HEADER OXIDOREDUCTASE 10-MAR-12 4E3X
TITLE CRYSTAL STRUCTURE OF MUS MUSCULUS 1-PYRROLINE-5-CARBOXYLATE
TITLE 2 DEHYDROGENASE CRYOPROTECTED IN PROLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: P5C DEHYDROGENASE, ALDEHYDE DEHYDROGENASE FAMILY 4 MEMBER
COMPND 6 A1;
COMPND 7 EC: 1.5.1.12;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ALDH4A1;
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;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS AMINO ACID METABOLISM, PROLINE INHIBITION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.TANNER,T.A.PEMBERTON
REVDAT 3 13-SEP-23 4E3X 1 REMARK SEQADV
REVDAT 2 29-AUG-12 4E3X 1 JRNL
REVDAT 1 25-JUL-12 4E3X 0
JRNL AUTH T.A.PEMBERTON,B.R.STILL,E.M.CHRISTENSEN,H.SINGH,
JRNL AUTH 2 D.SRIVASTAVA,J.J.TANNER
JRNL TITL PROLINE: MOTHER NATURE'S CRYOPROTECTANT APPLIED TO PROTEIN
JRNL TITL 2 CRYSTALLOGRAPHY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 68 1010 2012
JRNL REFN ISSN 0907-4449
JRNL PMID 22868767
JRNL DOI 10.1107/S0907444912019580
REMARK 2
REMARK 2 RESOLUTION. 1.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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) : 1.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 279273
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 14042
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 40.4793 - 3.8551 0.97 9621 517 0.1652 0.1746
REMARK 3 2 3.8551 - 3.0602 0.99 9505 525 0.1530 0.1638
REMARK 3 3 3.0602 - 2.6735 0.99 9412 499 0.1617 0.1702
REMARK 3 4 2.6735 - 2.4291 0.98 9277 515 0.1502 0.1559
REMARK 3 5 2.4291 - 2.2550 0.97 9192 503 0.1377 0.1524
REMARK 3 6 2.2550 - 2.1220 0.97 9175 459 0.1331 0.1664
REMARK 3 7 2.1220 - 2.0158 0.97 9102 474 0.1387 0.1574
REMARK 3 8 2.0158 - 1.9280 0.97 9107 477 0.1342 0.1658
REMARK 3 9 1.9280 - 1.8538 0.96 9064 485 0.1311 0.1685
REMARK 3 10 1.8538 - 1.7898 0.96 9051 444 0.1253 0.1563
REMARK 3 11 1.7898 - 1.7339 0.96 9047 444 0.1205 0.1551
REMARK 3 12 1.7339 - 1.6843 0.96 9033 471 0.1183 0.1504
REMARK 3 13 1.6843 - 1.6400 0.95 8877 518 0.1157 0.1629
REMARK 3 14 1.6400 - 1.5999 0.95 8895 505 0.1167 0.1534
REMARK 3 15 1.5999 - 1.5636 0.95 8868 455 0.1171 0.1567
REMARK 3 16 1.5636 - 1.5303 0.94 8825 488 0.1156 0.1510
REMARK 3 17 1.5303 - 1.4997 0.94 8776 473 0.1195 0.1564
REMARK 3 18 1.4997 - 1.4714 0.94 8803 460 0.1271 0.1738
REMARK 3 19 1.4714 - 1.4451 0.94 8783 471 0.1406 0.1837
REMARK 3 20 1.4451 - 1.4206 0.93 8680 472 0.1504 0.2037
REMARK 3 21 1.4206 - 1.3977 0.93 8746 437 0.1551 0.1940
REMARK 3 22 1.3977 - 1.3762 0.93 8607 485 0.1700 0.2331
REMARK 3 23 1.3762 - 1.3559 0.92 8636 425 0.1848 0.2352
REMARK 3 24 1.3559 - 1.3368 0.92 8595 432 0.2140 0.2723
REMARK 3 25 1.3368 - 1.3188 0.91 8545 431 0.2356 0.2781
REMARK 3 26 1.3188 - 1.3017 0.91 8535 416 0.2674 0.3020
REMARK 3 27 1.3017 - 1.2854 0.90 8420 439 0.2977 0.3418
REMARK 3 28 1.2854 - 1.2699 0.90 8340 479 0.3545 0.3924
REMARK 3 29 1.2699 - 1.2551 0.89 8392 434 0.3819 0.4282
REMARK 3 30 1.2551 - 1.2400 0.78 7322 409 0.4309 0.4740
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 : 0.86
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 41.38
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.96170
REMARK 3 B22 (A**2) : 0.51540
REMARK 3 B33 (A**2) : 0.44670
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 : 0.005 8652
REMARK 3 ANGLE : 1.078 11801
REMARK 3 CHIRALITY : 0.073 1304
REMARK 3 PLANARITY : 0.006 1544
REMARK 3 DIHEDRAL : 12.106 3109
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4E3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071137.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.25
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-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924
REMARK 200 MONOCHROMATOR : NULL
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 : 279378
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.240
REMARK 200 RESOLUTION RANGE LOW (A) : 45.639
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : 0.55000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 3V9J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1 M BIS-TRIS, PH 6.25,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 42.49000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.20300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.93900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.20300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.49000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.93900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 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 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 GLN A 563
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
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 HIS A 20 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 25 CG CD CE NZ
REMARK 470 HIS A 26 CG ND1 CD2 CE1 NE2
REMARK 470 THR A 27 OG1 CG2
REMARK 470 SER A 28 OG
REMARK 470 LYS A 31 CE NZ
REMARK 470 GLN A 42 CD OE1 NE2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 LYS A 114 CG CD CE NZ
REMARK 470 LYS A 130 CG CD CE NZ
REMARK 470 GLU A 314 CG CD OE1 OE2
REMARK 470 GLU A 370 CG 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 402 CG CD CE NZ
REMARK 470 LYS A 462 CG CD CE NZ
REMARK 470 GLU A 465 CD OE1 OE2
REMARK 470 LYS A 468 CE NZ
REMARK 470 LYS A 552 CG CD CE NZ
REMARK 470 ASP A 556 CG OD1 OD2
REMARK 470 ARG A 558 CG CD NE CZ NH1 NH2
REMARK 470 SER B 19 OG
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 HIS B 26 CG ND1 CD2 CE1 NE2
REMARK 470 SER B 28 OG
REMARK 470 GLN B 42 CD OE1 NE2
REMARK 470 LYS B 52 CG CD CE NZ
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 GLN B 126 CG CD OE1 NE2
REMARK 470 LYS B 130 CG CD CE NZ
REMARK 470 ARG B 247 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 314 CG CD OE1 OE2
REMARK 470 LYS B 358 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 LYS B 376 CG CD CE NZ
REMARK 470 LYS B 395 CG CD CE NZ
REMARK 470 LYS B 401 CE NZ
REMARK 470 LYS B 402 CG CD CE NZ
REMARK 470 GLU B 405 CG CD OE1 OE2
REMARK 470 GLN B 440 CG CD OE1 NE2
REMARK 470 ARG B 464 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 LYS B 552 CE NZ
REMARK 470 ARG B 558 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 563 CG CD OE1 NE2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 HIS A 20
REMARK 475 LYS A 25
REMARK 475 HIS A 26
REMARK 475 THR A 27
REMARK 475 SER A 28
REMARK 475 SER A 29
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 99 CB
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 79.97 -154.63
REMARK 500 ASP A 161 -78.21 -100.16
REMARK 500 ALA A 163 -82.13 -95.92
REMARK 500 PRO A 190 41.06 -101.29
REMARK 500 SER A 389 -164.54 -117.83
REMARK 500 LEU A 478 -81.44 -91.94
REMARK 500 ALA A 523 -141.51 -103.69
REMARK 500 ARG A 524 -138.00 50.30
REMARK 500 ASN B 86 76.92 -157.30
REMARK 500 ASP B 161 -76.57 -100.31
REMARK 500 ALA B 163 -81.09 -94.40
REMARK 500 PRO B 190 35.17 -98.27
REMARK 500 SER B 389 -163.14 -117.96
REMARK 500 LEU B 478 -79.02 -91.03
REMARK 500 ALA B 523 -141.51 -103.83
REMARK 500 ARG B 524 -136.44 50.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 16P A 605
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16P A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E3U RELATED DB: PDB
REMARK 900 RELATED ID: 4E3V RELATED DB: PDB
REMARK 900 RELATED ID: 4E3W RELATED DB: PDB
DBREF 4E3X A 22 563 UNP Q8CHT0 AL4A1_MOUSE 21 562
DBREF 4E3X B 22 563 UNP Q8CHT0 AL4A1_MOUSE 21 562
SEQADV 4E3X MET A 1 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X GLY A 2 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER A 3 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER A 4 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 5 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 6 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 7 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 8 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 9 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 10 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER A 11 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER A 12 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X GLY A 13 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X LEU A 14 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X VAL A 15 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X PRO A 16 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X ARG A 17 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X GLY A 18 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER A 19 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS A 20 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X MET A 21 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X ALA A 33 UNP Q8CHT0 THR 32 CONFLICT
SEQADV 4E3X THR A 61 UNP Q8CHT0 MET 60 CONFLICT
SEQADV 4E3X LYS A 468 UNP Q8CHT0 GLN 467 CONFLICT
SEQADV 4E3X MET B 1 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X GLY B 2 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER B 3 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER B 4 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 5 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 6 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 7 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 8 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 9 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 10 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER B 11 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER B 12 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X GLY B 13 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X LEU B 14 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X VAL B 15 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X PRO B 16 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X ARG B 17 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X GLY B 18 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X SER B 19 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X HIS B 20 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X MET B 21 UNP Q8CHT0 EXPRESSION TAG
SEQADV 4E3X ALA B 33 UNP Q8CHT0 THR 32 CONFLICT
SEQADV 4E3X THR B 61 UNP Q8CHT0 MET 60 CONFLICT
SEQADV 4E3X LYS B 468 UNP Q8CHT0 GLN 467 CONFLICT
SEQRES 1 A 563 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 563 LEU VAL PRO ARG GLY SER HIS MET LEU ARG TRP LYS HIS
SEQRES 3 A 563 THR SER SER LEU LYS VAL ALA ASN GLU PRO ILE LEU ALA
SEQRES 4 A 563 PHE SER GLN GLY SER PRO GLU ARG ASP ALA LEU GLN LYS
SEQRES 5 A 563 ALA LEU LYS ASP LEU LYS GLY GLN THR GLU ALA ILE PRO
SEQRES 6 A 563 CYS VAL VAL GLY ASP GLU GLU VAL TRP THR SER ASP ILE
SEQRES 7 A 563 GLN TYR GLN LEU SER PRO PHE ASN HIS ALA HIS LYS VAL
SEQRES 8 A 563 ALA LYS PHE CYS TYR ALA ASP LYS ALA LEU LEU ASN ARG
SEQRES 9 A 563 ALA ILE ASP ALA ALA LEU ALA ALA ARG LYS GLU TRP ASP
SEQRES 10 A 563 LEU LYS PRO MET ALA ASP ARG ALA GLN VAL PHE LEU LYS
SEQRES 11 A 563 ALA ALA ASP MET LEU SER GLY PRO ARG ARG ALA GLU VAL
SEQRES 12 A 563 LEU ALA LYS THR MET VAL GLY GLN GLY LYS THR VAL ILE
SEQRES 13 A 563 GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU ILE ASP PHE
SEQRES 14 A 563 PHE ARG PHE ASN ALA LYS PHE ALA VAL GLU LEU GLU GLY
SEQRES 15 A 563 GLU GLN PRO ILE SER VAL PRO PRO SER THR ASN HIS THR
SEQRES 16 A 563 VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA ALA ILE SER
SEQRES 17 A 563 PRO PHE ASN PHE THR ALA ILE GLY GLY ASN LEU ALA GLY
SEQRES 18 A 563 ALA PRO ALA LEU MET GLY ASN VAL VAL LEU TRP LYS PRO
SEQRES 19 A 563 SER ASP THR ALA MET LEU ALA SER TYR ALA VAL TYR ARG
SEQRES 20 A 563 ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN ILE ILE GLN
SEQRES 21 A 563 PHE VAL PRO ALA ASP GLY PRO THR PHE GLY ASP THR VAL
SEQRES 22 A 563 THR SER SER GLU HIS LEU CYS GLY ILE ASN PHE THR GLY
SEQRES 23 A 563 SER VAL PRO THR PHE LYS HIS LEU TRP ARG GLN VAL ALA
SEQRES 24 A 563 GLN ASN LEU ASP ARG PHE ARG THR PHE PRO ARG LEU ALA
SEQRES 25 A 563 GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE VAL HIS SER
SEQRES 26 A 563 SER ALA ASP VAL ASP SER VAL VAL SER GLY THR LEU ARG
SEQRES 27 A 563 SER ALA PHE GLU TYR GLY GLY GLN LYS CYS SER ALA CYS
SEQRES 28 A 563 SER ARG LEU TYR VAL PRO LYS SER LEU TRP PRO GLN ILE
SEQRES 29 A 563 LYS GLY ARG LEU LEU GLU GLU HIS SER ARG ILE LYS VAL
SEQRES 30 A 563 GLY ASP PRO ALA GLU ASP PHE GLY THR PHE PHE SER ALA
SEQRES 31 A 563 VAL ILE ASP ALA LYS ALA PHE ALA ARG ILE LYS LYS TRP
SEQRES 32 A 563 LEU GLU HIS ALA ARG SER SER PRO SER LEU SER ILE LEU
SEQRES 33 A 563 ALA GLY GLY GLN CYS ASN GLU SER VAL GLY TYR TYR VAL
SEQRES 34 A 563 GLU PRO CYS ILE ILE GLU SER LYS ASP PRO GLN GLU PRO
SEQRES 35 A 563 ILE MET LYS GLU GLU ILE PHE GLY PRO VAL LEU THR VAL
SEQRES 36 A 563 TYR VAL TYR PRO ASP ASP LYS TYR ARG GLU THR LEU LYS
SEQRES 37 A 563 LEU VAL ASP SER THR THR SER TYR GLY LEU THR GLY ALA
SEQRES 38 A 563 VAL PHE ALA GLN ASP LYS ALA ILE VAL GLN GLU ALA THR
SEQRES 39 A 563 ARG MET LEU ARG ASN ALA ALA GLY ASN PHE TYR ILE ASN
SEQRES 40 A 563 ASP LYS SER THR GLY SER VAL VAL GLY GLN GLN PRO PHE
SEQRES 41 A 563 GLY GLY ALA ARG ALA SER GLY THR ASN ASP LYS PRO GLY
SEQRES 42 A 563 GLY PRO HIS TYR ILE LEU ARG TRP THR SER PRO GLN VAL
SEQRES 43 A 563 ILE LYS GLU THR HIS LYS PRO LEU GLY ASP TRP ARG TYR
SEQRES 44 A 563 SER TYR MET GLN
SEQRES 1 B 563 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 563 LEU VAL PRO ARG GLY SER HIS MET LEU ARG TRP LYS HIS
SEQRES 3 B 563 THR SER SER LEU LYS VAL ALA ASN GLU PRO ILE LEU ALA
SEQRES 4 B 563 PHE SER GLN GLY SER PRO GLU ARG ASP ALA LEU GLN LYS
SEQRES 5 B 563 ALA LEU LYS ASP LEU LYS GLY GLN THR GLU ALA ILE PRO
SEQRES 6 B 563 CYS VAL VAL GLY ASP GLU GLU VAL TRP THR SER ASP ILE
SEQRES 7 B 563 GLN TYR GLN LEU SER PRO PHE ASN HIS ALA HIS LYS VAL
SEQRES 8 B 563 ALA LYS PHE CYS TYR ALA ASP LYS ALA LEU LEU ASN ARG
SEQRES 9 B 563 ALA ILE ASP ALA ALA LEU ALA ALA ARG LYS GLU TRP ASP
SEQRES 10 B 563 LEU LYS PRO MET ALA ASP ARG ALA GLN VAL PHE LEU LYS
SEQRES 11 B 563 ALA ALA ASP MET LEU SER GLY PRO ARG ARG ALA GLU VAL
SEQRES 12 B 563 LEU ALA LYS THR MET VAL GLY GLN GLY LYS THR VAL ILE
SEQRES 13 B 563 GLN ALA GLU ILE ASP ALA ALA ALA GLU LEU ILE ASP PHE
SEQRES 14 B 563 PHE ARG PHE ASN ALA LYS PHE ALA VAL GLU LEU GLU GLY
SEQRES 15 B 563 GLU GLN PRO ILE SER VAL PRO PRO SER THR ASN HIS THR
SEQRES 16 B 563 VAL TYR ARG GLY LEU GLU GLY PHE VAL ALA ALA ILE SER
SEQRES 17 B 563 PRO PHE ASN PHE THR ALA ILE GLY GLY ASN LEU ALA GLY
SEQRES 18 B 563 ALA PRO ALA LEU MET GLY ASN VAL VAL LEU TRP LYS PRO
SEQRES 19 B 563 SER ASP THR ALA MET LEU ALA SER TYR ALA VAL TYR ARG
SEQRES 20 B 563 ILE LEU ARG GLU ALA GLY LEU PRO PRO ASN ILE ILE GLN
SEQRES 21 B 563 PHE VAL PRO ALA ASP GLY PRO THR PHE GLY ASP THR VAL
SEQRES 22 B 563 THR SER SER GLU HIS LEU CYS GLY ILE ASN PHE THR GLY
SEQRES 23 B 563 SER VAL PRO THR PHE LYS HIS LEU TRP ARG GLN VAL ALA
SEQRES 24 B 563 GLN ASN LEU ASP ARG PHE ARG THR PHE PRO ARG LEU ALA
SEQRES 25 B 563 GLY GLU CYS GLY GLY LYS ASN PHE HIS PHE VAL HIS SER
SEQRES 26 B 563 SER ALA ASP VAL ASP SER VAL VAL SER GLY THR LEU ARG
SEQRES 27 B 563 SER ALA PHE GLU TYR GLY GLY GLN LYS CYS SER ALA CYS
SEQRES 28 B 563 SER ARG LEU TYR VAL PRO LYS SER LEU TRP PRO GLN ILE
SEQRES 29 B 563 LYS GLY ARG LEU LEU GLU GLU HIS SER ARG ILE LYS VAL
SEQRES 30 B 563 GLY ASP PRO ALA GLU ASP PHE GLY THR PHE PHE SER ALA
SEQRES 31 B 563 VAL ILE ASP ALA LYS ALA PHE ALA ARG ILE LYS LYS TRP
SEQRES 32 B 563 LEU GLU HIS ALA ARG SER SER PRO SER LEU SER ILE LEU
SEQRES 33 B 563 ALA GLY GLY GLN CYS ASN GLU SER VAL GLY TYR TYR VAL
SEQRES 34 B 563 GLU PRO CYS ILE ILE GLU SER LYS ASP PRO GLN GLU PRO
SEQRES 35 B 563 ILE MET LYS GLU GLU ILE PHE GLY PRO VAL LEU THR VAL
SEQRES 36 B 563 TYR VAL TYR PRO ASP ASP LYS TYR ARG GLU THR LEU LYS
SEQRES 37 B 563 LEU VAL ASP SER THR THR SER TYR GLY LEU THR GLY ALA
SEQRES 38 B 563 VAL PHE ALA GLN ASP LYS ALA ILE VAL GLN GLU ALA THR
SEQRES 39 B 563 ARG MET LEU ARG ASN ALA ALA GLY ASN PHE TYR ILE ASN
SEQRES 40 B 563 ASP LYS SER THR GLY SER VAL VAL GLY GLN GLN PRO PHE
SEQRES 41 B 563 GLY GLY ALA ARG ALA SER GLY THR ASN ASP LYS PRO GLY
SEQRES 42 B 563 GLY PRO HIS TYR ILE LEU ARG TRP THR SER PRO GLN VAL
SEQRES 43 B 563 ILE LYS GLU THR HIS LYS PRO LEU GLY ASP TRP ARG TYR
SEQRES 44 B 563 SER TYR MET GLN
HET PRO A 601 8
HET PRO A 602 8
HET PRO A 603 8
HET PRO A 604 8
HET 16P A 605 19
HET PGE A 606 10
HET PRO B 601 8
HET PRO B 602 8
HET PRO B 603 8
HETNAM PRO PROLINE
HETNAM 16P 3,6,9,12,15,18-HEXAOXAICOSANE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 PRO 7(C5 H9 N O2)
FORMUL 7 16P C14 H30 O6
FORMUL 8 PGE C6 H14 O4
FORMUL 12 HOH *882(H2 O)
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 181 1 19
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 ALA A 252 1 15
HELIX 10 10 ASP A 265 THR A 274 1 10
HELIX 11 11 SER A 287 ASN A 301 1 15
HELIX 12 12 ASP A 328 GLU A 342 1 15
HELIX 13 13 TYR A 343 GLN A 346 5 4
HELIX 14 14 LEU A 360 ARG A 374 1 15
HELIX 15 15 ASP A 393 SER A 410 1 18
HELIX 16 16 GLU A 441 LYS A 445 5 5
HELIX 17 17 PRO A 459 ASP A 461 5 3
HELIX 18 18 LYS A 462 THR A 473 1 12
HELIX 19 19 ASP A 486 LEU A 497 1 12
HELIX 20 20 HIS A 536 THR A 542 5 7
HELIX 21 21 SER B 44 ASP B 56 1 13
HELIX 22 22 ASP B 98 LYS B 119 1 22
HELIX 23 23 PRO B 120 GLY B 137 1 18
HELIX 24 24 ARG B 139 GLY B 152 1 14
HELIX 25 25 THR B 154 ALA B 162 1 9
HELIX 26 26 ALA B 163 GLU B 181 1 19
HELIX 27 27 PHE B 212 MET B 226 1 15
HELIX 28 28 SER B 235 THR B 237 5 3
HELIX 29 29 ALA B 238 ALA B 252 1 15
HELIX 30 30 ASP B 265 SER B 275 1 11
HELIX 31 31 SER B 287 ASN B 301 1 15
HELIX 32 32 ASP B 328 GLU B 342 1 15
HELIX 33 33 TYR B 343 GLN B 346 5 4
HELIX 34 34 LEU B 360 SER B 373 1 14
HELIX 35 35 ASP B 393 SER B 410 1 18
HELIX 36 36 GLU B 441 LYS B 445 5 5
HELIX 37 37 PRO B 459 ASP B 461 5 3
HELIX 38 38 LYS B 462 THR B 473 1 12
HELIX 39 39 ASP B 486 LEU B 497 1 12
HELIX 40 40 HIS B 536 ARG B 540 5 5
HELIX 41 41 TYR B 559 GLN B 563 5 5
SHEET 1 A 3 GLU A 62 ALA A 63 0
SHEET 2 A 3 ASN A 86 CYS A 95 1 O LYS A 93 N GLU A 62
SHEET 3 A 3 ILE A 78 SER A 83 -1 N GLN A 79 O PHE A 94
SHEET 1 B 2 CYS A 66 VAL A 68 0
SHEET 2 B 2 GLU A 71 VAL A 73 -1 O VAL A 73 N CYS A 66
SHEET 1 C 9 SER A 191 VAL A 196 0
SHEET 2 C 9 GLN A 545 THR A 550 -1 O GLN A 545 N VAL A 196
SHEET 3 C 9 ASN B 503 ILE B 506 1 O ILE B 506 N LYS A 548
SHEET 4 C 9 THR B 479 PHE B 483 1 N VAL B 482 O TYR B 505
SHEET 5 C 9 ASN B 319 VAL B 323 1 N PHE B 322 O ALA B 481
SHEET 6 C 9 CYS B 351 PRO B 357 1 O TYR B 355 N HIS B 321
SHEET 7 C 9 VAL B 452 TYR B 458 1 O TYR B 456 N LEU B 354
SHEET 8 C 9 CYS B 432 SER B 436 1 N ILE B 434 O LEU B 453
SHEET 9 C 9 LEU B 413 ALA B 417 -1 N SER B 414 O GLU B 435
SHEET 1 D 5 ILE A 259 PHE A 261 0
SHEET 2 D 5 VAL A 230 LYS A 233 1 N VAL A 230 O GLN A 260
SHEET 3 D 5 PHE A 203 ILE A 207 1 N ALA A 206 O LYS A 233
SHEET 4 D 5 LEU A 279 THR A 285 1 O ASN A 283 N ALA A 205
SHEET 5 D 5 ARG A 310 GLU A 314 1 O ALA A 312 N PHE A 284
SHEET 1 E 9 LEU A 413 ALA A 417 0
SHEET 2 E 9 CYS A 432 SER A 436 -1 O GLU A 435 N SER A 414
SHEET 3 E 9 VAL A 452 TYR A 458 1 O LEU A 453 N ILE A 434
SHEET 4 E 9 CYS A 351 PRO A 357 1 N LEU A 354 O TYR A 456
SHEET 5 E 9 ASN A 319 VAL A 323 1 N VAL A 323 O TYR A 355
SHEET 6 E 9 THR A 479 PHE A 483 1 O ALA A 481 N PHE A 322
SHEET 7 E 9 ASN A 503 ILE A 506 1 O TYR A 505 N VAL A 482
SHEET 8 E 9 THR B 542 THR B 550 1 O LYS B 548 N ILE A 506
SHEET 9 E 9 SER B 191 GLY B 199 -1 N VAL B 196 O GLN B 545
SHEET 1 F 2 CYS A 421 ASN A 422 0
SHEET 2 F 2 TYR A 428 VAL A 429 -1 O TYR A 428 N ASN A 422
SHEET 1 G 2 TYR A 476 GLY A 477 0
SHEET 2 G 2 ALA A 523 ARG A 524 -1 N ALA A 523 O GLY A 477
SHEET 1 H 3 GLU B 62 ALA B 63 0
SHEET 2 H 3 ASN B 86 CYS B 95 1 O LYS B 93 N GLU B 62
SHEET 3 H 3 ILE B 78 SER B 83 -1 N GLN B 79 O PHE B 94
SHEET 1 I 2 CYS B 66 VAL B 68 0
SHEET 2 I 2 GLU B 71 VAL B 73 -1 O VAL B 73 N CYS B 66
SHEET 1 J 5 ILE B 259 PHE B 261 0
SHEET 2 J 5 VAL B 230 LYS B 233 1 N VAL B 230 O GLN B 260
SHEET 3 J 5 PHE B 203 ILE B 207 1 N ALA B 206 O LEU B 231
SHEET 4 J 5 LEU B 279 THR B 285 1 O ASN B 283 N ALA B 205
SHEET 5 J 5 ARG B 310 GLU B 314 1 O ALA B 312 N PHE B 284
SHEET 1 K 2 CYS B 421 ASN B 422 0
SHEET 2 K 2 TYR B 428 VAL B 429 -1 O TYR B 428 N ASN B 422
SHEET 1 L 2 TYR B 476 GLY B 477 0
SHEET 2 L 2 ALA B 523 ARG B 524 -1 O ALA B 523 N GLY B 477
CISPEP 1 PRO A 189 PRO A 190 0 6.32
CISPEP 2 PRO B 189 PRO B 190 0 7.36
SITE 1 AC1 6 LEU A 302 ASP A 303 PHE A 305 THR A 307
SITE 2 AC1 6 LYS B 292 ALA B 525
SITE 1 AC2 7 PHE A 210 ILE A 392 ASP A 393 LYS A 395
SITE 2 AC2 7 ALA A 396 ARG A 399 HOH A 867
SITE 1 AC3 12 SER A 41 GLN A 42 GLY A 43 SER A 44
SITE 2 AC3 12 PRO A 45 GLN A 184 PRO A 185 ILE A 186
SITE 3 AC3 12 HOH A 758 HOH A 930 HOH A 967 HOH A1062
SITE 1 AC4 9 CYS A 348 SER A 349 THR A 511 GLY A 512
SITE 2 AC4 9 SER A 513 PHE A 520 HOH A 855 HOH A 860
SITE 3 AC4 9 HOH A1127
SITE 1 AC5 8 THR A 61 TRP A 74 TYR A 80 LYS A 93
SITE 2 AC5 8 PGE A 606 THR B 61 LYS B 90 LYS B 93
SITE 1 AC6 2 16P A 605 LYS B 93
SITE 1 AC7 5 LYS A 292 ALA A 525 LEU B 302 ASP B 303
SITE 2 AC7 5 PHE B 305
SITE 1 AC8 6 PHE B 210 ILE B 392 ASP B 393 LYS B 395
SITE 2 AC8 6 ALA B 396 ARG B 399
SITE 1 AC9 10 GLU B 165 PHE B 212 CYS B 348 SER B 349
SITE 2 AC9 10 THR B 511 GLY B 512 SER B 513 PHE B 520
SITE 3 AC9 10 HOH B 838 HOH B 839
CRYST1 84.980 93.878 132.406 90.00 90.00 90.00 P 21 21 21 8
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 0.011767 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010652 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007553 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
