HEADER LYASE 05-MAY-09 3HBX
TITLE CRYSTAL STRUCTURE OF GAD1 FROM ARABIDOPSIS THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DECARBOXYLASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: GAD 1;
COMPND 5 EC: 4.1.1.15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT5G17330, GAD, GAD1, GDH1, MKP11.30, MKP11_18;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET12B
KEYWDS CALMODULIN-BINDING, DECARBOXYLASE, LYASE, PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.GUT,P.DOMINICI,S.PILATI,M.G.GRUETTER,G.CAPITANI
REVDAT 6 22-NOV-23 3HBX 1 REMARK
REVDAT 5 06-SEP-23 3HBX 1 LINK
REVDAT 4 01-NOV-17 3HBX 1 REMARK
REVDAT 3 08-DEC-09 3HBX 1 MTRIX1 MTRIX2 MTRIX3
REVDAT 2 15-SEP-09 3HBX 1 JRNL
REVDAT 1 28-JUL-09 3HBX 0
JRNL AUTH H.GUT,P.DOMINICI,S.PILATI,A.ASTEGNO,M.V.PETOUKHOV,
JRNL AUTH 2 D.I.SVERGUN,M.G.GRUTTER,G.CAPITANI
JRNL TITL A COMMON STRUCTURAL BASIS FOR PH- AND CALMODULIN-MEDIATED
JRNL TITL 2 REGULATION IN PLANT GLUTAMATE DECARBOXYLASE.
JRNL REF J.MOL.BIOL. V. 392 334 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19580813
JRNL DOI 10.1016/J.JMB.2009.06.080
REMARK 2
REMARK 2 RESOLUTION. 2.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.4_29
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) : 2.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.510
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 85127
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.610
REMARK 3 FREE R VALUE TEST SET COUNT : 2223
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.0927 - 6.7077 0.91 4897 139 0.1612 0.1714
REMARK 3 2 6.7077 - 5.3348 0.94 5062 148 0.1810 0.2145
REMARK 3 3 5.3348 - 4.6636 0.94 5014 166 0.1674 0.1719
REMARK 3 4 4.6636 - 4.2386 0.95 5057 150 0.1643 0.1775
REMARK 3 5 4.2386 - 3.9356 0.96 5158 167 0.1777 0.1781
REMARK 3 6 3.9356 - 3.7040 0.97 5190 133 0.1794 0.2026
REMARK 3 7 3.7040 - 3.5188 0.97 5262 168 0.1993 0.2307
REMARK 3 8 3.5188 - 3.3659 0.98 5253 130 0.2078 0.2269
REMARK 3 9 3.3659 - 3.2365 0.98 5338 150 0.2226 0.2406
REMARK 3 10 3.2365 - 3.1250 0.98 5246 178 0.2415 0.2577
REMARK 3 11 3.1250 - 3.0273 0.98 5278 144 0.2540 0.2659
REMARK 3 12 3.0273 - 2.9409 0.99 5346 117 0.2655 0.3089
REMARK 3 13 2.9409 - 2.8635 0.98 5350 113 0.2756 0.2683
REMARK 3 14 2.8635 - 2.7937 0.98 5333 97 0.2785 0.3089
REMARK 3 15 2.7937 - 2.7303 0.97 5189 126 0.2870 0.3461
REMARK 3 16 2.7303 - 2.6720 0.91 4931 97 0.3029 0.3526
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 28.07
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.54800
REMARK 3 B22 (A**2) : -8.54800
REMARK 3 B33 (A**2) : 17.09700
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 : 0.002 21624
REMARK 3 ANGLE : 0.606 29356
REMARK 3 CHIRALITY : 0.043 3240
REMARK 3 PLANARITY : 0.002 3788
REMARK 3 DIHEDRAL : 14.335 7978
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 : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND BACKBONE AND RESSEQ 300:314
REMARK 3 SELECTION : CHAIN B AND BACKBONE AND RESSEQ 300:314
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.019
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND BACKBONE AND RESSEQ 300:314
REMARK 3 SELECTION : CHAIN C AND BACKBONE AND RESSEQ 300:314
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.015
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND BACKBONE AND RESSEQ 300:314
REMARK 3 SELECTION : CHAIN D AND BACKBONE AND RESSEQ 300:314
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.012
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND BACKBONE AND RESSEQ 300:314
REMARK 3 SELECTION : CHAIN E AND BACKBONE AND RESSEQ 300:314
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.012
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND BACKBONE AND RESSEQ 300:314
REMARK 3 SELECTION : CHAIN F AND BACKBONE AND RESSEQ 300:314
REMARK 3 ATOM PAIRS NUMBER : 60
REMARK 3 RMSD : 0.017
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 ATOM PAIRS NUMBER : 3202
REMARK 3 RMSD : 0.009
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 ATOM PAIRS NUMBER : 3202
REMARK 3 RMSD : 0.008
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 ATOM PAIRS NUMBER : 3202
REMARK 3 RMSD : 0.008
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 ATOM PAIRS NUMBER : 3202
REMARK 3 RMSD : 0.007
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 12:111 OR RESSEQ
REMARK 3 117:148 OR RESSEQ 150:255 OR RESSEQ 260:
REMARK 3 276 OR RESSEQ 278:299 OR RESSEQ 315:404
REMARK 3 OR RESSEQ 415:447 )
REMARK 3 ATOM PAIRS NUMBER : 3202
REMARK 3 RMSD : 0.009
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-05
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90002
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85232
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 1PMM (E. COLI GADB)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 UL PROTEIN SOLUTION (1.9 MG/ML GAD1,
REMARK 280 50 MM HEPES PH 7.2, 150 MM NACL AND 10 UM PLP) + 1 UL RESERVOIR
REMARK 280 SOLUTION (100 MM NA ACETATE PH 5.5, 720 MM NA FORMATE, 9 % PEG
REMARK 280 8000 AND 9 % PEG 1000), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 133.71733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 66.85867
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 VAL A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 ALA A 6
REMARK 465 VAL A 7
REMARK 465 SER A 8
REMARK 465 GLU A 9
REMARK 465 SER A 10
REMARK 465 ASP A 11
REMARK 465 SER A 449
REMARK 465 ARG A 450
REMARK 465 VAL A 451
REMARK 465 ILE A 452
REMARK 465 HIS A 453
REMARK 465 LYS A 454
REMARK 465 ILE A 455
REMARK 465 SER A 456
REMARK 465 LEU A 457
REMARK 465 GLY A 458
REMARK 465 GLN A 459
REMARK 465 GLU A 460
REMARK 465 LYS A 461
REMARK 465 SER A 462
REMARK 465 GLU A 463
REMARK 465 SER A 464
REMARK 465 ASN A 465
REMARK 465 SER A 466
REMARK 465 ASP A 467
REMARK 465 ASN A 468
REMARK 465 LEU A 469
REMARK 465 MET A 470
REMARK 465 VAL A 471
REMARK 465 THR A 472
REMARK 465 VAL A 473
REMARK 465 LYS A 474
REMARK 465 LYS A 475
REMARK 465 SER A 476
REMARK 465 ASP A 477
REMARK 465 ILE A 478
REMARK 465 ASP A 479
REMARK 465 LYS A 480
REMARK 465 GLN A 481
REMARK 465 ARG A 482
REMARK 465 ASP A 483
REMARK 465 ILE A 484
REMARK 465 ILE A 485
REMARK 465 THR A 486
REMARK 465 GLY A 487
REMARK 465 TRP A 488
REMARK 465 LYS A 489
REMARK 465 LYS A 490
REMARK 465 PHE A 491
REMARK 465 VAL A 492
REMARK 465 ALA A 493
REMARK 465 ASP A 494
REMARK 465 ARG A 495
REMARK 465 LYS A 496
REMARK 465 LYS A 497
REMARK 465 THR A 498
REMARK 465 SER A 499
REMARK 465 GLY A 500
REMARK 465 ILE A 501
REMARK 465 CYS A 502
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 ALA B 6
REMARK 465 VAL B 7
REMARK 465 SER B 8
REMARK 465 GLU B 9
REMARK 465 SER B 10
REMARK 465 ASP B 11
REMARK 465 SER B 449
REMARK 465 ARG B 450
REMARK 465 VAL B 451
REMARK 465 ILE B 452
REMARK 465 HIS B 453
REMARK 465 LYS B 454
REMARK 465 ILE B 455
REMARK 465 SER B 456
REMARK 465 LEU B 457
REMARK 465 GLY B 458
REMARK 465 GLN B 459
REMARK 465 GLU B 460
REMARK 465 LYS B 461
REMARK 465 SER B 462
REMARK 465 GLU B 463
REMARK 465 SER B 464
REMARK 465 ASN B 465
REMARK 465 SER B 466
REMARK 465 ASP B 467
REMARK 465 ASN B 468
REMARK 465 LEU B 469
REMARK 465 MET B 470
REMARK 465 VAL B 471
REMARK 465 THR B 472
REMARK 465 VAL B 473
REMARK 465 LYS B 474
REMARK 465 LYS B 475
REMARK 465 SER B 476
REMARK 465 ASP B 477
REMARK 465 ILE B 478
REMARK 465 ASP B 479
REMARK 465 LYS B 480
REMARK 465 GLN B 481
REMARK 465 ARG B 482
REMARK 465 ASP B 483
REMARK 465 ILE B 484
REMARK 465 ILE B 485
REMARK 465 THR B 486
REMARK 465 GLY B 487
REMARK 465 TRP B 488
REMARK 465 LYS B 489
REMARK 465 LYS B 490
REMARK 465 PHE B 491
REMARK 465 VAL B 492
REMARK 465 ALA B 493
REMARK 465 ASP B 494
REMARK 465 ARG B 495
REMARK 465 LYS B 496
REMARK 465 LYS B 497
REMARK 465 THR B 498
REMARK 465 SER B 499
REMARK 465 GLY B 500
REMARK 465 ILE B 501
REMARK 465 CYS B 502
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 LEU C 3
REMARK 465 SER C 4
REMARK 465 HIS C 5
REMARK 465 ALA C 6
REMARK 465 VAL C 7
REMARK 465 SER C 8
REMARK 465 GLU C 9
REMARK 465 SER C 10
REMARK 465 ASP C 11
REMARK 465 SER C 449
REMARK 465 ARG C 450
REMARK 465 VAL C 451
REMARK 465 ILE C 452
REMARK 465 HIS C 453
REMARK 465 LYS C 454
REMARK 465 ILE C 455
REMARK 465 SER C 456
REMARK 465 LEU C 457
REMARK 465 GLY C 458
REMARK 465 GLN C 459
REMARK 465 GLU C 460
REMARK 465 LYS C 461
REMARK 465 SER C 462
REMARK 465 GLU C 463
REMARK 465 SER C 464
REMARK 465 ASN C 465
REMARK 465 SER C 466
REMARK 465 ASP C 467
REMARK 465 ASN C 468
REMARK 465 LEU C 469
REMARK 465 MET C 470
REMARK 465 VAL C 471
REMARK 465 THR C 472
REMARK 465 VAL C 473
REMARK 465 LYS C 474
REMARK 465 LYS C 475
REMARK 465 SER C 476
REMARK 465 ASP C 477
REMARK 465 ILE C 478
REMARK 465 ASP C 479
REMARK 465 LYS C 480
REMARK 465 GLN C 481
REMARK 465 ARG C 482
REMARK 465 ASP C 483
REMARK 465 ILE C 484
REMARK 465 ILE C 485
REMARK 465 THR C 486
REMARK 465 GLY C 487
REMARK 465 TRP C 488
REMARK 465 LYS C 489
REMARK 465 LYS C 490
REMARK 465 PHE C 491
REMARK 465 VAL C 492
REMARK 465 ALA C 493
REMARK 465 ASP C 494
REMARK 465 ARG C 495
REMARK 465 LYS C 496
REMARK 465 LYS C 497
REMARK 465 THR C 498
REMARK 465 SER C 499
REMARK 465 GLY C 500
REMARK 465 ILE C 501
REMARK 465 CYS C 502
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 LEU D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 ALA D 6
REMARK 465 VAL D 7
REMARK 465 SER D 8
REMARK 465 GLU D 9
REMARK 465 SER D 10
REMARK 465 ASP D 11
REMARK 465 PRO D 448
REMARK 465 SER D 449
REMARK 465 ARG D 450
REMARK 465 VAL D 451
REMARK 465 ILE D 452
REMARK 465 HIS D 453
REMARK 465 LYS D 454
REMARK 465 ILE D 455
REMARK 465 SER D 456
REMARK 465 LEU D 457
REMARK 465 GLY D 458
REMARK 465 GLN D 459
REMARK 465 GLU D 460
REMARK 465 LYS D 461
REMARK 465 SER D 462
REMARK 465 GLU D 463
REMARK 465 SER D 464
REMARK 465 ASN D 465
REMARK 465 SER D 466
REMARK 465 ASP D 467
REMARK 465 ASN D 468
REMARK 465 LEU D 469
REMARK 465 MET D 470
REMARK 465 VAL D 471
REMARK 465 THR D 472
REMARK 465 VAL D 473
REMARK 465 LYS D 474
REMARK 465 LYS D 475
REMARK 465 SER D 476
REMARK 465 ASP D 477
REMARK 465 ILE D 478
REMARK 465 ASP D 479
REMARK 465 LYS D 480
REMARK 465 GLN D 481
REMARK 465 ARG D 482
REMARK 465 ASP D 483
REMARK 465 ILE D 484
REMARK 465 ILE D 485
REMARK 465 THR D 486
REMARK 465 GLY D 487
REMARK 465 TRP D 488
REMARK 465 LYS D 489
REMARK 465 LYS D 490
REMARK 465 PHE D 491
REMARK 465 VAL D 492
REMARK 465 ALA D 493
REMARK 465 ASP D 494
REMARK 465 ARG D 495
REMARK 465 LYS D 496
REMARK 465 LYS D 497
REMARK 465 THR D 498
REMARK 465 SER D 499
REMARK 465 GLY D 500
REMARK 465 ILE D 501
REMARK 465 CYS D 502
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 LEU E 3
REMARK 465 SER E 4
REMARK 465 HIS E 5
REMARK 465 ALA E 6
REMARK 465 VAL E 7
REMARK 465 SER E 8
REMARK 465 GLU E 9
REMARK 465 SER E 10
REMARK 465 ASP E 11
REMARK 465 PRO E 448
REMARK 465 SER E 449
REMARK 465 ARG E 450
REMARK 465 VAL E 451
REMARK 465 ILE E 452
REMARK 465 HIS E 453
REMARK 465 LYS E 454
REMARK 465 ILE E 455
REMARK 465 SER E 456
REMARK 465 LEU E 457
REMARK 465 GLY E 458
REMARK 465 GLN E 459
REMARK 465 GLU E 460
REMARK 465 LYS E 461
REMARK 465 SER E 462
REMARK 465 GLU E 463
REMARK 465 SER E 464
REMARK 465 ASN E 465
REMARK 465 SER E 466
REMARK 465 ASP E 467
REMARK 465 ASN E 468
REMARK 465 LEU E 469
REMARK 465 MET E 470
REMARK 465 VAL E 471
REMARK 465 THR E 472
REMARK 465 VAL E 473
REMARK 465 LYS E 474
REMARK 465 LYS E 475
REMARK 465 SER E 476
REMARK 465 ASP E 477
REMARK 465 ILE E 478
REMARK 465 ASP E 479
REMARK 465 LYS E 480
REMARK 465 GLN E 481
REMARK 465 ARG E 482
REMARK 465 ASP E 483
REMARK 465 ILE E 484
REMARK 465 ILE E 485
REMARK 465 THR E 486
REMARK 465 GLY E 487
REMARK 465 TRP E 488
REMARK 465 LYS E 489
REMARK 465 LYS E 490
REMARK 465 PHE E 491
REMARK 465 VAL E 492
REMARK 465 ALA E 493
REMARK 465 ASP E 494
REMARK 465 ARG E 495
REMARK 465 LYS E 496
REMARK 465 LYS E 497
REMARK 465 THR E 498
REMARK 465 SER E 499
REMARK 465 GLY E 500
REMARK 465 ILE E 501
REMARK 465 CYS E 502
REMARK 465 MET F 1
REMARK 465 VAL F 2
REMARK 465 LEU F 3
REMARK 465 SER F 4
REMARK 465 HIS F 5
REMARK 465 ALA F 6
REMARK 465 VAL F 7
REMARK 465 SER F 8
REMARK 465 GLU F 9
REMARK 465 SER F 10
REMARK 465 ASP F 11
REMARK 465 SER F 449
REMARK 465 ARG F 450
REMARK 465 VAL F 451
REMARK 465 ILE F 452
REMARK 465 HIS F 453
REMARK 465 LYS F 454
REMARK 465 ILE F 455
REMARK 465 SER F 456
REMARK 465 LEU F 457
REMARK 465 GLY F 458
REMARK 465 GLN F 459
REMARK 465 GLU F 460
REMARK 465 LYS F 461
REMARK 465 SER F 462
REMARK 465 GLU F 463
REMARK 465 SER F 464
REMARK 465 ASN F 465
REMARK 465 SER F 466
REMARK 465 ASP F 467
REMARK 465 ASN F 468
REMARK 465 LEU F 469
REMARK 465 MET F 470
REMARK 465 VAL F 471
REMARK 465 THR F 472
REMARK 465 VAL F 473
REMARK 465 LYS F 474
REMARK 465 LYS F 475
REMARK 465 SER F 476
REMARK 465 ASP F 477
REMARK 465 ILE F 478
REMARK 465 ASP F 479
REMARK 465 LYS F 480
REMARK 465 GLN F 481
REMARK 465 ARG F 482
REMARK 465 ASP F 483
REMARK 465 ILE F 484
REMARK 465 ILE F 485
REMARK 465 THR F 486
REMARK 465 GLY F 487
REMARK 465 TRP F 488
REMARK 465 LYS F 489
REMARK 465 LYS F 490
REMARK 465 PHE F 491
REMARK 465 VAL F 492
REMARK 465 ALA F 493
REMARK 465 ASP F 494
REMARK 465 ARG F 495
REMARK 465 LYS F 496
REMARK 465 LYS F 497
REMARK 465 THR F 498
REMARK 465 SER F 499
REMARK 465 GLY F 500
REMARK 465 ILE F 501
REMARK 465 CYS F 502
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 30 -53.52 -122.22
REMARK 500 PRO A 111 86.87 -69.72
REMARK 500 GLU A 113 -159.55 -74.57
REMARK 500 ASN A 215 14.69 -148.56
REMARK 500 ASP A 238 58.00 -107.52
REMARK 500 ILE A 251 -51.04 -120.09
REMARK 500 TRP A 261 -15.10 -141.01
REMARK 500 ASP A 262 -146.70 -99.94
REMARK 500 LLP A 277 -100.73 -95.12
REMARK 500 ASN A 305 22.09 -152.54
REMARK 500 PHE A 318 -95.16 -125.05
REMARK 500 PRO A 374 87.37 -63.14
REMARK 500 ASP A 382 81.19 67.03
REMARK 500 SER A 383 42.98 -83.58
REMARK 500 SER A 384 -78.18 -79.60
REMARK 500 ASN A 410 56.98 -95.48
REMARK 500 GLN A 412 0.85 -67.31
REMARK 500 PHE B 30 -53.45 -121.62
REMARK 500 ASN B 215 15.19 -148.61
REMARK 500 ASP B 238 57.99 -106.97
REMARK 500 ALA B 245 40.34 -104.62
REMARK 500 TRP B 261 -15.45 -140.96
REMARK 500 ASP B 262 -146.55 -99.74
REMARK 500 LLP B 277 -104.68 -95.75
REMARK 500 ASN B 305 15.51 -150.97
REMARK 500 PHE B 318 -94.94 -125.08
REMARK 500 PRO B 374 87.09 -63.30
REMARK 500 ASP B 382 81.40 67.20
REMARK 500 SER B 383 42.86 -83.69
REMARK 500 SER B 384 -78.19 -79.57
REMARK 500 ASN B 410 59.07 -103.10
REMARK 500 PHE C 30 -53.73 -122.01
REMARK 500 PRO C 111 84.87 -69.66
REMARK 500 GLU C 113 55.80 -98.98
REMARK 500 GLU C 114 -72.04 68.59
REMARK 500 ASN C 215 14.86 -148.49
REMARK 500 ASP C 238 57.74 -107.63
REMARK 500 TRP C 261 -15.53 -141.31
REMARK 500 ASP C 262 -146.83 -99.99
REMARK 500 LLP C 277 -106.28 -94.73
REMARK 500 ASN C 305 26.82 -153.67
REMARK 500 PHE C 318 -95.05 -125.67
REMARK 500 PRO C 374 87.53 -63.39
REMARK 500 ASP C 382 81.34 66.97
REMARK 500 SER C 383 42.97 -83.61
REMARK 500 SER C 384 -78.36 -79.67
REMARK 500 ALA C 411 30.76 -158.23
REMARK 500 PHE D 30 -53.37 -122.24
REMARK 500 GLU D 113 46.49 -100.16
REMARK 500 GLU D 114 -55.24 72.98
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HBX A 1 502 UNP Q42521 DCE1_ARATH 12 513
DBREF 3HBX B 1 502 UNP Q42521 DCE1_ARATH 12 513
DBREF 3HBX C 1 502 UNP Q42521 DCE1_ARATH 12 513
DBREF 3HBX D 1 502 UNP Q42521 DCE1_ARATH 12 513
DBREF 3HBX E 1 502 UNP Q42521 DCE1_ARATH 12 513
DBREF 3HBX F 1 502 UNP Q42521 DCE1_ARATH 12 513
SEQRES 1 A 502 MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES 2 A 502 VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES 3 A 502 LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES 4 A 502 GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES 5 A 502 ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES 6 A 502 THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES 7 A 502 SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES 8 A 502 VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES 9 A 502 ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES 10 A 502 ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES 11 A 502 MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES 12 A 502 LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES 13 A 502 ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES 14 A 502 PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES 15 A 502 LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES 16 A 502 VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES 17 A 502 ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES 18 A 502 LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES 19 A 502 THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES 20 A 502 GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES 21 A 502 TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES 22 A 502 SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES 23 A 502 TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES 24 A 502 LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES 25 A 502 THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES 26 A 502 ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES 27 A 502 GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES 28 A 502 ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES 29 A 502 ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES 30 A 502 PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES 31 A 502 ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES 32 A 502 ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES 33 A 502 LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES 34 A 502 ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES 35 A 502 GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES 36 A 502 SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES 37 A 502 LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES 38 A 502 ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES 39 A 502 ARG LYS LYS THR SER GLY ILE CYS
SEQRES 1 B 502 MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES 2 B 502 VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES 3 B 502 LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES 4 B 502 GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES 5 B 502 ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES 6 B 502 THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES 7 B 502 SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES 8 B 502 VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES 9 B 502 ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES 10 B 502 ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES 11 B 502 MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES 12 B 502 LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES 13 B 502 ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES 14 B 502 PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES 15 B 502 LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES 16 B 502 VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES 17 B 502 ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES 18 B 502 LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES 19 B 502 THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES 20 B 502 GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES 21 B 502 TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES 22 B 502 SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES 23 B 502 TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES 24 B 502 LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES 25 B 502 THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES 26 B 502 ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES 27 B 502 GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES 28 B 502 ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES 29 B 502 ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES 30 B 502 PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES 31 B 502 ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES 32 B 502 ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES 33 B 502 LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES 34 B 502 ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES 35 B 502 GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES 36 B 502 SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES 37 B 502 LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES 38 B 502 ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES 39 B 502 ARG LYS LYS THR SER GLY ILE CYS
SEQRES 1 C 502 MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES 2 C 502 VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES 3 C 502 LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES 4 C 502 GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES 5 C 502 ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES 6 C 502 THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES 7 C 502 SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES 8 C 502 VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES 9 C 502 ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES 10 C 502 ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES 11 C 502 MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES 12 C 502 LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES 13 C 502 ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES 14 C 502 PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES 15 C 502 LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES 16 C 502 VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES 17 C 502 ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES 18 C 502 LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES 19 C 502 THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES 20 C 502 GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES 21 C 502 TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES 22 C 502 SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES 23 C 502 TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES 24 C 502 LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES 25 C 502 THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES 26 C 502 ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES 27 C 502 GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES 28 C 502 ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES 29 C 502 ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES 30 C 502 PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES 31 C 502 ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES 32 C 502 ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES 33 C 502 LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES 34 C 502 ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES 35 C 502 GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES 36 C 502 SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES 37 C 502 LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES 38 C 502 ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES 39 C 502 ARG LYS LYS THR SER GLY ILE CYS
SEQRES 1 D 502 MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES 2 D 502 VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES 3 D 502 LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES 4 D 502 GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES 5 D 502 ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES 6 D 502 THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES 7 D 502 SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES 8 D 502 VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES 9 D 502 ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES 10 D 502 ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES 11 D 502 MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES 12 D 502 LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES 13 D 502 ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES 14 D 502 PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES 15 D 502 LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES 16 D 502 VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES 17 D 502 ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES 18 D 502 LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES 19 D 502 THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES 20 D 502 GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES 21 D 502 TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES 22 D 502 SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES 23 D 502 TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES 24 D 502 LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES 25 D 502 THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES 26 D 502 ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES 27 D 502 GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES 28 D 502 ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES 29 D 502 ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES 30 D 502 PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES 31 D 502 ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES 32 D 502 ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES 33 D 502 LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES 34 D 502 ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES 35 D 502 GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES 36 D 502 SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES 37 D 502 LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES 38 D 502 ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES 39 D 502 ARG LYS LYS THR SER GLY ILE CYS
SEQRES 1 E 502 MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES 2 E 502 VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES 3 E 502 LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES 4 E 502 GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES 5 E 502 ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES 6 E 502 THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES 7 E 502 SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES 8 E 502 VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES 9 E 502 ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES 10 E 502 ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES 11 E 502 MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES 12 E 502 LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES 13 E 502 ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES 14 E 502 PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES 15 E 502 LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES 16 E 502 VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES 17 E 502 ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES 18 E 502 LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES 19 E 502 THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES 20 E 502 GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES 21 E 502 TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES 22 E 502 SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES 23 E 502 TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES 24 E 502 LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES 25 E 502 THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES 26 E 502 ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES 27 E 502 GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES 28 E 502 ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES 29 E 502 ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES 30 E 502 PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES 31 E 502 ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES 32 E 502 ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES 33 E 502 LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES 34 E 502 ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES 35 E 502 GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES 36 E 502 SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES 37 E 502 LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES 38 E 502 ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES 39 E 502 ARG LYS LYS THR SER GLY ILE CYS
SEQRES 1 F 502 MET VAL LEU SER HIS ALA VAL SER GLU SER ASP VAL SER
SEQRES 2 F 502 VAL HIS SER THR PHE ALA SER ARG TYR VAL ARG THR SER
SEQRES 3 F 502 LEU PRO ARG PHE LYS MET PRO GLU ASN SER ILE PRO LYS
SEQRES 4 F 502 GLU ALA ALA TYR GLN ILE ILE ASN ASP GLU LEU MET LEU
SEQRES 5 F 502 ASP GLY ASN PRO ARG LEU ASN LEU ALA SER PHE VAL THR
SEQRES 6 F 502 THR TRP MET GLU PRO GLU CYS ASP LYS LEU ILE MET SER
SEQRES 7 F 502 SER ILE ASN LYS ASN TYR VAL ASP MET ASP GLU TYR PRO
SEQRES 8 F 502 VAL THR THR GLU LEU GLN ASN ARG CYS VAL ASN MET ILE
SEQRES 9 F 502 ALA HIS LEU PHE ASN ALA PRO LEU GLU GLU ALA GLU THR
SEQRES 10 F 502 ALA VAL GLY VAL GLY THR VAL GLY SER SER GLU ALA ILE
SEQRES 11 F 502 MET LEU ALA GLY LEU ALA PHE LYS ARG LYS TRP GLN ASN
SEQRES 12 F 502 LYS ARG LYS ALA GLU GLY LYS PRO VAL ASP LYS PRO ASN
SEQRES 13 F 502 ILE VAL THR GLY ALA ASN VAL GLN VAL CYS TRP GLU LYS
SEQRES 14 F 502 PHE ALA ARG TYR PHE GLU VAL GLU LEU LYS GLU VAL LYS
SEQRES 15 F 502 LEU SER GLU GLY TYR TYR VAL MET ASP PRO GLN GLN ALA
SEQRES 16 F 502 VAL ASP MET VAL ASP GLU ASN THR ILE CYS VAL ALA ALA
SEQRES 17 F 502 ILE LEU GLY SER THR LEU ASN GLY GLU PHE GLU ASP VAL
SEQRES 18 F 502 LYS LEU LEU ASN ASP LEU LEU VAL GLU LYS ASN LYS GLU
SEQRES 19 F 502 THR GLY TRP ASP THR PRO ILE HIS VAL ASP ALA ALA SER
SEQRES 20 F 502 GLY GLY PHE ILE ALA PRO PHE LEU TYR PRO GLU LEU GLU
SEQRES 21 F 502 TRP ASP PHE ARG LEU PRO LEU VAL LYS SER ILE ASN VAL
SEQRES 22 F 502 SER GLY HIS LLP TYR GLY LEU VAL TYR ALA GLY ILE GLY
SEQRES 23 F 502 TRP VAL ILE TRP ARG ASN LYS GLU ASP LEU PRO GLU GLU
SEQRES 24 F 502 LEU ILE PHE HIS ILE ASN TYR LEU GLY ALA ASP GLN PRO
SEQRES 25 F 502 THR PHE THR LEU ASN PHE SER LYS GLY SER SER GLN VAL
SEQRES 26 F 502 ILE ALA GLN TYR TYR GLN LEU ILE ARG LEU GLY HIS GLU
SEQRES 27 F 502 GLY TYR ARG ASN VAL MET GLU ASN CYS ARG GLU ASN MET
SEQRES 28 F 502 ILE VAL LEU ARG GLU GLY LEU GLU LYS THR GLU ARG PHE
SEQRES 29 F 502 ASN ILE VAL SER LYS ASP GLU GLY VAL PRO LEU VAL ALA
SEQRES 30 F 502 PHE SER LEU LYS ASP SER SER CYS HIS THR GLU PHE GLU
SEQRES 31 F 502 ILE SER ASP MET LEU ARG ARG TYR GLY TRP ILE VAL PRO
SEQRES 32 F 502 ALA TYR THR MET PRO PRO ASN ALA GLN HIS ILE THR VAL
SEQRES 33 F 502 LEU ARG VAL VAL ILE ARG GLU ASP PHE SER ARG THR LEU
SEQRES 34 F 502 ALA GLU ARG LEU VAL ILE ASP ILE GLU LYS VAL MET ARG
SEQRES 35 F 502 GLU LEU ASP GLU LEU PRO SER ARG VAL ILE HIS LYS ILE
SEQRES 36 F 502 SER LEU GLY GLN GLU LYS SER GLU SER ASN SER ASP ASN
SEQRES 37 F 502 LEU MET VAL THR VAL LYS LYS SER ASP ILE ASP LYS GLN
SEQRES 38 F 502 ARG ASP ILE ILE THR GLY TRP LYS LYS PHE VAL ALA ASP
SEQRES 39 F 502 ARG LYS LYS THR SER GLY ILE CYS
MODRES 3HBX LLP A 277 LYS
MODRES 3HBX LLP B 277 LYS
MODRES 3HBX LLP C 277 LYS
MODRES 3HBX LLP D 277 LYS
MODRES 3HBX LLP E 277 LYS
MODRES 3HBX LLP F 277 LYS
HET LLP A 277 24
HET LLP B 277 24
HET LLP C 277 24
HET LLP D 277 24
HET LLP E 277 24
HET LLP F 277 24
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP 6(C14 H22 N3 O7 P)
FORMUL 7 HOH *314(H2 O)
HELIX 1 1 ARG A 21 THR A 25 5 5
HELIX 2 2 PRO A 38 LEU A 50 1 13
HELIX 3 3 MET A 51 ASP A 53 5 3
HELIX 4 4 ASN A 55 ASN A 59 5 5
HELIX 5 5 GLU A 69 SER A 79 1 11
HELIX 6 6 TYR A 90 PHE A 108 1 19
HELIX 7 7 GLY A 125 GLU A 148 1 24
HELIX 8 8 GLN A 164 PHE A 174 1 11
HELIX 9 9 ASP A 191 VAL A 199 1 9
HELIX 10 10 ASP A 220 GLY A 236 1 17
HELIX 11 11 SER A 247 PHE A 250 5 4
HELIX 12 12 ILE A 251 TYR A 256 1 6
HELIX 13 13 ASN A 292 LEU A 296 5 5
HELIX 14 14 PRO A 297 ILE A 301 5 5
HELIX 15 15 SER A 322 LYS A 360 1 39
HELIX 16 16 THR A 387 ARG A 397 1 11
HELIX 17 17 SER A 426 GLU A 446 1 21
HELIX 18 18 ARG B 21 THR B 25 5 5
HELIX 19 19 PRO B 38 LEU B 50 1 13
HELIX 20 20 MET B 51 ASP B 53 5 3
HELIX 21 21 ASN B 55 ASN B 59 5 5
HELIX 22 22 GLU B 69 SER B 79 1 11
HELIX 23 23 TYR B 90 PHE B 108 1 19
HELIX 24 24 GLY B 125 GLU B 148 1 24
HELIX 25 25 GLN B 164 PHE B 174 1 11
HELIX 26 26 ASP B 191 VAL B 199 1 9
HELIX 27 27 ASP B 220 GLY B 236 1 17
HELIX 28 28 SER B 247 PHE B 250 5 4
HELIX 29 29 ILE B 251 TYR B 256 1 6
HELIX 30 30 ASN B 292 LEU B 296 5 5
HELIX 31 31 PRO B 297 ILE B 301 5 5
HELIX 32 32 SER B 322 LYS B 360 1 39
HELIX 33 33 THR B 387 ARG B 397 1 11
HELIX 34 34 SER B 426 GLU B 446 1 21
HELIX 35 35 ARG C 21 THR C 25 5 5
HELIX 36 36 PRO C 38 LEU C 50 1 13
HELIX 37 37 MET C 51 ASP C 53 5 3
HELIX 38 38 ASN C 55 ASN C 59 5 5
HELIX 39 39 GLU C 69 SER C 79 1 11
HELIX 40 40 TYR C 90 PHE C 108 1 19
HELIX 41 41 GLY C 125 GLU C 148 1 24
HELIX 42 42 GLN C 164 PHE C 174 1 11
HELIX 43 43 ASP C 191 VAL C 199 1 9
HELIX 44 44 ASP C 220 GLY C 236 1 17
HELIX 45 45 SER C 247 PHE C 250 5 4
HELIX 46 46 ILE C 251 TYR C 256 1 6
HELIX 47 47 ASN C 292 LEU C 296 5 5
HELIX 48 48 PRO C 297 ILE C 301 5 5
HELIX 49 49 SER C 322 LYS C 360 1 39
HELIX 50 50 THR C 387 ARG C 397 1 11
HELIX 51 51 SER C 426 GLU C 446 1 21
HELIX 52 52 ARG D 21 THR D 25 5 5
HELIX 53 53 PRO D 38 LEU D 50 1 13
HELIX 54 54 MET D 51 ASP D 53 5 3
HELIX 55 55 ASN D 55 ASN D 59 5 5
HELIX 56 56 GLU D 69 SER D 79 1 11
HELIX 57 57 TYR D 90 PHE D 108 1 19
HELIX 58 58 GLY D 125 GLU D 148 1 24
HELIX 59 59 GLN D 164 PHE D 174 1 11
HELIX 60 60 ASP D 191 VAL D 199 1 9
HELIX 61 61 ASP D 220 GLY D 236 1 17
HELIX 62 62 SER D 247 PHE D 250 5 4
HELIX 63 63 ILE D 251 TYR D 256 1 6
HELIX 64 64 ASN D 292 LEU D 296 5 5
HELIX 65 65 PRO D 297 ILE D 301 5 5
HELIX 66 66 SER D 322 LYS D 360 1 39
HELIX 67 67 THR D 387 ARG D 397 1 11
HELIX 68 68 SER D 426 GLU D 446 1 21
HELIX 69 69 ARG E 21 THR E 25 5 5
HELIX 70 70 PRO E 38 LEU E 50 1 13
HELIX 71 71 MET E 51 ASP E 53 5 3
HELIX 72 72 ASN E 55 ASN E 59 5 5
HELIX 73 73 GLU E 69 SER E 79 1 11
HELIX 74 74 TYR E 90 PHE E 108 1 19
HELIX 75 75 GLY E 125 GLU E 148 1 24
HELIX 76 76 GLN E 164 PHE E 174 1 11
HELIX 77 77 ASP E 191 VAL E 199 1 9
HELIX 78 78 ASP E 220 GLY E 236 1 17
HELIX 79 79 SER E 247 PHE E 250 5 4
HELIX 80 80 ILE E 251 TYR E 256 1 6
HELIX 81 81 ASN E 292 LEU E 296 5 5
HELIX 82 82 PRO E 297 ILE E 301 5 5
HELIX 83 83 SER E 322 LYS E 360 1 39
HELIX 84 84 THR E 387 ARG E 397 1 11
HELIX 85 85 SER E 426 GLU E 446 1 21
HELIX 86 86 ARG F 21 THR F 25 5 5
HELIX 87 87 PRO F 38 LEU F 50 1 13
HELIX 88 88 MET F 51 ASP F 53 5 3
HELIX 89 89 ASN F 55 ASN F 59 5 5
HELIX 90 90 GLU F 69 SER F 79 1 11
HELIX 91 91 TYR F 90 PHE F 108 1 19
HELIX 92 92 GLY F 125 GLU F 148 1 24
HELIX 93 93 GLN F 164 PHE F 174 1 11
HELIX 94 94 ASP F 191 VAL F 199 1 9
HELIX 95 95 ASP F 220 GLY F 236 1 17
HELIX 96 96 SER F 247 PHE F 250 5 4
HELIX 97 97 ILE F 251 TYR F 256 1 6
HELIX 98 98 ASN F 292 LEU F 296 5 5
HELIX 99 99 PRO F 297 ILE F 301 5 5
HELIX 100 100 SER F 322 LYS F 360 1 39
HELIX 101 101 THR F 387 ARG F 397 1 11
HELIX 102 102 SER F 426 GLU F 446 1 21
SHEET 1 A 7 VAL A 119 THR A 123 0
SHEET 2 A 7 GLY A 286 TRP A 290 -1 O GLY A 286 N THR A 123
SHEET 3 A 7 VAL A 268 SER A 274 -1 N ILE A 271 O ILE A 289
SHEET 4 A 7 ILE A 241 ASP A 244 1 N ILE A 241 O LYS A 269
SHEET 5 A 7 THR A 203 ILE A 209 1 N ALA A 208 O ASP A 244
SHEET 6 A 7 ASN A 156 GLY A 160 1 N ASN A 156 O ILE A 204
SHEET 7 A 7 GLU A 177 VAL A 181 1 O LYS A 179 N ILE A 157
SHEET 1 B 2 PHE A 302 ILE A 304 0
SHEET 2 B 2 GLN A 311 THR A 313 -1 O THR A 313 N PHE A 302
SHEET 1 C 4 PHE A 364 ILE A 366 0
SHEET 2 C 4 LEU A 375 LEU A 380 -1 O SER A 379 N ASN A 365
SHEET 3 C 4 THR A 415 VAL A 420 -1 O LEU A 417 N PHE A 378
SHEET 4 C 4 ALA A 404 THR A 406 -1 N TYR A 405 O VAL A 416
SHEET 1 D 7 VAL B 119 THR B 123 0
SHEET 2 D 7 GLY B 286 TRP B 290 -1 O GLY B 286 N THR B 123
SHEET 3 D 7 VAL B 268 SER B 274 -1 N ILE B 271 O ILE B 289
SHEET 4 D 7 ILE B 241 ASP B 244 1 N ILE B 241 O LYS B 269
SHEET 5 D 7 THR B 203 ILE B 209 1 N ALA B 208 O ASP B 244
SHEET 6 D 7 ASN B 156 GLY B 160 1 N ASN B 156 O ILE B 204
SHEET 7 D 7 GLU B 177 VAL B 181 1 O LYS B 179 N ILE B 157
SHEET 1 E 2 PHE B 302 ILE B 304 0
SHEET 2 E 2 GLN B 311 THR B 313 -1 O THR B 313 N PHE B 302
SHEET 1 F 4 PHE B 364 ILE B 366 0
SHEET 2 F 4 LEU B 375 LEU B 380 -1 O SER B 379 N ASN B 365
SHEET 3 F 4 THR B 415 VAL B 420 -1 O LEU B 417 N PHE B 378
SHEET 4 F 4 ALA B 404 THR B 406 -1 N TYR B 405 O VAL B 416
SHEET 1 G 7 VAL C 119 THR C 123 0
SHEET 2 G 7 GLY C 286 TRP C 290 -1 O TRP C 290 N VAL C 119
SHEET 3 G 7 VAL C 268 SER C 274 -1 N ILE C 271 O ILE C 289
SHEET 4 G 7 ILE C 241 ASP C 244 1 N ILE C 241 O LYS C 269
SHEET 5 G 7 THR C 203 ILE C 209 1 N ALA C 208 O ASP C 244
SHEET 6 G 7 ASN C 156 GLY C 160 1 N ASN C 156 O ILE C 204
SHEET 7 G 7 GLU C 177 VAL C 181 1 O LYS C 179 N ILE C 157
SHEET 1 H 2 PHE C 302 ILE C 304 0
SHEET 2 H 2 GLN C 311 THR C 313 -1 O THR C 313 N PHE C 302
SHEET 1 I 4 PHE C 364 ILE C 366 0
SHEET 2 I 4 LEU C 375 LEU C 380 -1 O SER C 379 N ASN C 365
SHEET 3 I 4 THR C 415 VAL C 420 -1 O LEU C 417 N PHE C 378
SHEET 4 I 4 ALA C 404 THR C 406 -1 N TYR C 405 O VAL C 416
SHEET 1 J 7 VAL D 119 THR D 123 0
SHEET 2 J 7 GLY D 286 TRP D 290 -1 O GLY D 286 N THR D 123
SHEET 3 J 7 VAL D 268 SER D 274 -1 N ILE D 271 O ILE D 289
SHEET 4 J 7 ILE D 241 ASP D 244 1 N ILE D 241 O LYS D 269
SHEET 5 J 7 THR D 203 ILE D 209 1 N ALA D 208 O ASP D 244
SHEET 6 J 7 ASN D 156 GLY D 160 1 N ASN D 156 O ILE D 204
SHEET 7 J 7 GLU D 177 VAL D 181 1 O LYS D 179 N ILE D 157
SHEET 1 K 2 PHE D 302 ILE D 304 0
SHEET 2 K 2 GLN D 311 THR D 313 -1 O THR D 313 N PHE D 302
SHEET 1 L 4 PHE D 364 ILE D 366 0
SHEET 2 L 4 LEU D 375 LEU D 380 -1 O SER D 379 N ASN D 365
SHEET 3 L 4 THR D 415 VAL D 420 -1 O LEU D 417 N PHE D 378
SHEET 4 L 4 ALA D 404 THR D 406 -1 N TYR D 405 O VAL D 416
SHEET 1 M 7 VAL E 119 THR E 123 0
SHEET 2 M 7 GLY E 286 TRP E 290 -1 O GLY E 286 N THR E 123
SHEET 3 M 7 VAL E 268 SER E 274 -1 N ILE E 271 O ILE E 289
SHEET 4 M 7 ILE E 241 ASP E 244 1 N ILE E 241 O LYS E 269
SHEET 5 M 7 THR E 203 ILE E 209 1 N ALA E 208 O ASP E 244
SHEET 6 M 7 ASN E 156 GLY E 160 1 N ASN E 156 O ILE E 204
SHEET 7 M 7 GLU E 177 VAL E 181 1 O LYS E 179 N ILE E 157
SHEET 1 N 2 PHE E 302 ILE E 304 0
SHEET 2 N 2 GLN E 311 THR E 313 -1 O THR E 313 N PHE E 302
SHEET 1 O 4 PHE E 364 ILE E 366 0
SHEET 2 O 4 LEU E 375 LEU E 380 -1 O SER E 379 N ASN E 365
SHEET 3 O 4 THR E 415 VAL E 420 -1 O LEU E 417 N PHE E 378
SHEET 4 O 4 ALA E 404 THR E 406 -1 N TYR E 405 O VAL E 416
SHEET 1 P 7 VAL F 119 THR F 123 0
SHEET 2 P 7 GLY F 286 TRP F 290 -1 O GLY F 286 N THR F 123
SHEET 3 P 7 VAL F 268 SER F 274 -1 N ILE F 271 O ILE F 289
SHEET 4 P 7 ILE F 241 ASP F 244 1 N ILE F 241 O LYS F 269
SHEET 5 P 7 THR F 203 ILE F 209 1 N ALA F 208 O ASP F 244
SHEET 6 P 7 ASN F 156 GLY F 160 1 N ASN F 156 O ILE F 204
SHEET 7 P 7 GLU F 177 VAL F 181 1 O LYS F 179 N ILE F 157
SHEET 1 Q 2 PHE F 302 ILE F 304 0
SHEET 2 Q 2 GLN F 311 THR F 313 -1 O THR F 313 N PHE F 302
SHEET 1 R 4 PHE F 364 ILE F 366 0
SHEET 2 R 4 LEU F 375 LEU F 380 -1 O SER F 379 N ASN F 365
SHEET 3 R 4 THR F 415 VAL F 420 -1 O LEU F 417 N PHE F 378
SHEET 4 R 4 ALA F 404 THR F 406 -1 N TYR F 405 O VAL F 416
LINK C HIS A 276 N LLP A 277 1555 1555 1.33
LINK C LLP A 277 N TYR A 278 1555 1555 1.33
LINK C HIS B 276 N LLP B 277 1555 1555 1.33
LINK C LLP B 277 N TYR B 278 1555 1555 1.33
LINK C HIS C 276 N LLP C 277 1555 1555 1.33
LINK C LLP C 277 N TYR C 278 1555 1555 1.33
LINK C HIS D 276 N LLP D 277 1555 1555 1.33
LINK C LLP D 277 N TYR D 278 1555 1555 1.33
LINK C HIS E 276 N LLP E 277 1555 1555 1.33
LINK C LLP E 277 N TYR E 278 1555 1555 1.33
LINK C HIS F 276 N LLP F 277 1555 1555 1.33
LINK C LLP F 277 N TYR F 278 1555 1555 1.33
CISPEP 1 GLU A 114 ALA A 115 0 0.13
CISPEP 2 PRO A 409 ASN A 410 0 -0.17
CISPEP 3 PRO B 409 ASN B 410 0 0.93
CISPEP 4 PRO C 409 ASN C 410 0 0.17
CISPEP 5 PRO D 409 ASN D 410 0 0.80
CISPEP 6 PRO E 409 ASN E 410 0 -0.33
CISPEP 7 PRO F 409 ASN F 410 0 0.44
CRYST1 118.098 118.098 200.576 90.00 90.00 120.00 P 32 18
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 0.008468 0.004889 0.000000 0.00000
SCALE2 0.000000 0.009777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004986 0.00000
MTRIX1 1 0.318302 0.947977 0.004831 -54.36670 1
MTRIX2 1 0.947233 -0.317841 -0.041559 75.45140 1
MTRIX3 1 -0.037861 0.017805 -0.999124 -1.46108 1
MTRIX1 2 -0.503232 0.864004 0.015946 -48.50860 1
MTRIX2 2 -0.864137 -0.503243 -0.003575 88.45970 1
MTRIX3 2 0.004936 -0.015578 0.999866 1.23684 1
MTRIX1 3 -0.979238 -0.202103 0.015704 13.92040 1
MTRIX2 3 -0.202182 0.979341 -0.003624 1.35622 1
MTRIX3 3 -0.014647 -0.006724 -0.999870 0.68996 1
MTRIX1 4 -0.497458 -0.867314 0.017358 52.35720 1
MTRIX2 4 0.867356 -0.497632 -0.007499 86.29350 1
MTRIX3 4 0.015142 0.011325 0.999821 -0.80090 1
MTRIX1 5 0.667823 -0.744318 0.001814 43.75040 1
MTRIX2 5 -0.744144 -0.667715 -0.020149 97.96570 1
MTRIX3 5 0.016208 0.012106 -0.999795 -1.02356 1
MTRIX1 6 0.317723 0.948059 -0.015386 -54.46810 1
MTRIX2 6 0.948068 -0.317896 -0.010433 75.69090 1
MTRIX3 6 -0.014782 -0.011273 -0.999827 0.62471 1
MTRIX1 7 -0.500290 0.865677 0.017686 -48.81490 1
MTRIX2 7 -0.865653 -0.500512 0.011547 88.35250 1
MTRIX3 7 0.018848 -0.009533 0.999777 0.40187 1
MTRIX1 8 -0.979966 -0.199142 0.002942 13.77390 1
MTRIX2 8 -0.199138 0.979970 0.001718 1.29489 1
MTRIX3 8 -0.003225 0.001098 -0.999994 0.05058 1
MTRIX1 9 -0.499153 -0.866332 0.017746 52.19540 1
MTRIX2 9 0.866352 -0.499351 -0.009100 86.47640 1
MTRIX3 9 0.016745 0.010832 0.999801 -0.71221 1
MTRIX1 10 0.664267 -0.747260 -0.018753 44.00390 1
MTRIX2 10 -0.747290 -0.664464 0.006800 97.82600 1
MTRIX3 10 -0.017542 0.009497 -0.999801 -0.54785 1
(ATOM LINES ARE NOT SHOWN.)
END
