HEADER OXIDOREDUCTASE 27-DEC-11 3V9I
TITLE CRYSTAL STRUCTURE OF HUMAN 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE
TITLE 2 MUTANT S352L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: UNP RESIDUES 18-563;
COMPND 6 SYNONYM: 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE, P5C DEHYDROGENASE,
COMPND 7 ALDEHYDE DEHYDROGENASE FAMILY 4 MEMBER A1;
COMPND 8 EC: 1.5.1.12;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDH4, ALDH4A1, P5CDH;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALDEHYDE DEHYDROGENASE, ROSSMANN FOLD, NUCLEOTIDE BINDING, ACTING ON
KEYWDS 2 ALDEHYDE OR OXO GROUP OF DONORS, NAD OR NADP AS ACCEPTOR,
KEYWDS 3 MITOCHONDRIA, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.TANNER,R.K.SINGH
REVDAT 3 13-SEP-23 3V9I 1 SEQADV
REVDAT 2 27-JUN-12 3V9I 1 JRNL
REVDAT 1 02-MAY-12 3V9I 0
JRNL AUTH D.SRIVASTAVA,R.K.SINGH,M.A.MOXLEY,M.T.HENZL,D.F.BECKER,
JRNL AUTH 2 J.J.TANNER
JRNL TITL THE THREE-DIMENSIONAL STRUCTURAL BASIS OF TYPE II
JRNL TITL 2 HYPERPROLINEMIA.
JRNL REF J.MOL.BIOL. V. 420 176 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22516612
JRNL DOI 10.1016/J.JMB.2012.04.010
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 55850
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1338
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 43.8314 - 6.1351 0.92 5232 127 0.2088 0.2536
REMARK 3 2 6.1351 - 4.8717 0.95 5362 128 0.2212 0.2407
REMARK 3 3 4.8717 - 4.2564 0.96 5392 135 0.1697 0.2130
REMARK 3 4 4.2564 - 3.8675 0.97 5460 132 0.1844 0.2657
REMARK 3 5 3.8675 - 3.5904 0.98 5479 137 0.1987 0.2502
REMARK 3 6 3.5904 - 3.3788 0.98 5504 134 0.2050 0.2635
REMARK 3 7 3.3788 - 3.2097 0.99 5502 137 0.2275 0.2796
REMARK 3 8 3.2097 - 3.0700 0.99 5556 134 0.2347 0.3559
REMARK 3 9 3.0700 - 2.9518 0.99 5513 138 0.2653 0.3506
REMARK 3 10 2.9518 - 2.8500 0.99 5512 136 0.3059 0.3772
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 : 0.34
REMARK 3 B_SOL : 49.05
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.900
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.66770
REMARK 3 B22 (A**2) : 10.66770
REMARK 3 B33 (A**2) : -1.00630
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 : 0.011 14254
REMARK 3 ANGLE : 1.231 19520
REMARK 3 CHIRALITY : 0.079 2280
REMARK 3 PLANARITY : 0.005 2537
REMARK 3 DIHEDRAL : 13.889 4556
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 30:41 OR RESSEQ 43:99
REMARK 3 OR RESSEQ 101:164 OR RESSEQ 166:178 OR
REMARK 3 RESSEQ 180:182 OR RESSEQ 192:246 OR
REMARK 3 RESSEQ 248:315 OR RESSEQ 317:317 OR
REMARK 3 RESSEQ 320:346 OR RESSEQ 355:381 OR
REMARK 3 RESSEQ 383:402 OR RESSEQ 409:442 OR
REMARK 3 RESSEQ 448:475 OR RESSEQ 477:511)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 30:41 OR RESSEQ 43:99
REMARK 3 OR RESSEQ 101:164 OR RESSEQ 166:178 OR
REMARK 3 RESSEQ 180:182 OR RESSEQ 192:246 OR
REMARK 3 RESSEQ 248:315 OR RESSEQ 317:317 OR
REMARK 3 RESSEQ 320:346 OR RESSEQ 355:381 OR
REMARK 3 RESSEQ 383:402 OR RESSEQ 409:439 OR
REMARK 3 RESSEQ 448:475 OR RESSEQ 477:511)
REMARK 3 ATOM PAIRS NUMBER : 3148
REMARK 3 RMSD : 0.086
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 30:41 OR RESSEQ 43:99
REMARK 3 OR RESSEQ 101:164 OR RESSEQ 166:178 OR
REMARK 3 RESSEQ 180:182 OR RESSEQ 192:246 OR
REMARK 3 RESSEQ 248:315 OR RESSEQ 317:317 OR
REMARK 3 RESSEQ 320:346 OR RESSEQ 355:381 OR
REMARK 3 RESSEQ 383:402 OR RESSEQ 409:442 OR
REMARK 3 RESSEQ 448:475 OR RESSEQ 477:511)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 30:41 OR RESSEQ 43:99
REMARK 3 OR RESSEQ 101:164 OR RESSEQ 166:178 OR
REMARK 3 RESSEQ 180:182 OR RESSEQ 192:246 OR
REMARK 3 RESSEQ 248:295 OR RESSEQ 297:315 OR
REMARK 3 RESSEQ 317:317 OR RESSEQ 320:346 OR
REMARK 3 RESSEQ 355:381 OR RESSEQ 383:402 OR
REMARK 3 RESSEQ 409:412 OR RESSEQ 414:441 OR
REMARK 3 RESSEQ 448:475 OR RESSEQ 478:511)
REMARK 3 ATOM PAIRS NUMBER : 3117
REMARK 3 RMSD : 0.069
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 30:41 OR RESSEQ 43:99
REMARK 3 OR RESSEQ 101:164 OR RESSEQ 166:178 OR
REMARK 3 RESSEQ 180:182 OR RESSEQ 192:246 OR
REMARK 3 RESSEQ 248:315 OR RESSEQ 317:317 OR
REMARK 3 RESSEQ 320:346 OR RESSEQ 355:381 OR
REMARK 3 RESSEQ 383:402 OR RESSEQ 409:442 OR
REMARK 3 RESSEQ 448:475 OR RESSEQ 477:511)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 30:41 OR RESSEQ 43:57
REMARK 3 OR RESSEQ 59:88 OR RESSEQ 91:99 OR RESSEQ
REMARK 3 102:164 OR RESSEQ 166:178 OR RESSEQ 180:
REMARK 3 182 OR RESSEQ 192:246 OR RESSEQ 248:315
REMARK 3 OR RESSEQ 317:317 OR RESSEQ 320:346 OR
REMARK 3 RESSEQ 355:356 OR RESSEQ 358:372 OR
REMARK 3 RESSEQ 374:377 OR RESSEQ 387:399 OR
REMARK 3 RESSEQ 402:402 OR RESSEQ 409:424 OR
REMARK 3 RESSEQ 427:440 OR RESSEQ 448:475 OR
REMARK 3 RESSEQ 477:511)
REMARK 3 ATOM PAIRS NUMBER : 2723
REMARK 3 RMSD : 0.095
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3V9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069764.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979490
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55880
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.839
REMARK 200 RESOLUTION RANGE LOW (A) : 47.784
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.62600
REMARK 200 R SYM FOR SHELL (I) : 0.62600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3V9G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 22.5% PEG3350, 0.2 M
REMARK 280 AMMONIUM SULFATE, 0.1 M HEPES, PH 7.5, CRYOPROTECTANT: 25%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 128.34533
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 64.17267
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 96.25900
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 32.08633
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 160.43167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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: 4430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 SER A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 VAL A 12
REMARK 465 PRO A 13
REMARK 465 ARG A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 HIS A 17
REMARK 465 THR A 18
REMARK 465 GLY A 19
REMARK 465 ALA A 20
REMARK 465 GLY A 21
REMARK 465 LEU A 22
REMARK 465 GLN A 183
REMARK 465 GLN A 184
REMARK 465 PRO A 185
REMARK 465 ILE A 186
REMARK 465 SER A 187
REMARK 465 VAL A 188
REMARK 465 PRO A 189
REMARK 465 GLY A 316
REMARK 465 GLY A 512
REMARK 465 SER A 513
REMARK 465 ILE A 514
REMARK 465 VAL A 515
REMARK 465 GLY A 516
REMARK 465 GLN A 517
REMARK 465 GLN A 518
REMARK 465 PRO A 519
REMARK 465 PHE A 520
REMARK 465 GLY A 521
REMARK 465 GLY A 522
REMARK 465 ALA A 523
REMARK 465 ARG A 524
REMARK 465 ALA A 525
REMARK 465 SER A 526
REMARK 465 GLY A 527
REMARK 465 THR A 528
REMARK 465 ASN A 529
REMARK 465 ASP A 530
REMARK 465 LYS A 531
REMARK 465 PRO A 532
REMARK 465 GLY A 533
REMARK 465 GLY A 534
REMARK 465 PRO A 535
REMARK 465 HIS A 536
REMARK 465 TYR A 537
REMARK 465 GLN A 563
REMARK 465 MET B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 SER B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 VAL B 12
REMARK 465 PRO B 13
REMARK 465 ARG B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 HIS B 17
REMARK 465 THR B 18
REMARK 465 GLY B 19
REMARK 465 ALA B 20
REMARK 465 GLY B 21
REMARK 465 LEU B 22
REMARK 465 GLN B 183
REMARK 465 GLN B 184
REMARK 465 PRO B 185
REMARK 465 ILE B 186
REMARK 465 SER B 187
REMARK 465 VAL B 188
REMARK 465 PRO B 189
REMARK 465 GLY B 316
REMARK 465 PRO B 442
REMARK 465 ILE B 443
REMARK 465 MET B 444
REMARK 465 LYS B 445
REMARK 465 GLU B 446
REMARK 465 GLY B 512
REMARK 465 SER B 513
REMARK 465 ILE B 514
REMARK 465 VAL B 515
REMARK 465 GLY B 516
REMARK 465 GLN B 517
REMARK 465 GLN B 518
REMARK 465 PRO B 519
REMARK 465 PHE B 520
REMARK 465 GLY B 521
REMARK 465 GLY B 522
REMARK 465 ALA B 523
REMARK 465 ARG B 524
REMARK 465 ALA B 525
REMARK 465 SER B 526
REMARK 465 GLY B 527
REMARK 465 THR B 528
REMARK 465 ASN B 529
REMARK 465 ASP B 530
REMARK 465 LYS B 531
REMARK 465 PRO B 532
REMARK 465 GLY B 533
REMARK 465 GLY B 534
REMARK 465 PRO B 535
REMARK 465 HIS B 536
REMARK 465 TYR B 537
REMARK 465 MET C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 SER C 1
REMARK 465 HIS C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 SER C 8
REMARK 465 SER C 9
REMARK 465 GLY C 10
REMARK 465 LEU C 11
REMARK 465 VAL C 12
REMARK 465 PRO C 13
REMARK 465 ARG C 14
REMARK 465 GLY C 15
REMARK 465 SER C 16
REMARK 465 HIS C 17
REMARK 465 THR C 18
REMARK 465 GLY C 19
REMARK 465 ALA C 20
REMARK 465 GLY C 21
REMARK 465 LEU C 22
REMARK 465 ILE C 186
REMARK 465 SER C 187
REMARK 465 VAL C 188
REMARK 465 PRO C 189
REMARK 465 PRO C 190
REMARK 465 GLY C 316
REMARK 465 LEU C 413
REMARK 465 PRO C 442
REMARK 465 ILE C 443
REMARK 465 MET C 444
REMARK 465 LYS C 445
REMARK 465 GLY C 512
REMARK 465 SER C 513
REMARK 465 ILE C 514
REMARK 465 VAL C 515
REMARK 465 GLY C 516
REMARK 465 GLN C 517
REMARK 465 GLN C 518
REMARK 465 PRO C 519
REMARK 465 PHE C 520
REMARK 465 GLY C 521
REMARK 465 GLY C 522
REMARK 465 ALA C 523
REMARK 465 ARG C 524
REMARK 465 ALA C 525
REMARK 465 SER C 526
REMARK 465 GLY C 527
REMARK 465 THR C 528
REMARK 465 ASN C 529
REMARK 465 ASP C 530
REMARK 465 LYS C 531
REMARK 465 PRO C 532
REMARK 465 GLY C 533
REMARK 465 GLY C 534
REMARK 465 PRO C 535
REMARK 465 HIS C 536
REMARK 465 TYR C 537
REMARK 465 LYS C 552
REMARK 465 PRO C 553
REMARK 465 LEU C 554
REMARK 465 GLY C 555
REMARK 465 ASP C 556
REMARK 465 TRP C 557
REMARK 465 SER C 558
REMARK 465 TYR C 559
REMARK 465 ALA C 560
REMARK 465 TYR C 561
REMARK 465 MET C 562
REMARK 465 GLN C 563
REMARK 465 MET D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 SER D 1
REMARK 465 HIS D 2
REMARK 465 HIS D 3
REMARK 465 HIS D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 SER D 8
REMARK 465 SER D 9
REMARK 465 GLY D 10
REMARK 465 LEU D 11
REMARK 465 VAL D 12
REMARK 465 PRO D 13
REMARK 465 ARG D 14
REMARK 465 GLY D 15
REMARK 465 SER D 16
REMARK 465 HIS D 17
REMARK 465 THR D 18
REMARK 465 GLY D 19
REMARK 465 ALA D 20
REMARK 465 GLY D 21
REMARK 465 LEU D 22
REMARK 465 LYS D 58
REMARK 465 HIS D 89
REMARK 465 LYS D 90
REMARK 465 LEU D 101
REMARK 465 GLN D 184
REMARK 465 PRO D 185
REMARK 465 ILE D 186
REMARK 465 SER D 187
REMARK 465 VAL D 188
REMARK 465 PRO D 189
REMARK 465 GLY D 316
REMARK 465 LYS D 347
REMARK 465 PRO D 357
REMARK 465 SER D 373
REMARK 465 GLY D 378
REMARK 465 ASP D 379
REMARK 465 PRO D 380
REMARK 465 ALA D 381
REMARK 465 GLU D 382
REMARK 465 ASP D 383
REMARK 465 PHE D 384
REMARK 465 GLY D 385
REMARK 465 THR D 386
REMARK 465 ILE D 400
REMARK 465 LYS D 401
REMARK 465 VAL D 425
REMARK 465 GLY D 426
REMARK 465 GLU D 441
REMARK 465 PRO D 442
REMARK 465 ILE D 443
REMARK 465 MET D 444
REMARK 465 LYS D 445
REMARK 465 GLY D 512
REMARK 465 SER D 513
REMARK 465 ILE D 514
REMARK 465 VAL D 515
REMARK 465 GLY D 516
REMARK 465 GLN D 517
REMARK 465 GLN D 518
REMARK 465 PRO D 519
REMARK 465 PHE D 520
REMARK 465 GLY D 521
REMARK 465 GLY D 522
REMARK 465 ALA D 523
REMARK 465 ARG D 524
REMARK 465 ALA D 525
REMARK 465 SER D 526
REMARK 465 GLY D 527
REMARK 465 THR D 528
REMARK 465 ASN D 529
REMARK 465 ASP D 530
REMARK 465 LYS D 531
REMARK 465 PRO D 532
REMARK 465 GLY D 533
REMARK 465 GLY D 534
REMARK 465 PRO D 535
REMARK 465 HIS D 536
REMARK 465 TYR D 537
REMARK 465 GLN D 563
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 SER A 28 OG
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 GLN A 42 CG CD OE1 NE2
REMARK 470 ASP A 48 CG OD1 OD2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2
REMARK 470 SER A 76 OG
REMARK 470 LYS A 90 NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 SER A 100 OG
REMARK 470 LYS A 104 CG CD CE NZ
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 GLU A 115 CG CD OE1 OE2
REMARK 470 LYS A 119 NZ
REMARK 470 ILE A 121 CD1
REMARK 470 GLN A 126 CD OE1 NE2
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 ARG A 139 CZ NH1 NH2
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 GLU A 181 CG CD OE1 OE2
REMARK 470 SER A 191 OG
REMARK 470 ASN A 193 CG OD1 ND2
REMARK 470 GLU A 201 CG CD OE1 OE2
REMARK 470 GLU A 251 CG CD OE1 OE2
REMARK 470 ASP A 271 CG OD1 OD2
REMARK 470 LYS A 292 CE NZ
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 ARG A 325 NH1 NH2
REMARK 470 GLU A 370 CD OE1 OE2
REMARK 470 ARG A 374 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 376 CG CD CE NZ
REMARK 470 GLU A 382 CG CD OE1 OE2
REMARK 470 LYS A 395 CG CD CE NZ
REMARK 470 LYS A 401 CG CD CE NZ
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 GLU A 405 CG CD OE1 OE2
REMARK 470 LYS A 420 CG CD CE NZ
REMARK 470 ILE A 443 CG1 CG2 CD1
REMARK 470 LYS A 445 CG CD CE NZ
REMARK 470 GLU A 446 CG CD OE1 OE2
REMARK 470 SER A 454 OG
REMARK 470 ASP A 461 CG OD1 OD2
REMARK 470 LYS A 462 CG CD CE NZ
REMARK 470 LYS A 464 NZ
REMARK 470 SER A 475 OG
REMARK 470 ASP A 486 CG OD1 OD2
REMARK 470 LYS A 487 CG CD CE NZ
REMARK 470 ASP A 488 CG OD1 OD2
REMARK 470 GLN A 491 CG CD OE1 NE2
REMARK 470 LYS A 495 CG CD CE NZ
REMARK 470 LYS A 509 NZ
REMARK 470 ILE A 538 CG1 CG2 CD1
REMARK 470 ARG A 540 NE CZ NH1 NH2
REMARK 470 LYS A 548 CG CD CE NZ
REMARK 470 LYS A 552 CG CD CE NZ
REMARK 470 ASP A 556 CG OD1 OD2
REMARK 470 SER A 558 OG
REMARK 470 ARG B 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 SER B 28 OG
REMARK 470 SER B 29 OG
REMARK 470 LYS B 31 CG CD CE NZ
REMARK 470 GLN B 42 CG CD OE1 NE2
REMARK 470 ASP B 48 CG OD1 OD2
REMARK 470 GLN B 51 CG CD OE1 NE2
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 ASP B 56 CG OD1 OD2
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 ARG B 60 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 71 CG CD OE1 OE2
REMARK 470 THR B 75 OG1 CG2
REMARK 470 SER B 76 OG
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 LYS B 93 CE NZ
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 SER B 100 OG
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 LYS B 119 CE NZ
REMARK 470 ILE B 121 CD1
REMARK 470 GLN B 126 CG CD OE1 NE2
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 GLU B 165 CD OE1 OE2
REMARK 470 LYS B 175 NZ
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 GLU B 181 CG CD OE1 OE2
REMARK 470 SER B 191 OG
REMARK 470 ASN B 193 CG OD1 ND2
REMARK 470 GLU B 201 CG CD OE1 OE2
REMARK 470 ILE B 215 CD1
REMARK 470 ASP B 236 OD1 OD2
REMARK 470 GLU B 251 CG CD OE1 OE2
REMARK 470 ASP B 271 OD1 OD2
REMARK 470 SER B 275 OG
REMARK 470 LYS B 292 CE NZ
REMARK 470 GLN B 300 CG CD OE1 NE2
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 LYS B 318 CG CD CE NZ
REMARK 470 ARG B 325 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 328 CG OD1 OD2
REMARK 470 GLU B 330 CG CD OE1 OE2
REMARK 470 ARG B 353 NE CZ NH1 NH2
REMARK 470 ILE B 364 CG1 CG2 CD1
REMARK 470 LYS B 365 CG CD CE NZ
REMARK 470 ARG B 367 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 370 CG CD OE1 OE2
REMARK 470 ARG B 374 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 375 CD1
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 GLU B 382 CG CD OE1 OE2
REMARK 470 LYS B 395 CG CD CE NZ
REMARK 470 ARG B 399 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 401 CG CD CE NZ
REMARK 470 LYS B 402 CG CD CE NZ
REMARK 470 TRP B 403 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 403 CZ3 CH2
REMARK 470 GLU B 405 CG CD OE1 OE2
REMARK 470 HIS B 406 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 408 NE CZ NH1 NH2
REMARK 470 SER B 409 OG
REMARK 470 SER B 410 OG
REMARK 470 SER B 412 OG
REMARK 470 LEU B 413 CG CD1 CD2
REMARK 470 THR B 414 OG1 CG2
REMARK 470 ILE B 415 CD1
REMARK 470 LYS B 420 CG CD CE NZ
REMARK 470 GLU B 430 CG CD OE1 OE2
REMARK 470 GLU B 435 CD OE1 OE2
REMARK 470 SER B 436 OG
REMARK 470 LYS B 437 CG CD CE NZ
REMARK 470 GLN B 440 CG CD OE1 NE2
REMARK 470 GLU B 441 CG CD OE1 OE2
REMARK 470 GLU B 447 CG CD OE1 OE2
REMARK 470 ILE B 448 CG1 CG2 CD1
REMARK 470 LYS B 462 CE NZ
REMARK 470 LYS B 464 CE NZ
REMARK 470 GLN B 468 CD OE1 NE2
REMARK 470 SER B 472 OG
REMARK 470 THR B 473 OG1 CG2
REMARK 470 SER B 475 OG
REMARK 470 TYR B 476 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 485 CG CD OE1 NE2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 ASP B 488 CG OD1 OD2
REMARK 470 VAL B 489 CG1 CG2
REMARK 470 GLN B 491 CG CD OE1 NE2
REMARK 470 GLU B 492 OE1 OE2
REMARK 470 LYS B 495 CE NZ
REMARK 470 ILE B 506 CD1
REMARK 470 LYS B 509 NZ
REMARK 470 ARG B 540 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 548 CG CD CE NZ
REMARK 470 LYS B 552 CG CD CE NZ
REMARK 470 ASP B 556 CG OD1 OD2
REMARK 470 SER B 558 OG
REMARK 470 GLN B 563 CG CD OE1 NE2
REMARK 470 ARG C 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 25 CG CD CE NZ
REMARK 470 SER C 28 OG
REMARK 470 LYS C 31 CG CD CE NZ
REMARK 470 GLN C 42 CG CD OE1 NE2
REMARK 470 ASP C 48 CG OD1 OD2
REMARK 470 LYS C 52 CG CD CE NZ
REMARK 470 LYS C 55 CG CD CE NZ
REMARK 470 ASP C 56 CG OD1 OD2
REMARK 470 LEU C 57 CG CD1 CD2
REMARK 470 LYS C 58 CG CD CE NZ
REMARK 470 ARG C 60 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 62 CG CD OE1 OE2
REMARK 470 GLU C 71 CG CD OE1 OE2
REMARK 470 SER C 76 OG
REMARK 470 LYS C 90 CG CD CE NZ
REMARK 470 LYS C 93 CG CD CE NZ
REMARK 470 LYS C 99 CG CD CE NZ
REMARK 470 SER C 100 OG
REMARK 470 LYS C 104 CG CD CE NZ
REMARK 470 GLU C 107 CG CD OE1 OE2
REMARK 470 LYS C 114 CG CD CE NZ
REMARK 470 GLU C 115 CG CD OE1 OE2
REMARK 470 LYS C 153 NZ
REMARK 470 GLU C 179 CG CD OE1 OE2
REMARK 470 GLU C 181 OE1 OE2
REMARK 470 GLN C 183 OE1 NE2
REMARK 470 ASN C 193 CG OD1 ND2
REMARK 470 GLU C 201 CD OE1 OE2
REMARK 470 ASN C 211 CG OD1 ND2
REMARK 470 THR C 213 OG1 CG2
REMARK 470 ARG C 247 NE CZ NH1 NH2
REMARK 470 ASP C 271 OD1 OD2
REMARK 470 GLU C 277 CD OE1 OE2
REMARK 470 LYS C 292 CG CD CE NZ
REMARK 470 LYS C 296 CG CD CE NZ
REMARK 470 GLN C 300 CG CD OE1 NE2
REMARK 470 ASN C 301 CG OD1 ND2
REMARK 470 ASP C 303 CG OD1 OD2
REMARK 470 ARG C 304 NE CZ NH1 NH2
REMARK 470 THR C 307 OG1 CG2
REMARK 470 PHE C 308 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 314 CG CD OE1 OE2
REMARK 470 LYS C 318 CG CD CE NZ
REMARK 470 ARG C 325 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 329 CG1 CG2
REMARK 470 GLU C 330 CG CD OE1 OE2
REMARK 470 VAL C 333 CG1 CG2
REMARK 470 ARG C 353 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 356 CG1 CG2
REMARK 470 LEU C 360 CG CD1 CD2
REMARK 470 GLN C 363 CD OE1 NE2
REMARK 470 LYS C 365 CE NZ
REMARK 470 GLU C 370 OE1 OE2
REMARK 470 ARG C 374 NE CZ NH1 NH2
REMARK 470 LYS C 376 CG CD CE NZ
REMARK 470 GLU C 382 CG CD OE1 OE2
REMARK 470 LYS C 395 CG CD CE NZ
REMARK 470 ARG C 399 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 400 CG1 CG2 CD1
REMARK 470 LYS C 401 CG CD CE NZ
REMARK 470 LYS C 402 CG CD CE NZ
REMARK 470 TRP C 403 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 403 CZ3 CH2
REMARK 470 GLU C 405 CG CD OE1 OE2
REMARK 470 HIS C 406 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 408 CG CD NE CZ NH1 NH2
REMARK 470 SER C 410 OG
REMARK 470 THR C 414 OG1 CG2
REMARK 470 LYS C 420 CG CD CE NZ
REMARK 470 GLU C 430 CG CD OE1 OE2
REMARK 470 SER C 436 OG
REMARK 470 LYS C 437 CG CD CE NZ
REMARK 470 GLN C 440 CG CD OE1 NE2
REMARK 470 GLU C 441 CD OE1 OE2
REMARK 470 GLU C 446 CG CD OE1 OE2
REMARK 470 GLU C 447 CG CD OE1 OE2
REMARK 470 ILE C 448 CG1 CG2 CD1
REMARK 470 ASP C 461 CG OD1 OD2
REMARK 470 LYS C 462 CG CD CE NZ
REMARK 470 LYS C 464 CG CD CE NZ
REMARK 470 GLU C 465 CG CD OE1 OE2
REMARK 470 GLN C 468 CG CD OE1 NE2
REMARK 470 LEU C 469 CD1 CD2
REMARK 470 THR C 473 OG1 CG2
REMARK 470 SER C 475 OG
REMARK 470 VAL C 482 CG1 CG2
REMARK 470 ASP C 486 CG OD1 OD2
REMARK 470 LYS C 487 CG CD CE NZ
REMARK 470 ASP C 488 CG OD1 OD2
REMARK 470 GLN C 491 CG CD OE1 NE2
REMARK 470 GLU C 492 CG CD OE1 OE2
REMARK 470 LYS C 495 CG CD CE NZ
REMARK 470 ILE C 506 CD1
REMARK 470 LYS C 509 NZ
REMARK 470 ILE C 538 CG1 CG2 CD1
REMARK 470 LYS C 548 CG CD CE NZ
REMARK 470 HIS C 551 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 25 CG CD CE NZ
REMARK 470 HIS D 26 CG ND1 CD2 CE1 NE2
REMARK 470 THR D 27 OG1 CG2
REMARK 470 SER D 28 OG
REMARK 470 LYS D 31 CG CD CE NZ
REMARK 470 VAL D 37 CG1 CG2
REMARK 470 LEU D 38 CD1 CD2
REMARK 470 THR D 41 OG1 CG2
REMARK 470 GLN D 42 CG CD OE1 NE2
REMARK 470 ARG D 47 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 48 CG OD1 OD2
REMARK 470 LEU D 50 CG CD1 CD2
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 LEU D 54 CG CD1 CD2
REMARK 470 LYS D 55 CG CD CE NZ
REMARK 470 ASP D 56 CG OD1 OD2
REMARK 470 LEU D 57 CG CD1 CD2
REMARK 470 ARG D 60 CG CD NE CZ NH1 NH2
REMARK 470 MET D 61 CG SD CE
REMARK 470 GLU D 62 CG CD OE1 OE2
REMARK 470 ILE D 64 CG1 CG2 CD1
REMARK 470 VAL D 67 CG1 CG2
REMARK 470 ASP D 70 CG OD1 OD2
REMARK 470 GLU D 71 CG CD OE1 OE2
REMARK 470 GLU D 72 CG CD OE1 OE2
REMARK 470 VAL D 73 CG1 CG2
REMARK 470 THR D 75 OG1 CG2
REMARK 470 SER D 76 OG
REMARK 470 ASP D 77 CG OD1 OD2
REMARK 470 VAL D 78 CG1 CG2
REMARK 470 TYR D 80 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN D 81 CG CD OE1 NE2
REMARK 470 VAL D 82 CG1 CG2
REMARK 470 PHE D 85 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN D 86 CG OD1 ND2
REMARK 470 VAL D 91 CG1 CG2
REMARK 470 LYS D 93 CG CD CE NZ
REMARK 470 PHE D 94 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 98 CG OD1 OD2
REMARK 470 LYS D 99 CG CD CE NZ
REMARK 470 SER D 100 OG
REMARK 470 LEU D 102 CG CD1 CD2
REMARK 470 ASN D 103 CG OD1 ND2
REMARK 470 LYS D 104 CG CD CE NZ
REMARK 470 ILE D 106 CD1
REMARK 470 GLU D 107 CG CD OE1 OE2
REMARK 470 LYS D 114 CG CD CE NZ
REMARK 470 GLU D 115 CG CD OE1 OE2
REMARK 470 LYS D 119 CG CD CE NZ
REMARK 470 ILE D 121 CD1
REMARK 470 ASP D 123 CG OD1 OD2
REMARK 470 GLN D 126 CG CD OE1 NE2
REMARK 470 LYS D 130 CG CD CE NZ
REMARK 470 SER D 136 OG
REMARK 470 ARG D 139 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 144 CG CD1 CD2
REMARK 470 LYS D 146 CE NZ
REMARK 470 THR D 147 OG1 CG2
REMARK 470 MET D 148 CE
REMARK 470 VAL D 149 CG1 CG2
REMARK 470 GLN D 151 CG CD OE1 NE2
REMARK 470 LYS D 153 CG CD CE NZ
REMARK 470 THR D 154 OG1 CG2
REMARK 470 VAL D 155 CG1 CG2
REMARK 470 ILE D 156 CG1 CG2 CD1
REMARK 470 GLU D 159 CG CD OE1 OE2
REMARK 470 ASP D 161 CG OD1 OD2
REMARK 470 GLU D 165 CG CD OE1 OE2
REMARK 470 TYR D 176 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D 179 OE1 OE2
REMARK 470 GLU D 181 CG CD OE1 OE2
REMARK 470 SER D 191 OG
REMARK 470 ASN D 193 CG OD1 ND2
REMARK 470 SER D 194 OG
REMARK 470 GLU D 201 CD OE1 OE2
REMARK 470 THR D 213 OG1 CG2
REMARK 470 ILE D 215 CG1 CG2 CD1
REMARK 470 ASN D 218 CG OD1 ND2
REMARK 470 LEU D 240 CG CD1 CD2
REMARK 470 SER D 242 OG
REMARK 470 ARG D 247 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 249 CG CD1 CD2
REMARK 470 GLU D 251 CG CD OE1 OE2
REMARK 470 PHE D 269 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP D 271 CG OD1 OD2
REMARK 470 VAL D 273 CG1 CG2
REMARK 470 SER D 276 OG
REMARK 470 GLU D 277 CG CD OE1 OE2
REMARK 470 LYS D 292 CD CE NZ
REMARK 470 LEU D 294 CG CD1 CD2
REMARK 470 GLN D 297 CG CD OE1 NE2
REMARK 470 GLN D 300 CG CD OE1 NE2
REMARK 470 LEU D 302 CD1 CD2
REMARK 470 ASP D 303 CG OD1 OD2
REMARK 470 ARG D 304 CG CD NE CZ NH1 NH2
REMARK 470 HIS D 306 CG ND1 CD2 CE1 NE2
REMARK 470 THR D 307 OG1 CG2
REMARK 470 LEU D 311 CG CD1 CD2
REMARK 470 GLU D 314 CG CD OE1 OE2
REMARK 470 LYS D 318 CD CE NZ
REMARK 470 VAL D 323 CG1 CG2
REMARK 470 ARG D 325 CG CD NE CZ NH1 NH2
REMARK 470 SER D 326 OG
REMARK 470 VAL D 329 CG1 CG2
REMARK 470 GLU D 330 CG CD OE1 OE2
REMARK 470 SER D 331 OG
REMARK 470 VAL D 332 CG1 CG2
REMARK 470 VAL D 333 CG1 CG2
REMARK 470 THR D 336 OG1 CG2
REMARK 470 LEU D 337 CG CD1 CD2
REMARK 470 ARG D 338 CG CD NE CZ NH1 NH2
REMARK 470 SER D 339 OG
REMARK 470 PHE D 341 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 342 CG CD OE1 OE2
REMARK 470 CYS D 351 SG
REMARK 470 ARG D 353 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 356 CG1 CG2
REMARK 470 HIS D 358 CG ND1 CD2 CE1 NE2
REMARK 470 LEU D 360 CG CD1 CD2
REMARK 470 GLN D 363 CG CD OE1 NE2
REMARK 470 ILE D 364 CG1 CG2 CD1
REMARK 470 LYS D 365 CG CD CE NZ
REMARK 470 ARG D 367 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 368 CG CD1 CD2
REMARK 470 LEU D 369 CG CD1 CD2
REMARK 470 GLU D 370 CG CD OE1 OE2
REMARK 470 GLU D 371 CG CD OE1 OE2
REMARK 470 ARG D 374 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 375 CG1 CG2 CD1
REMARK 470 LYS D 376 CG CD CE NZ
REMARK 470 VAL D 377 CG1 CG2
REMARK 470 PHE D 387 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE D 388 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER D 389 OG
REMARK 470 VAL D 391 CG1 CG2
REMARK 470 ILE D 392 CG1 CG2 CD1
REMARK 470 ASP D 393 CG OD1 OD2
REMARK 470 LYS D 395 CG CD CE NZ
REMARK 470 PHE D 397 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 399 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 402 CG CD CE NZ
REMARK 470 TRP D 403 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 403 CZ3 CH2
REMARK 470 LEU D 404 CG CD1 CD2
REMARK 470 GLU D 405 CG CD OE1 OE2
REMARK 470 HIS D 406 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 408 CG CD NE CZ NH1 NH2
REMARK 470 SER D 409 OG
REMARK 470 SER D 410 OG
REMARK 470 SER D 412 OG
REMARK 470 LEU D 413 CG CD1 CD2
REMARK 470 ILE D 415 CD1
REMARK 470 LEU D 416 CG CD1 CD2
REMARK 470 LYS D 420 CG CD CE NZ
REMARK 470 ASP D 422 CG OD1 OD2
REMARK 470 PHE D 428 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 430 CG CD OE1 OE2
REMARK 470 CYS D 432 SG
REMARK 470 ILE D 433 CD1
REMARK 470 GLU D 435 CG CD OE1 OE2
REMARK 470 SER D 436 OG
REMARK 470 LYS D 437 CG CD CE NZ
REMARK 470 GLN D 440 CG CD OE1 NE2
REMARK 470 GLU D 446 CG CD OE1 OE2
REMARK 470 GLU D 447 CG CD OE1 OE2
REMARK 470 ILE D 448 CG1 CG2 CD1
REMARK 470 VAL D 452 CG1 CG2
REMARK 470 LEU D 453 CG CD1 CD2
REMARK 470 ASP D 460 CG OD1 OD2
REMARK 470 ASP D 461 CG OD1 OD2
REMARK 470 LYS D 462 CG CD CE NZ
REMARK 470 TYR D 463 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 464 CG CD CE NZ
REMARK 470 GLU D 465 CG CD OE1 OE2
REMARK 470 GLN D 468 CD OE1 NE2
REMARK 470 LEU D 469 CG CD1 CD2
REMARK 470 ASP D 471 CG OD1 OD2
REMARK 470 SER D 472 OG
REMARK 470 THR D 473 OG1 CG2
REMARK 470 SER D 475 OG
REMARK 470 TYR D 476 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL D 482 CG1 CG2
REMARK 470 GLN D 485 CG CD OE1 NE2
REMARK 470 ASP D 486 CG OD1 OD2
REMARK 470 LYS D 487 CG CD CE NZ
REMARK 470 ASP D 488 CG OD1 OD2
REMARK 470 VAL D 489 CG1 CG2
REMARK 470 VAL D 490 CG1 CG2
REMARK 470 GLN D 491 CG CD OE1 NE2
REMARK 470 LYS D 495 CG CD CE NZ
REMARK 470 LYS D 509 NZ
REMARK 470 LEU D 539 CD1 CD2
REMARK 470 ARG D 540 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 545 OE1 NE2
REMARK 470 VAL D 546 CG1 CG2
REMARK 470 LYS D 548 CE NZ
REMARK 470 LYS D 552 CG CD CE NZ
REMARK 470 ASP D 556 CG OD1 OD2
REMARK 470 TRP D 557 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 557 CZ3 CH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 371 CG GLU B 371 CD 0.104
REMARK 500 GLU B 371 CD GLU B 371 OE1 0.096
REMARK 500 GLU B 371 CD GLU B 371 OE2 0.082
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 140 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 304 NE - CZ - NH1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 304 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 LEU A 360 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 LEU A 360 CB - CG - CD1 ANGL. DEV. = 13.2 DEGREES
REMARK 500 LEU A 360 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG A 367 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 367 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 498 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG A 498 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 PRO A 544 C - N - CA ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 304 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 304 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU B 360 CB - CG - CD1 ANGL. DEV. = -10.3 DEGREES
REMARK 500 ARG B 498 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG B 498 NE - CZ - NH1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG B 498 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 PRO B 544 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG C 140 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG C 140 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU C 302 CB - CG - CD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG C 367 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG C 367 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG C 498 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG C 498 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG D 140 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG D 140 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG D 140 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG D 498 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG D 498 NE - CZ - NH1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG D 498 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 86 65.64 -157.10
REMARK 500 HIS A 87 2.17 -62.62
REMARK 500 ASP A 161 -77.33 -98.16
REMARK 500 ALA A 163 -98.45 -99.99
REMARK 500 ALA A 164 -59.95 -26.50
REMARK 500 GLU A 181 22.03 -73.38
REMARK 500 SER A 389 -146.22 -106.25
REMARK 500 SER A 410 135.44 -29.81
REMARK 500 CYS A 421 125.74 -175.43
REMARK 500 ILE A 448 -63.44 -108.73
REMARK 500 PHE A 449 31.34 70.77
REMARK 500 SER A 475 -60.33 -90.11
REMARK 500 SER A 510 33.41 -80.21
REMARK 500 TRP B 24 145.10 176.93
REMARK 500 SER B 29 -154.35 -120.71
REMARK 500 ASN B 86 72.99 -152.43
REMARK 500 ASP B 161 -80.55 -100.17
REMARK 500 ALA B 163 -96.38 -96.93
REMARK 500 ALA B 164 -71.83 -26.19
REMARK 500 GLU B 181 21.91 -69.92
REMARK 500 ALA B 238 12.98 -145.11
REMARK 500 SER B 389 -143.43 -105.99
REMARK 500 TRP B 403 37.59 -81.56
REMARK 500 LEU B 404 -42.31 -144.11
REMARK 500 GLU B 405 -83.14 -63.87
REMARK 500 HIS B 406 15.13 -57.96
REMARK 500 ALA B 407 -61.61 -100.15
REMARK 500 ARG B 408 4.77 -50.85
REMARK 500 SER B 409 -61.79 -102.31
REMARK 500 SER B 410 135.64 -32.03
REMARK 500 CYS B 421 126.18 -177.56
REMARK 500 ILE B 448 -62.88 -95.40
REMARK 500 PHE B 449 30.57 72.06
REMARK 500 LEU B 478 -62.53 -91.25
REMARK 500 SER B 484 132.97 -173.09
REMARK 500 SER B 510 30.28 -75.82
REMARK 500 GLN C 42 -124.59 64.07
REMARK 500 ASN C 86 71.11 -153.33
REMARK 500 HIS C 87 0.96 -67.51
REMARK 500 ASP C 161 -78.45 -101.50
REMARK 500 ALA C 163 -96.49 -97.37
REMARK 500 ALA C 164 -63.37 -28.42
REMARK 500 GLU C 181 21.65 -74.71
REMARK 500 SER C 389 -147.76 -107.94
REMARK 500 TRP C 403 38.18 -79.07
REMARK 500 LEU C 404 -26.01 -166.15
REMARK 500 SER C 409 -63.47 -108.91
REMARK 500 SER C 410 135.61 -33.95
REMARK 500 CYS C 421 128.76 -176.22
REMARK 500 ILE C 448 -65.73 -96.67
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3V9G RELATED DB: PDB
REMARK 900 HUMAN 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE
REMARK 900 RELATED ID: 3V9H RELATED DB: PDB
REMARK 900 HUMAN 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE MUTANT S352A
REMARK 900 RELATED ID: 3V9J RELATED DB: PDB
REMARK 900 MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE COMPLEXED WITH
REMARK 900 SULFATE ION
REMARK 900 RELATED ID: 3V9K RELATED DB: PDB
REMARK 900 MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE COMPLEXED WITH THE
REMARK 900 PRODUCT GLUTAMATE
REMARK 900 RELATED ID: 3V9L RELATED DB: PDB
REMARK 900 MOUSE 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE COMPLEXED WITH NAD+
DBREF 3V9I A 18 563 UNP P30038 AL4A1_HUMAN 18 563
DBREF 3V9I B 18 563 UNP P30038 AL4A1_HUMAN 18 563
DBREF 3V9I C 18 563 UNP P30038 AL4A1_HUMAN 18 563
DBREF 3V9I D 18 563 UNP P30038 AL4A1_HUMAN 18 563
SEQADV 3V9I MET A -2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY A -1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER A 0 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER A 1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 3 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 4 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 5 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 6 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 7 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER A 8 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER A 9 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY A 10 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU A 11 UNP P30038 EXPRESSION TAG
SEQADV 3V9I VAL A 12 UNP P30038 EXPRESSION TAG
SEQADV 3V9I PRO A 13 UNP P30038 EXPRESSION TAG
SEQADV 3V9I ARG A 14 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY A 15 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER A 16 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS A 17 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU A 352 UNP P30038 SER 352 ENGINEERED MUTATION
SEQADV 3V9I MET B -2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY B -1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER B 0 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER B 1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 3 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 4 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 5 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 6 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 7 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER B 8 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER B 9 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY B 10 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU B 11 UNP P30038 EXPRESSION TAG
SEQADV 3V9I VAL B 12 UNP P30038 EXPRESSION TAG
SEQADV 3V9I PRO B 13 UNP P30038 EXPRESSION TAG
SEQADV 3V9I ARG B 14 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY B 15 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER B 16 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS B 17 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU B 352 UNP P30038 SER 352 ENGINEERED MUTATION
SEQADV 3V9I MET C -2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY C -1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER C 0 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER C 1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 3 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 4 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 5 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 6 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 7 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER C 8 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER C 9 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY C 10 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU C 11 UNP P30038 EXPRESSION TAG
SEQADV 3V9I VAL C 12 UNP P30038 EXPRESSION TAG
SEQADV 3V9I PRO C 13 UNP P30038 EXPRESSION TAG
SEQADV 3V9I ARG C 14 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY C 15 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER C 16 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS C 17 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU C 352 UNP P30038 SER 352 ENGINEERED MUTATION
SEQADV 3V9I MET D -2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY D -1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER D 0 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER D 1 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 2 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 3 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 4 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 5 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 6 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 7 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER D 8 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER D 9 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY D 10 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU D 11 UNP P30038 EXPRESSION TAG
SEQADV 3V9I VAL D 12 UNP P30038 EXPRESSION TAG
SEQADV 3V9I PRO D 13 UNP P30038 EXPRESSION TAG
SEQADV 3V9I ARG D 14 UNP P30038 EXPRESSION TAG
SEQADV 3V9I GLY D 15 UNP P30038 EXPRESSION TAG
SEQADV 3V9I SER D 16 UNP P30038 EXPRESSION TAG
SEQADV 3V9I HIS D 17 UNP P30038 EXPRESSION TAG
SEQADV 3V9I LEU D 352 UNP P30038 SER 352 ENGINEERED MUTATION
SEQRES 1 A 566 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 566 LEU VAL PRO ARG GLY SER HIS THR GLY ALA GLY LEU ARG
SEQRES 3 A 566 TRP LYS HIS THR SER SER LEU LYS VAL ALA ASN GLU PRO
SEQRES 4 A 566 VAL LEU ALA PHE THR GLN GLY SER PRO GLU ARG ASP ALA
SEQRES 5 A 566 LEU GLN LYS ALA LEU LYS ASP LEU LYS GLY ARG MET GLU
SEQRES 6 A 566 ALA ILE PRO CYS VAL VAL GLY ASP GLU GLU VAL TRP THR
SEQRES 7 A 566 SER ASP VAL GLN TYR GLN VAL SER PRO PHE ASN HIS GLY
SEQRES 8 A 566 HIS LYS VAL ALA LYS PHE CYS TYR ALA ASP LYS SER LEU
SEQRES 9 A 566 LEU ASN LYS ALA ILE GLU ALA ALA LEU ALA ALA ARG LYS
SEQRES 10 A 566 GLU TRP ASP LEU LYS PRO ILE ALA ASP ARG ALA GLN ILE
SEQRES 11 A 566 PHE LEU LYS ALA ALA ASP MET LEU SER GLY PRO ARG ARG
SEQRES 12 A 566 ALA GLU ILE LEU ALA LYS THR MET VAL GLY GLN GLY LYS
SEQRES 13 A 566 THR VAL ILE GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU
SEQRES 14 A 566 ILE ASP PHE PHE ARG PHE ASN ALA LYS TYR ALA VAL GLU
SEQRES 15 A 566 LEU GLU GLY GLN GLN PRO ILE SER VAL PRO PRO SER THR
SEQRES 16 A 566 ASN SER THR VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA
SEQRES 17 A 566 ALA ILE SER PRO PHE ASN PHE THR ALA ILE GLY GLY ASN
SEQRES 18 A 566 LEU ALA GLY ALA PRO ALA LEU MET GLY ASN VAL VAL LEU
SEQRES 19 A 566 TRP LYS PRO SER ASP THR ALA MET LEU ALA SER TYR ALA
SEQRES 20 A 566 VAL TYR ARG ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN
SEQRES 21 A 566 ILE ILE GLN PHE VAL PRO ALA ASP GLY PRO LEU PHE GLY
SEQRES 22 A 566 ASP THR VAL THR SER SER GLU HIS LEU CYS GLY ILE ASN
SEQRES 23 A 566 PHE THR GLY SER VAL PRO THR PHE LYS HIS LEU TRP LYS
SEQRES 24 A 566 GLN VAL ALA GLN ASN LEU ASP ARG PHE HIS THR PHE PRO
SEQRES 25 A 566 ARG LEU ALA GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE
SEQRES 26 A 566 VAL HIS ARG SER ALA ASP VAL GLU SER VAL VAL SER GLY
SEQRES 27 A 566 THR LEU ARG SER ALA PHE GLU TYR GLY GLY GLN LYS CYS
SEQRES 28 A 566 SER ALA CYS LEU ARG LEU TYR VAL PRO HIS SER LEU TRP
SEQRES 29 A 566 PRO GLN ILE LYS GLY ARG LEU LEU GLU GLU HIS SER ARG
SEQRES 30 A 566 ILE LYS VAL GLY ASP PRO ALA GLU ASP PHE GLY THR PHE
SEQRES 31 A 566 PHE SER ALA VAL ILE ASP ALA LYS SER PHE ALA ARG ILE
SEQRES 32 A 566 LYS LYS TRP LEU GLU HIS ALA ARG SER SER PRO SER LEU
SEQRES 33 A 566 THR ILE LEU ALA GLY GLY LYS CYS ASP ASP SER VAL GLY
SEQRES 34 A 566 TYR PHE VAL GLU PRO CYS ILE VAL GLU SER LYS ASP PRO
SEQRES 35 A 566 GLN GLU PRO ILE MET LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES 36 A 566 LEU SER VAL TYR VAL TYR PRO ASP ASP LYS TYR LYS GLU
SEQRES 37 A 566 THR LEU GLN LEU VAL ASP SER THR THR SER TYR GLY LEU
SEQRES 38 A 566 THR GLY ALA VAL PHE SER GLN ASP LYS ASP VAL VAL GLN
SEQRES 39 A 566 GLU ALA THR LYS VAL LEU ARG ASN ALA ALA GLY ASN PHE
SEQRES 40 A 566 TYR ILE ASN ASP LYS SER THR GLY SER ILE VAL GLY GLN
SEQRES 41 A 566 GLN PRO PHE GLY GLY ALA ARG ALA SER GLY THR ASN ASP
SEQRES 42 A 566 LYS PRO GLY GLY PRO HIS TYR ILE LEU ARG TRP THR SER
SEQRES 43 A 566 PRO GLN VAL ILE LYS GLU THR HIS LYS PRO LEU GLY ASP
SEQRES 44 A 566 TRP SER TYR ALA TYR MET GLN
SEQRES 1 B 566 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 566 LEU VAL PRO ARG GLY SER HIS THR GLY ALA GLY LEU ARG
SEQRES 3 B 566 TRP LYS HIS THR SER SER LEU LYS VAL ALA ASN GLU PRO
SEQRES 4 B 566 VAL LEU ALA PHE THR GLN GLY SER PRO GLU ARG ASP ALA
SEQRES 5 B 566 LEU GLN LYS ALA LEU LYS ASP LEU LYS GLY ARG MET GLU
SEQRES 6 B 566 ALA ILE PRO CYS VAL VAL GLY ASP GLU GLU VAL TRP THR
SEQRES 7 B 566 SER ASP VAL GLN TYR GLN VAL SER PRO PHE ASN HIS GLY
SEQRES 8 B 566 HIS LYS VAL ALA LYS PHE CYS TYR ALA ASP LYS SER LEU
SEQRES 9 B 566 LEU ASN LYS ALA ILE GLU ALA ALA LEU ALA ALA ARG LYS
SEQRES 10 B 566 GLU TRP ASP LEU LYS PRO ILE ALA ASP ARG ALA GLN ILE
SEQRES 11 B 566 PHE LEU LYS ALA ALA ASP MET LEU SER GLY PRO ARG ARG
SEQRES 12 B 566 ALA GLU ILE LEU ALA LYS THR MET VAL GLY GLN GLY LYS
SEQRES 13 B 566 THR VAL ILE GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU
SEQRES 14 B 566 ILE ASP PHE PHE ARG PHE ASN ALA LYS TYR ALA VAL GLU
SEQRES 15 B 566 LEU GLU GLY GLN GLN PRO ILE SER VAL PRO PRO SER THR
SEQRES 16 B 566 ASN SER THR VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA
SEQRES 17 B 566 ALA ILE SER PRO PHE ASN PHE THR ALA ILE GLY GLY ASN
SEQRES 18 B 566 LEU ALA GLY ALA PRO ALA LEU MET GLY ASN VAL VAL LEU
SEQRES 19 B 566 TRP LYS PRO SER ASP THR ALA MET LEU ALA SER TYR ALA
SEQRES 20 B 566 VAL TYR ARG ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN
SEQRES 21 B 566 ILE ILE GLN PHE VAL PRO ALA ASP GLY PRO LEU PHE GLY
SEQRES 22 B 566 ASP THR VAL THR SER SER GLU HIS LEU CYS GLY ILE ASN
SEQRES 23 B 566 PHE THR GLY SER VAL PRO THR PHE LYS HIS LEU TRP LYS
SEQRES 24 B 566 GLN VAL ALA GLN ASN LEU ASP ARG PHE HIS THR PHE PRO
SEQRES 25 B 566 ARG LEU ALA GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE
SEQRES 26 B 566 VAL HIS ARG SER ALA ASP VAL GLU SER VAL VAL SER GLY
SEQRES 27 B 566 THR LEU ARG SER ALA PHE GLU TYR GLY GLY GLN LYS CYS
SEQRES 28 B 566 SER ALA CYS LEU ARG LEU TYR VAL PRO HIS SER LEU TRP
SEQRES 29 B 566 PRO GLN ILE LYS GLY ARG LEU LEU GLU GLU HIS SER ARG
SEQRES 30 B 566 ILE LYS VAL GLY ASP PRO ALA GLU ASP PHE GLY THR PHE
SEQRES 31 B 566 PHE SER ALA VAL ILE ASP ALA LYS SER PHE ALA ARG ILE
SEQRES 32 B 566 LYS LYS TRP LEU GLU HIS ALA ARG SER SER PRO SER LEU
SEQRES 33 B 566 THR ILE LEU ALA GLY GLY LYS CYS ASP ASP SER VAL GLY
SEQRES 34 B 566 TYR PHE VAL GLU PRO CYS ILE VAL GLU SER LYS ASP PRO
SEQRES 35 B 566 GLN GLU PRO ILE MET LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES 36 B 566 LEU SER VAL TYR VAL TYR PRO ASP ASP LYS TYR LYS GLU
SEQRES 37 B 566 THR LEU GLN LEU VAL ASP SER THR THR SER TYR GLY LEU
SEQRES 38 B 566 THR GLY ALA VAL PHE SER GLN ASP LYS ASP VAL VAL GLN
SEQRES 39 B 566 GLU ALA THR LYS VAL LEU ARG ASN ALA ALA GLY ASN PHE
SEQRES 40 B 566 TYR ILE ASN ASP LYS SER THR GLY SER ILE VAL GLY GLN
SEQRES 41 B 566 GLN PRO PHE GLY GLY ALA ARG ALA SER GLY THR ASN ASP
SEQRES 42 B 566 LYS PRO GLY GLY PRO HIS TYR ILE LEU ARG TRP THR SER
SEQRES 43 B 566 PRO GLN VAL ILE LYS GLU THR HIS LYS PRO LEU GLY ASP
SEQRES 44 B 566 TRP SER TYR ALA TYR MET GLN
SEQRES 1 C 566 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 566 LEU VAL PRO ARG GLY SER HIS THR GLY ALA GLY LEU ARG
SEQRES 3 C 566 TRP LYS HIS THR SER SER LEU LYS VAL ALA ASN GLU PRO
SEQRES 4 C 566 VAL LEU ALA PHE THR GLN GLY SER PRO GLU ARG ASP ALA
SEQRES 5 C 566 LEU GLN LYS ALA LEU LYS ASP LEU LYS GLY ARG MET GLU
SEQRES 6 C 566 ALA ILE PRO CYS VAL VAL GLY ASP GLU GLU VAL TRP THR
SEQRES 7 C 566 SER ASP VAL GLN TYR GLN VAL SER PRO PHE ASN HIS GLY
SEQRES 8 C 566 HIS LYS VAL ALA LYS PHE CYS TYR ALA ASP LYS SER LEU
SEQRES 9 C 566 LEU ASN LYS ALA ILE GLU ALA ALA LEU ALA ALA ARG LYS
SEQRES 10 C 566 GLU TRP ASP LEU LYS PRO ILE ALA ASP ARG ALA GLN ILE
SEQRES 11 C 566 PHE LEU LYS ALA ALA ASP MET LEU SER GLY PRO ARG ARG
SEQRES 12 C 566 ALA GLU ILE LEU ALA LYS THR MET VAL GLY GLN GLY LYS
SEQRES 13 C 566 THR VAL ILE GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU
SEQRES 14 C 566 ILE ASP PHE PHE ARG PHE ASN ALA LYS TYR ALA VAL GLU
SEQRES 15 C 566 LEU GLU GLY GLN GLN PRO ILE SER VAL PRO PRO SER THR
SEQRES 16 C 566 ASN SER THR VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA
SEQRES 17 C 566 ALA ILE SER PRO PHE ASN PHE THR ALA ILE GLY GLY ASN
SEQRES 18 C 566 LEU ALA GLY ALA PRO ALA LEU MET GLY ASN VAL VAL LEU
SEQRES 19 C 566 TRP LYS PRO SER ASP THR ALA MET LEU ALA SER TYR ALA
SEQRES 20 C 566 VAL TYR ARG ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN
SEQRES 21 C 566 ILE ILE GLN PHE VAL PRO ALA ASP GLY PRO LEU PHE GLY
SEQRES 22 C 566 ASP THR VAL THR SER SER GLU HIS LEU CYS GLY ILE ASN
SEQRES 23 C 566 PHE THR GLY SER VAL PRO THR PHE LYS HIS LEU TRP LYS
SEQRES 24 C 566 GLN VAL ALA GLN ASN LEU ASP ARG PHE HIS THR PHE PRO
SEQRES 25 C 566 ARG LEU ALA GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE
SEQRES 26 C 566 VAL HIS ARG SER ALA ASP VAL GLU SER VAL VAL SER GLY
SEQRES 27 C 566 THR LEU ARG SER ALA PHE GLU TYR GLY GLY GLN LYS CYS
SEQRES 28 C 566 SER ALA CYS LEU ARG LEU TYR VAL PRO HIS SER LEU TRP
SEQRES 29 C 566 PRO GLN ILE LYS GLY ARG LEU LEU GLU GLU HIS SER ARG
SEQRES 30 C 566 ILE LYS VAL GLY ASP PRO ALA GLU ASP PHE GLY THR PHE
SEQRES 31 C 566 PHE SER ALA VAL ILE ASP ALA LYS SER PHE ALA ARG ILE
SEQRES 32 C 566 LYS LYS TRP LEU GLU HIS ALA ARG SER SER PRO SER LEU
SEQRES 33 C 566 THR ILE LEU ALA GLY GLY LYS CYS ASP ASP SER VAL GLY
SEQRES 34 C 566 TYR PHE VAL GLU PRO CYS ILE VAL GLU SER LYS ASP PRO
SEQRES 35 C 566 GLN GLU PRO ILE MET LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES 36 C 566 LEU SER VAL TYR VAL TYR PRO ASP ASP LYS TYR LYS GLU
SEQRES 37 C 566 THR LEU GLN LEU VAL ASP SER THR THR SER TYR GLY LEU
SEQRES 38 C 566 THR GLY ALA VAL PHE SER GLN ASP LYS ASP VAL VAL GLN
SEQRES 39 C 566 GLU ALA THR LYS VAL LEU ARG ASN ALA ALA GLY ASN PHE
SEQRES 40 C 566 TYR ILE ASN ASP LYS SER THR GLY SER ILE VAL GLY GLN
SEQRES 41 C 566 GLN PRO PHE GLY GLY ALA ARG ALA SER GLY THR ASN ASP
SEQRES 42 C 566 LYS PRO GLY GLY PRO HIS TYR ILE LEU ARG TRP THR SER
SEQRES 43 C 566 PRO GLN VAL ILE LYS GLU THR HIS LYS PRO LEU GLY ASP
SEQRES 44 C 566 TRP SER TYR ALA TYR MET GLN
SEQRES 1 D 566 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 566 LEU VAL PRO ARG GLY SER HIS THR GLY ALA GLY LEU ARG
SEQRES 3 D 566 TRP LYS HIS THR SER SER LEU LYS VAL ALA ASN GLU PRO
SEQRES 4 D 566 VAL LEU ALA PHE THR GLN GLY SER PRO GLU ARG ASP ALA
SEQRES 5 D 566 LEU GLN LYS ALA LEU LYS ASP LEU LYS GLY ARG MET GLU
SEQRES 6 D 566 ALA ILE PRO CYS VAL VAL GLY ASP GLU GLU VAL TRP THR
SEQRES 7 D 566 SER ASP VAL GLN TYR GLN VAL SER PRO PHE ASN HIS GLY
SEQRES 8 D 566 HIS LYS VAL ALA LYS PHE CYS TYR ALA ASP LYS SER LEU
SEQRES 9 D 566 LEU ASN LYS ALA ILE GLU ALA ALA LEU ALA ALA ARG LYS
SEQRES 10 D 566 GLU TRP ASP LEU LYS PRO ILE ALA ASP ARG ALA GLN ILE
SEQRES 11 D 566 PHE LEU LYS ALA ALA ASP MET LEU SER GLY PRO ARG ARG
SEQRES 12 D 566 ALA GLU ILE LEU ALA LYS THR MET VAL GLY GLN GLY LYS
SEQRES 13 D 566 THR VAL ILE GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU
SEQRES 14 D 566 ILE ASP PHE PHE ARG PHE ASN ALA LYS TYR ALA VAL GLU
SEQRES 15 D 566 LEU GLU GLY GLN GLN PRO ILE SER VAL PRO PRO SER THR
SEQRES 16 D 566 ASN SER THR VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA
SEQRES 17 D 566 ALA ILE SER PRO PHE ASN PHE THR ALA ILE GLY GLY ASN
SEQRES 18 D 566 LEU ALA GLY ALA PRO ALA LEU MET GLY ASN VAL VAL LEU
SEQRES 19 D 566 TRP LYS PRO SER ASP THR ALA MET LEU ALA SER TYR ALA
SEQRES 20 D 566 VAL TYR ARG ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN
SEQRES 21 D 566 ILE ILE GLN PHE VAL PRO ALA ASP GLY PRO LEU PHE GLY
SEQRES 22 D 566 ASP THR VAL THR SER SER GLU HIS LEU CYS GLY ILE ASN
SEQRES 23 D 566 PHE THR GLY SER VAL PRO THR PHE LYS HIS LEU TRP LYS
SEQRES 24 D 566 GLN VAL ALA GLN ASN LEU ASP ARG PHE HIS THR PHE PRO
SEQRES 25 D 566 ARG LEU ALA GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE
SEQRES 26 D 566 VAL HIS ARG SER ALA ASP VAL GLU SER VAL VAL SER GLY
SEQRES 27 D 566 THR LEU ARG SER ALA PHE GLU TYR GLY GLY GLN LYS CYS
SEQRES 28 D 566 SER ALA CYS LEU ARG LEU TYR VAL PRO HIS SER LEU TRP
SEQRES 29 D 566 PRO GLN ILE LYS GLY ARG LEU LEU GLU GLU HIS SER ARG
SEQRES 30 D 566 ILE LYS VAL GLY ASP PRO ALA GLU ASP PHE GLY THR PHE
SEQRES 31 D 566 PHE SER ALA VAL ILE ASP ALA LYS SER PHE ALA ARG ILE
SEQRES 32 D 566 LYS LYS TRP LEU GLU HIS ALA ARG SER SER PRO SER LEU
SEQRES 33 D 566 THR ILE LEU ALA GLY GLY LYS CYS ASP ASP SER VAL GLY
SEQRES 34 D 566 TYR PHE VAL GLU PRO CYS ILE VAL GLU SER LYS ASP PRO
SEQRES 35 D 566 GLN GLU PRO ILE MET LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES 36 D 566 LEU SER VAL TYR VAL TYR PRO ASP ASP LYS TYR LYS GLU
SEQRES 37 D 566 THR LEU GLN LEU VAL ASP SER THR THR SER TYR GLY LEU
SEQRES 38 D 566 THR GLY ALA VAL PHE SER GLN ASP LYS ASP VAL VAL GLN
SEQRES 39 D 566 GLU ALA THR LYS VAL LEU ARG ASN ALA ALA GLY ASN PHE
SEQRES 40 D 566 TYR ILE ASN ASP LYS SER THR GLY SER ILE VAL GLY GLN
SEQRES 41 D 566 GLN PRO PHE GLY GLY ALA ARG ALA SER GLY THR ASN ASP
SEQRES 42 D 566 LYS PRO GLY GLY PRO HIS TYR ILE LEU ARG TRP THR SER
SEQRES 43 D 566 PRO GLN VAL ILE LYS GLU THR HIS LYS PRO LEU GLY ASP
SEQRES 44 D 566 TRP SER TYR ALA TYR MET GLN
HELIX 1 1 SER A 44 ASP A 56 1 13
HELIX 2 2 ASP A 98 LYS A 119 1 22
HELIX 3 3 PRO A 120 GLY A 137 1 18
HELIX 4 4 ARG A 139 GLY A 152 1 14
HELIX 5 5 THR A 154 ALA A 162 1 9
HELIX 6 6 ALA A 163 GLU A 179 1 17
HELIX 7 7 PHE A 212 MET A 226 1 15
HELIX 8 8 SER A 235 THR A 237 5 3
HELIX 9 9 ALA A 238 GLY A 253 1 16
HELIX 10 10 ASP A 265 SER A 275 1 11
HELIX 11 11 SER A 287 ASN A 301 1 15
HELIX 12 12 LEU A 302 PHE A 305 5 4
HELIX 13 13 ASP A 328 GLU A 342 1 15
HELIX 14 14 TYR A 343 GLN A 346 5 4
HELIX 15 15 LEU A 360 ILE A 375 1 16
HELIX 16 16 ASP A 393 SER A 410 1 18
HELIX 17 17 GLU A 441 LYS A 445 5 5
HELIX 18 18 PRO A 459 ASP A 461 5 3
HELIX 19 19 LYS A 462 SER A 472 1 11
HELIX 20 20 ASP A 486 LEU A 497 1 12
HELIX 21 21 ILE A 538 ARG A 540 5 3
HELIX 22 22 SER B 44 ASP B 56 1 13
HELIX 23 23 ASP B 98 LYS B 119 1 22
HELIX 24 24 PRO B 120 GLY B 137 1 18
HELIX 25 25 ARG B 139 GLY B 152 1 14
HELIX 26 26 THR B 154 ALA B 162 1 9
HELIX 27 27 ALA B 163 GLU B 181 1 19
HELIX 28 28 PHE B 212 MET B 226 1 15
HELIX 29 29 SER B 235 THR B 237 5 3
HELIX 30 30 ALA B 238 GLY B 253 1 16
HELIX 31 31 ASP B 265 SER B 275 1 11
HELIX 32 32 SER B 287 ASN B 301 1 15
HELIX 33 33 LEU B 302 PHE B 305 5 4
HELIX 34 34 ASP B 328 GLU B 342 1 15
HELIX 35 35 TYR B 343 GLN B 346 5 4
HELIX 36 36 LEU B 360 ARG B 374 1 15
HELIX 37 37 ASP B 393 HIS B 406 1 14
HELIX 38 38 PRO B 459 ASP B 461 5 3
HELIX 39 39 LYS B 462 SER B 472 1 11
HELIX 40 40 ASP B 486 LEU B 497 1 12
HELIX 41 41 ILE B 538 ARG B 540 5 3
HELIX 42 42 TYR B 559 GLN B 563 5 5
HELIX 43 43 SER C 44 ASP C 56 1 13
HELIX 44 44 ASP C 98 LYS C 119 1 22
HELIX 45 45 PRO C 120 GLY C 137 1 18
HELIX 46 46 ARG C 139 GLY C 152 1 14
HELIX 47 47 THR C 154 ALA C 162 1 9
HELIX 48 48 ALA C 163 GLU C 181 1 19
HELIX 49 49 PHE C 212 MET C 226 1 15
HELIX 50 50 SER C 235 THR C 237 5 3
HELIX 51 51 ALA C 238 GLY C 253 1 16
HELIX 52 52 ASP C 265 SER C 275 1 11
HELIX 53 53 SER C 287 ASN C 301 1 15
HELIX 54 54 LEU C 302 PHE C 305 5 4
HELIX 55 55 ASP C 328 GLU C 342 1 15
HELIX 56 56 TYR C 343 GLN C 346 5 4
HELIX 57 57 LEU C 360 ILE C 375 1 16
HELIX 58 58 ASP C 393 HIS C 406 1 14
HELIX 59 59 PRO C 459 ASP C 461 5 3
HELIX 60 60 LYS C 462 SER C 472 1 11
HELIX 61 61 ASP C 486 LEU C 497 1 12
HELIX 62 62 ARG C 498 ALA C 500 5 3
HELIX 63 63 ILE C 538 ARG C 540 5 3
HELIX 64 64 SER D 44 ASP D 56 1 13
HELIX 65 65 LYS D 99 SER D 100 5 2
HELIX 66 66 LEU D 102 LEU D 102 5 1
HELIX 67 67 ASN D 103 LYS D 119 1 17
HELIX 68 68 PRO D 120 GLY D 137 1 18
HELIX 69 69 ARG D 139 GLY D 152 1 14
HELIX 70 70 THR D 154 ALA D 162 1 9
HELIX 71 71 ALA D 163 GLU D 181 1 19
HELIX 72 72 PHE D 212 MET D 226 1 15
HELIX 73 73 SER D 235 THR D 237 5 3
HELIX 74 74 ALA D 238 GLY D 253 1 16
HELIX 75 75 ASP D 265 SER D 275 1 11
HELIX 76 76 SER D 287 ASN D 301 1 15
HELIX 77 77 LEU D 302 PHE D 305 5 4
HELIX 78 78 ASP D 328 GLU D 342 1 15
HELIX 79 79 TYR D 343 GLN D 346 5 4
HELIX 80 80 LEU D 360 HIS D 372 1 13
HELIX 81 81 ASP D 393 ARG D 399 1 7
HELIX 82 82 TRP D 403 SER D 410 1 8
HELIX 83 83 PRO D 459 ASP D 461 5 3
HELIX 84 84 LYS D 462 SER D 472 1 11
HELIX 85 85 ASP D 486 LEU D 497 1 12
HELIX 86 86 ARG D 498 ALA D 500 5 3
HELIX 87 87 ILE D 538 ARG D 540 5 3
SHEET 1 A 2 TRP A 24 LEU A 30 0
SHEET 2 A 2 TRP C 24 LEU C 30 -1 O LYS C 25 N SER A 29
SHEET 1 B 3 GLU A 62 ILE A 64 0
SHEET 2 B 3 ASN A 86 CYS A 95 1 O LYS A 93 N ILE A 64
SHEET 3 B 3 VAL A 78 SER A 83 -1 N GLN A 79 O PHE A 94
SHEET 1 C 2 CYS A 66 VAL A 68 0
SHEET 2 C 2 GLU A 71 VAL A 73 -1 O VAL A 73 N CYS A 66
SHEET 1 D 3 SER A 191 THR A 192 0
SHEET 2 D 3 THR A 542 THR A 550 -1 O GLU A 549 N THR A 192
SHEET 3 D 3 THR A 195 GLY A 199 -1 N VAL A 196 O GLN A 545
SHEET 1 E 9 SER A 191 THR A 192 0
SHEET 2 E 9 THR A 542 THR A 550 -1 O GLU A 549 N THR A 192
SHEET 3 E 9 ASN B 503 ILE B 506 1 O ILE B 506 N LYS A 548
SHEET 4 E 9 GLY B 477 PHE B 483 1 N GLY B 480 O TYR B 505
SHEET 5 E 9 LYS B 318 VAL B 323 1 N PHE B 322 O ALA B 481
SHEET 6 E 9 LEU B 352 PRO B 357 1 O TYR B 355 N HIS B 321
SHEET 7 E 9 VAL B 452 TYR B 458 1 O SER B 454 N LEU B 354
SHEET 8 E 9 CYS B 432 SER B 436 1 N VAL B 434 O VAL B 455
SHEET 9 E 9 LEU B 413 ALA B 417 -1 N LEU B 416 O ILE B 433
SHEET 1 F 5 ILE A 259 PHE A 261 0
SHEET 2 F 5 VAL A 229 LYS A 233 1 N VAL A 230 O GLN A 260
SHEET 3 F 5 PHE A 203 ILE A 207 1 N ALA A 206 O LYS A 233
SHEET 4 F 5 LEU A 279 THR A 285 1 O ASN A 283 N ALA A 205
SHEET 5 F 5 ARG A 310 GLU A 314 1 O ALA A 312 N PHE A 284
SHEET 1 G 9 LEU A 413 ALA A 417 0
SHEET 2 G 9 CYS A 432 SER A 436 -1 O ILE A 433 N LEU A 416
SHEET 3 G 9 VAL A 452 TYR A 458 1 O LEU A 453 N VAL A 434
SHEET 4 G 9 LEU A 352 PRO A 357 1 N LEU A 354 O SER A 454
SHEET 5 G 9 PHE A 320 VAL A 323 1 N HIS A 321 O TYR A 355
SHEET 6 G 9 THR A 479 PHE A 483 1 O ALA A 481 N PHE A 322
SHEET 7 G 9 ASN A 503 ILE A 506 1 O TYR A 505 N GLY A 480
SHEET 8 G 9 THR B 542 THR B 550 1 O THR B 550 N ILE A 506
SHEET 9 G 9 SER B 191 THR B 192 -1 N THR B 192 O GLU B 549
SHEET 1 H 9 LEU A 413 ALA A 417 0
SHEET 2 H 9 CYS A 432 SER A 436 -1 O ILE A 433 N LEU A 416
SHEET 3 H 9 VAL A 452 TYR A 458 1 O LEU A 453 N VAL A 434
SHEET 4 H 9 LEU A 352 PRO A 357 1 N LEU A 354 O SER A 454
SHEET 5 H 9 PHE A 320 VAL A 323 1 N HIS A 321 O TYR A 355
SHEET 6 H 9 THR A 479 PHE A 483 1 O ALA A 481 N PHE A 322
SHEET 7 H 9 ASN A 503 ILE A 506 1 O TYR A 505 N GLY A 480
SHEET 8 H 9 THR B 542 THR B 550 1 O THR B 550 N ILE A 506
SHEET 9 H 9 THR B 195 GLY B 199 -1 N ARG B 198 O SER B 543
SHEET 1 I 2 CYS A 421 ASP A 422 0
SHEET 2 I 2 PHE A 428 VAL A 429 -1 O PHE A 428 N ASP A 422
SHEET 1 J 2 TRP B 24 VAL B 32 0
SHEET 2 J 2 TRP D 24 VAL D 32 -1 O LYS D 31 N LYS B 25
SHEET 1 K 3 GLU B 62 ILE B 64 0
SHEET 2 K 3 ASN B 86 CYS B 95 1 O LYS B 93 N ILE B 64
SHEET 3 K 3 VAL B 78 SER B 83 -1 N GLN B 79 O PHE B 94
SHEET 1 L 2 CYS B 66 VAL B 68 0
SHEET 2 L 2 GLU B 71 VAL B 73 -1 O VAL B 73 N CYS B 66
SHEET 1 M 5 ILE B 259 PHE B 261 0
SHEET 2 M 5 VAL B 229 LYS B 233 1 N VAL B 230 O GLN B 260
SHEET 3 M 5 PHE B 203 ILE B 207 1 N VAL B 204 O VAL B 229
SHEET 4 M 5 LEU B 279 THR B 285 1 O ASN B 283 N ALA B 205
SHEET 5 M 5 ARG B 310 GLU B 314 1 O ALA B 312 N PHE B 284
SHEET 1 N 2 CYS B 421 ASP B 422 0
SHEET 2 N 2 PHE B 428 VAL B 429 -1 O PHE B 428 N ASP B 422
SHEET 1 O 3 GLU C 62 ILE C 64 0
SHEET 2 O 3 ASN C 86 CYS C 95 1 O LYS C 93 N ILE C 64
SHEET 3 O 3 VAL C 78 SER C 83 -1 N GLN C 79 O PHE C 94
SHEET 1 P 2 CYS C 66 VAL C 68 0
SHEET 2 P 2 GLU C 71 VAL C 73 -1 O VAL C 73 N CYS C 66
SHEET 1 Q 9 THR C 195 GLY C 199 0
SHEET 2 Q 9 THR C 542 GLU C 549 -1 O SER C 543 N ARG C 198
SHEET 3 Q 9 ASN D 503 ILE D 506 1 O PHE D 504 N VAL C 546
SHEET 4 Q 9 THR D 479 PHE D 483 1 N GLY D 480 O TYR D 505
SHEET 5 Q 9 PHE D 320 VAL D 323 1 N PHE D 322 O PHE D 483
SHEET 6 Q 9 ARG D 353 VAL D 356 1 O TYR D 355 N VAL D 323
SHEET 7 Q 9 VAL D 452 VAL D 457 1 O SER D 454 N LEU D 354
SHEET 8 Q 9 CYS D 432 SER D 436 1 N VAL D 434 O VAL D 455
SHEET 9 Q 9 LEU D 413 ALA D 417 -1 N LEU D 416 O ILE D 433
SHEET 1 R 5 ILE C 259 PHE C 261 0
SHEET 2 R 5 VAL C 229 LYS C 233 1 N VAL C 230 O GLN C 260
SHEET 3 R 5 PHE C 203 ILE C 207 1 N ALA C 206 O LYS C 233
SHEET 4 R 5 LEU C 279 THR C 285 1 O ASN C 283 N ALA C 205
SHEET 5 R 5 ARG C 310 GLU C 314 1 O ALA C 312 N PHE C 284
SHEET 1 S 9 ILE C 415 ALA C 417 0
SHEET 2 S 9 CYS C 432 SER C 436 -1 O ILE C 433 N LEU C 416
SHEET 3 S 9 VAL C 452 TYR C 458 1 O VAL C 455 N VAL C 434
SHEET 4 S 9 LEU C 352 PRO C 357 1 N LEU C 354 O SER C 454
SHEET 5 S 9 LYS C 318 VAL C 323 1 N HIS C 321 O ARG C 353
SHEET 6 S 9 GLY C 477 PHE C 483 1 O ALA C 481 N PHE C 322
SHEET 7 S 9 ASN C 503 ILE C 506 1 O TYR C 505 N GLY C 480
SHEET 8 S 9 THR D 542 THR D 550 1 O LYS D 548 N PHE C 504
SHEET 9 S 9 SER D 191 GLY D 199 -1 N THR D 192 O GLU D 549
SHEET 1 T 2 CYS C 421 ASP C 422 0
SHEET 2 T 2 PHE C 428 VAL C 429 -1 O PHE C 428 N ASP C 422
SHEET 1 U 4 GLU D 62 ILE D 64 0
SHEET 2 U 4 ALA D 92 CYS D 95 1 O LYS D 93 N ILE D 64
SHEET 3 U 4 VAL D 78 SER D 83 -1 N GLN D 79 O PHE D 94
SHEET 4 U 4 ASN D 86 GLY D 88 -1 O ASN D 86 N SER D 83
SHEET 1 V 2 CYS D 66 VAL D 68 0
SHEET 2 V 2 GLU D 71 VAL D 73 -1 O VAL D 73 N CYS D 66
SHEET 1 W 5 ILE D 259 PHE D 261 0
SHEET 2 W 5 VAL D 229 LYS D 233 1 N VAL D 230 O GLN D 260
SHEET 3 W 5 PHE D 203 ILE D 207 1 N ALA D 206 O LYS D 233
SHEET 4 W 5 LEU D 279 THR D 285 1 O ASN D 283 N ALA D 205
SHEET 5 W 5 ARG D 310 GLU D 314 1 O ALA D 312 N PHE D 284
SHEET 1 X 2 CYS D 421 ASP D 422 0
SHEET 2 X 2 PHE D 428 VAL D 429 -1 O PHE D 428 N ASP D 422
CISPEP 1 GLN C 42 GLY C 43 0 -20.23
CRYST1 150.382 150.382 192.518 90.00 90.00 120.00 P 65 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 0.006650 0.003839 0.000000 0.00000
SCALE2 0.000000 0.007678 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005194 0.00000
MTRIX1 1 0.730852 0.682223 -0.020671 -32.81300 1
MTRIX2 1 0.682150 -0.731122 -0.011490 89.49550 1
MTRIX3 1 -0.022952 -0.005703 -0.999720 180.10201 1
MTRIX1 2 -0.709288 -0.681042 -0.181915 135.43900 1
MTRIX2 2 -0.659364 0.549712 0.512890 10.10130 1
MTRIX3 2 -0.249299 0.483735 -0.838958 144.81400 1
MTRIX1 3 -0.959486 -0.133748 0.247987 68.79490 1
MTRIX2 3 -0.005592 -0.870937 -0.491363 173.11301 1
MTRIX3 3 0.281700 -0.472843 0.834904 32.13070 1
(ATOM LINES ARE NOT SHOWN.)
END