARG
SEQRES 3 D 522 PHE LYS ASP PRO GLY LEU VAL ASP GLN LEU VAL LYS ALA
SEQRES 4 D 522 ASP SER GLU TRP ARG ARG CYS ARG PHE ARG ALA ASP ASN
SEQRES 5 D 522 LEU ASN LYS LEU LYS ASN LEU CYS SER LYS THR ILE GLY
SEQRES 6 D 522 GLU LYS MET LYS LYS LYS GLU PRO VAL GLY ASP ASP GLU
SEQRES 7 D 522 SER VAL PRO GLU ASN VAL LEU SER PHE ASP ASP LEU THR
SEQRES 8 D 522 ALA ASP ALA LEU ALA ASN LEU LYS VAL SER GLN ILE LYS
SEQRES 9 D 522 LYS VAL ARG LEU LEU ILE ASP GLU ALA ILE LEU LYS CYS
SEQRES 10 D 522 ASP ALA GLU ARG ILE LYS LEU GLU ALA GLU ARG PHE GLU
SEQRES 11 D 522 ASN LEU ARG GLU ILE GLY ASN LEU LEU HIS PRO SER VAL
SEQRES 12 D 522 PRO ILE SER ASN ASP GLU ASP VAL ASP ASN LYS VAL GLU
SEQRES 13 D 522 ARG ILE TRP GLY ASP CYS THR VAL ARG LYS LYS TYR SER
SEQRES 14 D 522 HIS VAL ASP LEU VAL VAL MET VAL ASP GLY PHE GLU GLY
SEQRES 15 D 522 GLU LYS GLY ALA VAL VAL ALA GLY SER ARG GLY TYR PHE
SEQRES 16 D 522 LEU LYS GLY VAL LEU VAL PHE LEU GLU GLN ALA LEU ILE
SEQRES 17 D 522 GLN TYR ALA LEU ARG THR LEU GLY SER ARG GLY TYR ILE
SEQRES 18 D 522 PRO ILE TYR THR PRO PHE PHE MET ARG LYS GLU VAL MET
SEQRES 19 D 522 GLN GLU VAL ALA GLN LEU SER GLN PHE ASP GLU GLU LEU
SEQRES 20 D 522 TYR LYS VAL ILE GLY LYS GLY SER GLU LYS SER ASP ASP
SEQRES 21 D 522 ASN SER TYR ASP GLU LYS TYR LEU ILE ALA THR SER GLU
SEQRES 22 D 522 GLN PRO ILE ALA ALA LEU HIS ARG ASP GLU TRP LEU ARG
SEQRES 23 D 522 PRO GLU ASP LEU PRO ILE LYS TYR ALA GLY LEU SER THR
SEQRES 24 D 522 CYS PHE ARG GLN GLU VAL GLY SER HIS GLY ARG ASP THR
SEQRES 25 D 522 ARG GLY ILE PHE ARG VAL HIS GLN PHE GLU LYS ILE GLU
SEQRES 26 D 522 GLN PHE VAL TYR SER SER PRO HIS ASP ASN LYS SER TRP
SEQRES 27 D 522 GLU MET PHE GLU GLU MET ILE THR THR ALA GLU GLU PHE
SEQRES 28 D 522 TYR GLN SER LEU GLY ILE PRO TYR HIS ILE VAL ASN ILE
SEQRES 29 D 522 VAL SER GLY SER LEU ASN HIS ALA ALA SER LYS LYS LEU
SEQRES 30 D 522 ASP LEU GLU ALA TRP PHE PRO GLY SER GLY ALA PHE ARG
SEQRES 31 D 522 GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN ALA
SEQRES 32 D 522 ARG ARG LEU ARG ILE ARG TYR GLY GLN THR LYS LYS MET
SEQRES 33 D 522 MET ASP LYS VAL GLU PHE VAL HIS MET LEU ASN ALA THR
SEQRES 34 D 522 MET CYS ALA THR THR ARG THR ILE CYS ALA ILE LEU GLU
SEQRES 35 D 522 ASN TYR GLN THR GLU LYS GLY ILE THR VAL PRO GLU LYS
SEQRES 36 D 522 LEU LYS GLU PHE MET PRO PRO GLY LEU GLN GLU LEU ILE
SEQRES 37 D 522 PRO PHE VAL LYS PRO ALA PRO ILE GLU GLN GLU PRO SER
SEQRES 38 D 522 LYS LYS GLN LYS LYS GLN HIS GLU GLY SER LYS LYS LYS
SEQRES 39 D 522 ALA ALA ALA ARG ASP VAL THR LEU GLU ASN ARG LEU GLN
SEQRES 40 D 522 ASN MET GLU VAL THR ASP ALA LEU GLU HIS HIS HIS HIS
SEQRES 41 D 522 HIS HIS
SEQRES 1 E 522 MET VAL LEU ASP LEU ASP LEU PHE ARG VAL ASP LYS GLY
SEQRES 2 E 522 GLY ASP PRO ALA LEU ILE ARG GLU THR GLN GLU LYS ARG
SEQRES 3 E 522 PHE LYS ASP PRO GLY LEU VAL ASP GLN LEU VAL LYS ALA
SEQRES 4 E 522 ASP SER GLU TRP ARG ARG CYS ARG PHE ARG ALA ASP ASN
SEQRES 5 E 522 LEU ASN LYS LEU LYS ASN LEU CYS SER LYS THR ILE GLY
SEQRES 6 E 522 GLU LYS MET LYS LYS LYS GLU PRO VAL GLY ASP ASP GLU
SEQRES 7 E 522 SER VAL PRO GLU ASN VAL LEU SER PHE ASP ASP LEU THR
SEQRES 8 E 522 ALA ASP ALA LEU ALA ASN LEU LYS VAL SER GLN ILE LYS
SEQRES 9 E 522 LYS VAL ARG LEU LEU ILE ASP GLU ALA ILE LEU LYS CYS
SEQRES 10 E 522 ASP ALA GLU ARG ILE LYS LEU GLU ALA GLU ARG PHE GLU
SEQRES 11 E 522 ASN LEU ARG GLU ILE GLY ASN LEU LEU HIS PRO SER VAL
SEQRES 12 E 522 PRO ILE SER ASN ASP GLU ASP VAL ASP ASN LYS VAL GLU
SEQRES 13 E 522 ARG ILE TRP GLY ASP CYS THR VAL ARG LYS LYS TYR SER
SEQRES 14 E 522 HIS VAL ASP LEU VAL VAL MET VAL ASP GLY PHE GLU GLY
SEQRES 15 E 522 GLU LYS GLY ALA VAL VAL ALA GLY SER ARG GLY TYR PHE
SEQRES 16 E 522 LEU LYS GLY VAL LEU VAL PHE LEU GLU GLN ALA LEU ILE
SEQRES 17 E 522 GLN TYR ALA LEU ARG THR LEU GLY SER ARG GLY TYR ILE
SEQRES 18 E 522 PRO ILE TYR THR PRO PHE PHE MET ARG LYS GLU VAL MET
SEQRES 19 E 522 GLN GLU VAL ALA GLN LEU SER GLN PHE ASP GLU GLU LEU
SEQRES 20 E 522 TYR LYS VAL ILE GLY LYS GLY SER GLU LYS SER ASP ASP
SEQRES 21 E 522 ASN SER TYR ASP GLU LYS TYR LEU ILE ALA THR SER GLU
SEQRES 22 E 522 GLN PRO ILE ALA ALA LEU HIS ARG ASP GLU TRP LEU ARG
SEQRES 23 E 522 PRO GLU ASP LEU PRO ILE LYS TYR ALA GLY LEU SER THR
SEQRES 24 E 522 CYS PHE ARG GLN GLU VAL GLY SER HIS GLY ARG ASP THR
SEQRES 25 E 522 ARG GLY ILE PHE ARG VAL HIS GLN PHE GLU LYS ILE GLU
SEQRES 26 E 522 GLN PHE VAL TYR SER SER PRO HIS ASP ASN LYS SER TRP
SEQRES 27 E 522 GLU MET PHE GLU GLU MET ILE THR THR ALA GLU GLU PHE
SEQRES 28 E 522 TYR GLN SER LEU GLY ILE PRO TYR HIS ILE VAL ASN ILE
SEQRES 29 E 522 VAL SER GLY SER LEU ASN HIS ALA ALA SER LYS LYS LEU
SEQRES 30 E 522 ASP LEU GLU ALA TRP PHE PRO GLY SER GLY ALA PHE ARG
SEQRES 31 E 522 GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN ALA
SEQRES 32 E 522 ARG ARG LEU ARG ILE ARG TYR GLY GLN THR LYS LYS MET
SEQRES 33 E 522 MET ASP LYS VAL GLU PHE VAL HIS MET LEU ASN ALA THR
SEQRES 34 E 522 MET CYS ALA THR THR ARG THR ILE CYS ALA ILE LEU GLU
SEQRES 35 E 522 ASN TYR GLN THR GLU LYS GLY ILE THR VAL PRO GLU LYS
SEQRES 36 E 522 LEU LYS GLU PHE MET PRO PRO GLY LEU GLN GLU LEU ILE
SEQRES 37 E 522 PRO PHE VAL LYS PRO ALA PRO ILE GLU GLN GLU PRO SER
SEQRES 38 E 522 LYS LYS GLN LYS LYS GLN HIS GLU GLY SER LYS LYS LYS
SEQRES 39 E 522 ALA ALA ALA ARG ASP VAL THR LEU GLU ASN ARG LEU GLN
SEQRES 40 E 522 ASN MET GLU VAL THR ASP ALA LEU GLU HIS HIS HIS HIS
SEQRES 41 E 522 HIS HIS
SEQRES 1 F 522 MET VAL LEU ASP LEU ASP LEU PHE ARG VAL ASP LYS GLY
SEQRES 2 F 522 GLY ASP PRO ALA LEU ILE ARG GLU THR GLN GLU LYS ARG
SEQRES 3 F 522 PHE LYS ASP PRO GLY LEU VAL ASP GLN LEU VAL LYS ALA
SEQRES 4 F 522 ASP SER GLU TRP ARG ARG CYS ARG PHE ARG ALA ASP ASN
SEQRES 5 F 522 LEU ASN LYS LEU LYS ASN LEU CYS SER LYS THR ILE GLY
SEQRES 6 F 522 GLU LYS MET LYS LYS LYS GLU PRO VAL GLY ASP ASP GLU
SEQRES 7 F 522 SER VAL PRO GLU ASN VAL LEU SER PHE ASP ASP LEU THR
SEQRES 8 F 522 ALA ASP ALA LEU ALA ASN LEU LYS VAL SER GLN ILE LYS
SEQRES 9 F 522 LYS VAL ARG LEU LEU ILE ASP GLU ALA ILE LEU LYS CYS
SEQRES 10 F 522 ASP ALA GLU ARG ILE LYS LEU GLU ALA GLU ARG PHE GLU
SEQRES 11 F 522 ASN LEU ARG GLU ILE GLY ASN LEU LEU HIS PRO SER VAL
SEQRES 12 F 522 PRO ILE SER ASN ASP GLU ASP VAL ASP ASN LYS VAL GLU
SEQRES 13 F 522 ARG ILE TRP GLY ASP CYS THR VAL ARG LYS LYS TYR SER
SEQRES 14 F 522 HIS VAL ASP LEU VAL VAL MET VAL ASP GLY PHE GLU GLY
SEQRES 15 F 522 GLU LYS GLY ALA VAL VAL ALA GLY SER ARG GLY TYR PHE
SEQRES 16 F 522 LEU LYS GLY VAL LEU VAL PHE LEU GLU GLN ALA LEU ILE
SEQRES 17 F 522 GLN TYR ALA LEU ARG THR LEU GLY SER ARG GLY TYR ILE
SEQRES 18 F 522 PRO ILE TYR THR PRO PHE PHE MET ARG LYS GLU VAL MET
SEQRES 19 F 522 GLN GLU VAL ALA GLN LEU SER GLN PHE ASP GLU GLU LEU
SEQRES 20 F 522 TYR LYS VAL ILE GLY LYS GLY SER GLU LYS SER ASP ASP
SEQRES 21 F 522 ASN SER TYR ASP GLU LYS TYR LEU ILE ALA THR SER GLU
SEQRES 22 F 522 GLN PRO ILE ALA ALA LEU HIS ARG ASP GLU TRP LEU ARG
SEQRES 23 F 522 PRO GLU ASP LEU PRO ILE LYS TYR ALA GLY LEU SER THR
SEQRES 24 F 522 CYS PHE ARG GLN GLU VAL GLY SER HIS GLY ARG ASP THR
SEQRES 25 F 522 ARG GLY ILE PHE ARG VAL HIS GLN PHE GLU LYS ILE GLU
SEQRES 26 F 522 GLN PHE VAL TYR SER SER PRO HIS ASP ASN LYS SER TRP
SEQRES 27 F 522 GLU MET PHE GLU GLU MET ILE THR THR ALA GLU GLU PHE
SEQRES 28 F 522 TYR GLN SER LEU GLY ILE PRO TYR HIS ILE VAL ASN ILE
SEQRES 29 F 522 VAL SER GLY SER LEU ASN HIS ALA ALA SER LYS LYS LEU
SEQRES 30 F 522 ASP LEU GLU ALA TRP PHE PRO GLY SER GLY ALA PHE ARG
SEQRES 31 F 522 GLU LEU VAL SER CYS SER ASN CYS THR ASP TYR GLN ALA
SEQRES 32 F 522 ARG ARG LEU ARG ILE ARG TYR GLY GLN THR LYS LYS MET
SEQRES 33 F 522 MET ASP LYS VAL GLU PHE VAL HIS MET LEU ASN ALA THR
SEQRES 34 F 522 MET CYS ALA THR THR ARG THR ILE CYS ALA ILE LEU GLU
SEQRES 35 F 522 ASN TYR GLN THR GLU LYS GLY ILE THR VAL PRO GLU LYS
SEQRES 36 F 522 LEU LYS GLU PHE MET PRO PRO GLY LEU GLN GLU LEU ILE
SEQRES 37 F 522 PRO PHE VAL LYS PRO ALA PRO ILE GLU GLN GLU PRO SER
SEQRES 38 F 522 LYS LYS GLN LYS LYS GLN HIS GLU GLY SER LYS LYS LYS
SEQRES 39 F 522 ALA ALA ALA ARG ASP VAL THR LEU GLU ASN ARG LEU GLN
SEQRES 40 F 522 ASN MET GLU VAL THR ASP ALA LEU GLU HIS HIS HIS HIS
SEQRES 41 F 522 HIS HIS
HET MG A 601 1
HET PO4 A 602 5
HET MG B 601 1
HET PO4 B 602 5
HET PO4 C 601 5
HET PO4 D 601 5
HET PO4 E 601 5
HET PO4 F 601 5
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 7 MG 2(MG 2+)
FORMUL 8 PO4 6(O4 P 3-)
FORMUL 15 HOH *15(H2 O)
HELIX 1 1 ASP A 4 PHE A 8 5 5
HELIX 2 2 ARG A 9 GLY A 13 5 5
HELIX 3 3 ASP A 15 ARG A 26 1 12
HELIX 4 4 PRO A 30 LYS A 71 1 42
HELIX 5 5 PRO A 81 LEU A 85 5 5
HELIX 6 6 THR A 91 ASN A 97 1 7
HELIX 7 7 GLN A 102 ALA A 113 1 12
HELIX 8 8 CYS A 117 LEU A 132 1 16
HELIX 9 9 ARG A 133 ILE A 135 5 3
HELIX 10 10 ASP A 148 ASN A 153 1 6
HELIX 11 11 SER A 169 VAL A 177 1 9
HELIX 12 12 GLY A 182 GLY A 190 1 9
HELIX 13 13 GLY A 198 ARG A 218 1 21
HELIX 14 14 LYS A 231 ALA A 238 1 8
HELIX 15 15 SER A 272 ALA A 278 1 7
HELIX 16 16 ASN A 335 LEU A 355 1 21
HELIX 17 17 VAL A 365 LEU A 369 5 5
HELIX 18 18 ASP A 400 ARG A 407 1 8
HELIX 19 19 THR A 433 GLN A 445 1 13
HELIX 20 20 PRO A 453 GLU A 458 1 6
HELIX 21 21 ASP B 4 GLY B 13 5 10
HELIX 22 22 ASP B 15 ARG B 26 1 12
HELIX 23 23 PRO B 30 MET B 68 1 39
HELIX 24 24 THR B 91 ASN B 97 1 7
HELIX 25 25 LYS B 99 ARG B 133 1 35
HELIX 26 26 ASP B 148 ASN B 153 1 6
HELIX 27 27 SER B 169 VAL B 177 1 9
HELIX 28 28 GLY B 182 GLY B 190 1 9
HELIX 29 29 GLY B 198 ARG B 218 1 21
HELIX 30 30 LYS B 231 ALA B 238 1 8
HELIX 31 31 SER B 241 GLU B 246 1 6
HELIX 32 32 SER B 272 ALA B 278 1 7
HELIX 33 33 ARG B 286 LEU B 290 5 5
HELIX 34 34 ASN B 335 LEU B 355 1 21
HELIX 35 35 VAL B 365 LEU B 369 5 5
HELIX 36 36 ASP B 400 LEU B 406 1 7
HELIX 37 37 THR B 433 GLN B 445 1 13
HELIX 38 38 PRO B 453 MET B 460 5 8
HELIX 39 39 ASP C 4 GLY C 13 5 10
HELIX 40 40 ASP C 15 ARG C 26 1 12
HELIX 41 41 PRO C 30 LYS C 70 1 41
HELIX 42 42 PRO C 81 LEU C 85 5 5
HELIX 43 43 ALA C 92 ALA C 96 5 5
HELIX 44 44 GLN C 102 ILE C 114 1 13
HELIX 45 45 CYS C 117 LEU C 132 1 16
HELIX 46 46 ARG C 133 ILE C 135 5 3
HELIX 47 47 SER C 169 VAL C 177 1 9
HELIX 48 48 GLY C 182 GLY C 190 1 9
HELIX 49 49 GLY C 198 SER C 217 1 20
HELIX 50 50 LYS C 231 ALA C 238 1 8
HELIX 51 51 SER C 272 ARG C 281 1 10
HELIX 52 52 ASN C 335 LEU C 355 1 21
HELIX 53 53 VAL C 365 LEU C 369 5 5
HELIX 54 54 THR C 399 LEU C 406 1 8
HELIX 55 55 THR C 433 GLN C 445 1 13
HELIX 56 56 PRO C 453 GLU C 458 1 6
HELIX 57 57 ARG D 9 GLY D 13 5 5
HELIX 58 58 ASP D 15 ARG D 26 1 12
HELIX 59 59 PRO D 30 MET D 68 1 39
HELIX 60 60 THR D 91 ALA D 96 1 6
HELIX 61 61 LYS D 99 ARG D 133 1 35
HELIX 62 62 ASP D 148 ASN D 153 1 6
HELIX 63 63 SER D 169 VAL D 177 1 9
HELIX 64 64 GLY D 182 GLY D 190 1 9
HELIX 65 65 GLY D 198 ARG D 218 1 21
HELIX 66 66 LYS D 231 GLN D 235 1 5
HELIX 67 67 SER D 272 ARG D 281 1 10
HELIX 68 68 ARG D 286 LEU D 290 5 5
HELIX 69 69 ASN D 335 LEU D 355 1 21
HELIX 70 70 VAL D 365 LEU D 369 5 5
HELIX 71 71 THR D 399 ARG D 407 1 9
HELIX 72 72 THR D 433 GLN D 445 1 13
HELIX 73 73 PRO D 453 GLU D 458 1 6
HELIX 74 74 ASP E 4 GLY E 13 5 10
HELIX 75 75 ASP E 15 ARG E 26 1 12
HELIX 76 76 PRO E 30 THR E 63 1 34
HELIX 77 77 THR E 91 ASN E 97 1 7
HELIX 78 78 LYS E 99 GLU E 134 1 36
HELIX 79 79 ASP E 148 ASN E 153 1 6
HELIX 80 80 SER E 169 VAL E 177 1 9
HELIX 81 81 GLY E 182 GLY E 190 1 9
HELIX 82 82 GLY E 198 SER E 217 1 20
HELIX 83 83 LYS E 231 ALA E 238 1 8
HELIX 84 84 SER E 272 ARG E 281 1 10
HELIX 85 85 ASN E 335 LEU E 355 1 21
HELIX 86 86 VAL E 365 LEU E 369 5 5
HELIX 87 87 ASP E 400 LEU E 406 1 7
HELIX 88 88 THR E 433 TYR E 444 1 12
HELIX 89 89 PRO E 453 GLU E 458 1 6
HELIX 90 90 PRO E 461 GLN E 465 5 5
HELIX 91 91 ASP F 4 GLY F 13 5 10
HELIX 92 92 ASP F 15 ARG F 26 1 12
HELIX 93 93 PRO F 30 MET F 68 1 39
HELIX 94 94 SER F 101 ARG F 133 1 33
HELIX 95 95 GLU F 149 ASN F 153 5 5
HELIX 96 96 SER F 169 VAL F 177 1 9
HELIX 97 97 LYS F 184 GLY F 190 1 7
HELIX 98 98 GLY F 198 ARG F 218 1 21
HELIX 99 99 LYS F 231 VAL F 237 1 7
HELIX 100 100 SER F 272 ARG F 281 1 10
HELIX 101 101 ASN F 335 LEU F 355 1 21
HELIX 102 102 VAL F 365 LEU F 369 5 5
HELIX 103 103 ASP F 400 LEU F 406 1 7
HELIX 104 104 THR F 433 GLN F 445 1 13
HELIX 105 105 PRO F 453 GLU F 458 1 6
SHEET 1 A10 LYS A 154 TRP A 159 0
SHEET 2 A10 TYR A 359 ASN A 363 -1 O ASN A 363 N LYS A 154
SHEET 3 A10 LYS A 375 PHE A 383 -1 O ASP A 378 N VAL A 362
SHEET 4 A10 ALA A 388 ASN A 397 -1 O ALA A 388 N PHE A 383
SHEET 5 A10 HIS A 424 ALA A 432 -1 O ASN A 427 N SER A 396
SHEET 6 A10 GLN A 320 SER A 330 -1 N GLN A 326 O ALA A 428
SHEET 7 A10 ILE A 292 PHE A 301 -1 N CYS A 300 O PHE A 321
SHEET 8 A10 ILE A 221 TYR A 224 1 N ILE A 223 O ALA A 295
SHEET 9 A10 PHE B 195 LYS B 197 -1 O LEU B 196 N TYR A 224
SHEET 10 A10 PHE B 180 GLU B 181 -1 N GLU B 181 O PHE B 195
SHEET 1 B10 PHE A 180 GLU A 181 0
SHEET 2 B10 PHE A 195 LYS A 197 -1 O PHE A 195 N GLU A 181
SHEET 3 B10 ILE B 221 TYR B 224 -1 O TYR B 224 N LEU A 196
SHEET 4 B10 ILE B 292 PHE B 301 1 O ALA B 295 N ILE B 223
SHEET 5 B10 GLN B 320 SER B 330 -1 O PHE B 321 N CYS B 300
SHEET 6 B10 HIS B 424 ALA B 432 -1 O ALA B 428 N GLN B 326
SHEET 7 B10 ALA B 388 ASN B 397 -1 N SER B 396 O ASN B 427
SHEET 8 B10 LYS B 375 PHE B 383 -1 N PHE B 383 O ALA B 388
SHEET 9 B10 TYR B 359 ASN B 363 -1 N VAL B 362 O ASP B 378
SHEET 10 B10 LYS B 154 TRP B 159 -1 N LYS B 154 O ASN B 363
SHEET 1 C 6 PHE A 228 ARG A 230 0
SHEET 2 C 6 LYS A 266 LEU A 268 -1 O TYR A 267 N MET A 229
SHEET 3 C 6 LYS A 249 ILE A 251 -1 N VAL A 250 O LYS A 266
SHEET 4 C 6 TYR B 248 VAL B 250 -1 O LYS B 249 N ILE A 251
SHEET 5 C 6 LYS B 266 LEU B 268 -1 O LYS B 266 N VAL B 250
SHEET 6 C 6 PHE B 228 ARG B 230 -1 N MET B 229 O TYR B 267
SHEET 1 D 2 TRP A 284 LEU A 285 0
SHEET 2 D 2 ARG A 409 TYR A 410 1 O ARG A 409 N LEU A 285
SHEET 1 E 2 GLY A 449 THR A 451 0
SHEET 2 E 2 LEU A 467 PRO A 469 -1 O ILE A 468 N ILE A 450
SHEET 1 F 2 GLU B 283 LEU B 285 0
SHEET 2 F 2 ILE B 408 TYR B 410 1 O ARG B 409 N GLU B 283
SHEET 1 G 2 GLY B 449 THR B 451 0
SHEET 2 G 2 LEU B 467 PRO B 469 -1 O ILE B 468 N ILE B 450
SHEET 1 H10 LYS C 154 TRP C 159 0
SHEET 2 H10 TYR C 359 ASN C 363 -1 O ASN C 363 N LYS C 154
SHEET 3 H10 LYS C 375 PHE C 383 -1 O GLU C 380 N HIS C 360
SHEET 4 H10 ALA C 388 ASN C 397 -1 O CYS C 395 N LEU C 377
SHEET 5 H10 HIS C 424 ALA C 432 -1 O ASN C 427 N SER C 396
SHEET 6 H10 GLN C 320 SER C 330 -1 N ILE C 324 O CYS C 431
SHEET 7 H10 ILE C 292 PHE C 301 -1 N TYR C 294 O PHE C 327
SHEET 8 H10 ILE C 221 TYR C 224 1 N ILE C 221 O LYS C 293
SHEET 9 H10 PHE D 195 LYS D 197 -1 O LEU D 196 N TYR C 224
SHEET 10 H10 PHE D 180 GLU D 181 -1 N GLU D 181 O PHE D 195
SHEET 1 I10 PHE C 180 GLU C 181 0
SHEET 2 I10 PHE C 195 LYS C 197 -1 O PHE C 195 N GLU C 181
SHEET 3 I10 ILE D 221 TYR D 224 -1 O TYR D 224 N LEU C 196
SHEET 4 I10 ILE D 292 PHE D 301 1 O ALA D 295 N ILE D 223
SHEET 5 I10 GLN D 320 SER D 330 -1 O GLU D 325 N GLY D 296
SHEET 6 I10 HIS D 424 ALA D 432 -1 O CYS D 431 N ILE D 324
SHEET 7 I10 ALA D 388 ASN D 397 -1 N SER D 396 O ASN D 427
SHEET 8 I10 LYS D 375 PHE D 383 -1 N ALA D 381 O ARG D 390
SHEET 9 I10 TYR D 359 ASN D 363 -1 N VAL D 362 O ASP D 378
SHEET 10 I10 LYS D 154 TRP D 159 -1 N LYS D 154 O ASN D 363
SHEET 1 J 6 PHE C 228 ARG C 230 0
SHEET 2 J 6 LYS C 266 LEU C 268 -1 O TYR C 267 N MET C 229
SHEET 3 J 6 LYS C 249 VAL C 250 -1 N VAL C 250 O LYS C 266
SHEET 4 J 6 LYS D 249 ILE D 251 -1 O ILE D 251 N LYS C 249
SHEET 5 J 6 LYS D 266 LEU D 268 -1 O LYS D 266 N VAL D 250
SHEET 6 J 6 PHE D 228 ARG D 230 -1 N MET D 229 O TYR D 267
SHEET 1 K 2 TRP C 284 LEU C 285 0
SHEET 2 K 2 ARG C 409 TYR C 410 1 O ARG C 409 N LEU C 285
SHEET 1 L 2 GLY C 449 ILE C 450 0
SHEET 2 L 2 ILE C 468 PRO C 469 -1 O ILE C 468 N ILE C 450
SHEET 1 M 2 TRP D 284 LEU D 285 0
SHEET 2 M 2 ARG D 409 TYR D 410 1 O ARG D 409 N LEU D 285
SHEET 1 N 2 GLY D 449 THR D 451 0
SHEET 2 N 2 LEU D 467 PRO D 469 -1 O ILE D 468 N ILE D 450
SHEET 1 O10 LYS E 154 TRP E 159 0
SHEET 2 O10 TYR E 359 ASN E 363 -1 O ASN E 363 N LYS E 154
SHEET 3 O10 LYS E 375 PHE E 383 -1 O ASP E 378 N VAL E 362
SHEET 4 O10 ALA E 388 ASN E 397 -1 O ALA E 388 N PHE E 383
SHEET 5 O10 HIS E 424 ALA E 432 -1 O ASN E 427 N SER E 396
SHEET 6 O10 GLN E 320 SER E 330 -1 N SER E 330 O HIS E 424
SHEET 7 O10 ILE E 292 PHE E 301 -1 N GLY E 296 O GLU E 325
SHEET 8 O10 ILE E 221 TYR E 224 1 N ILE E 223 O ALA E 295
SHEET 9 O10 PHE F 195 LYS F 197 -1 O LEU F 196 N TYR E 224
SHEET 10 O10 PHE F 180 GLU F 181 -1 N GLU F 181 O PHE F 195
SHEET 1 P10 PHE E 180 GLU E 181 0
SHEET 2 P10 PHE E 195 LYS E 197 -1 O PHE E 195 N GLU E 181
SHEET 3 P10 ILE F 221 TYR F 224 -1 O TYR F 224 N LEU E 196
SHEET 4 P10 ILE F 292 PHE F 301 1 O LYS F 293 N ILE F 221
SHEET 5 P10 GLN F 320 SER F 330 -1 O PHE F 321 N CYS F 300
SHEET 6 P10 HIS F 424 ALA F 432 -1 O ALA F 428 N GLN F 326
SHEET 7 P10 ALA F 388 ASN F 397 -1 N SER F 396 O ASN F 427
SHEET 8 P10 LYS F 375 PHE F 383 -1 N LEU F 377 O CYS F 395
SHEET 9 P10 TYR F 359 ASN F 363 -1 N HIS F 360 O GLU F 380
SHEET 10 P10 LYS F 154 TRP F 159 -1 N LYS F 154 O ASN F 363
SHEET 1 Q 5 GLU E 265 TYR E 267 0
SHEET 2 Q 5 LYS E 249 ILE E 251 -1 N VAL E 250 O LYS E 266
SHEET 3 Q 5 TYR F 248 VAL F 250 -1 O LYS F 249 N ILE E 251
SHEET 4 Q 5 LYS F 266 LEU F 268 -1 O LEU F 268 N TYR F 248
SHEET 5 Q 5 PHE F 228 ARG F 230 -1 N MET F 229 O TYR F 267
SHEET 1 R 2 TRP E 284 LEU E 285 0
SHEET 2 R 2 ARG E 409 TYR E 410 1 O ARG E 409 N LEU E 285
SHEET 1 S 2 GLY E 449 THR E 451 0
SHEET 2 S 2 LEU E 467 PRO E 469 -1 O ILE E 468 N ILE E 450
SHEET 1 T 2 GLY F 449 THR F 451 0
SHEET 2 T 2 LEU F 467 PRO F 469 -1 O ILE F 468 N ILE F 450
CISPEP 1 LEU A 290 PRO A 291 0 -6.89
CISPEP 2 LEU B 290 PRO B 291 0 -6.24
CISPEP 3 LEU C 290 PRO C 291 0 1.95
CISPEP 4 LEU D 290 PRO D 291 0 0.38
CISPEP 5 LEU E 290 PRO E 291 0 -3.93
CISPEP 6 LEU F 290 PRO F 291 0 -6.11
SITE 1 AC1 3 ARG A 302 PHE A 316 PHE A 321
SITE 1 AC2 3 THR A 312 GLY A 314 ARG A 317
SITE 1 AC3 1 GLU B 391
SITE 1 AC4 4 ARG B 192 GLY B 309 THR B 312 ARG B 317
SITE 1 AC5 2 THR C 312 ARG C 313
SITE 1 AC6 3 THR D 312 GLY D 314 ARG D 317
SITE 1 AC7 2 ARG E 313 ARG E 317
SITE 1 AC8 2 HIS F 170 ARG F 317
CRYST1 116.800 189.417 230.589 90.00 90.00 90.00 P 21 21 21 24
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 0.008562 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004337 0.00000
(ATOM LINES ARE NOT SHOWN.)
END