HEADER SIGNALING PROTEIN/RECEPTOR 26-OCT-05 2C5D
TITLE STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LG DOMAINS, RESIDUES 207-624;
COMPND 5 SYNONYM: GAS-6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TYROSINE-PROTEIN KINASE RECEPTOR UFO;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: IG DOMAINS, RESIDUES 26-220;
COMPND 11 SYNONYM: AXL ONCOGENE;
COMPND 12 EC: 2.7.1.112;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: 293-EBNA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PCEP-PU;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PASK-IBA12
KEYWDS SIGNALING PROTEIN/RECEPTOR, GROWTH REGULATION-COMPLEX, VITAMIN K-
KEYWDS 2 DEPENDENT PROTEIN, LAMININ G-LIKE DOMAIN, RECEPTOR TYROSINE KINASE,
KEYWDS 3 IMMUNOGLOBULIN-LIKE DOMAIN, GROWTH REGULATION, EGF-LIKE DOMAIN,
KEYWDS 4 RECEPTOR, SIGNALING PROTEIN-RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SASAKI,P.G.KNYAZEV,N.J.CLOUT,Y.CHEBURKIN,W.GOEHRING,A.ULLRICH,
AUTHOR 2 R.TIMPL,E.HOHENESTER
REVDAT 5 13-DEC-23 2C5D 1 HETSYN
REVDAT 4 29-JUL-20 2C5D 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 24-FEB-09 2C5D 1 VERSN
REVDAT 2 20-DEC-06 2C5D 1 JRNL
REVDAT 1 19-DEC-05 2C5D 0
JRNL AUTH T.SASAKI,P.G.KNYAZEV,N.J.CLOUT,Y.CHEBURKIN,W.GOEHRING,
JRNL AUTH 2 A.ULLRICH,R.TIMPL,E.HOHENESTER
JRNL TITL STRUCTURAL BASIS FOR GAS6-AXL SIGNALLING.
JRNL REF EMBO J. V. 25 80 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16362042
JRNL DOI 10.1038/SJ.EMBOJ.7600912
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.SASAKI,P.G.KNYAZEV,Y.CHEBURKIN,W.GOEHRING,D.TISI,
REMARK 1 AUTH 2 A.ULLRICH,R.TIMPL,E.HOHENESTER
REMARK 1 TITL CRYSTAL STRUCTURE OF A C-TERMINAL FRAGMENT OF GROWTH
REMARK 1 TITL 2 ARREST-SPECIFIC PROTEIN GAS6
REMARK 1 REF J.BIOL.CHEM. V. 277 44164 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12218057
REMARK 1 DOI 10.1074/JBC.M207340200
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.HEIRING,B.DAHLBACK,Y.A.MULLER
REMARK 1 TITL LIGAND RECOGNITION AND HOMOPHILIC INTERACTIONS IN TYRO3
REMARK 1 REF J.BIOL.CHEM. V. 279 6952 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 14623883
REMARK 1 DOI 10.1074/JBC.M311750200
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 47648
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2384
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8814
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.16300
REMARK 3 B22 (A**2) : -7.16300
REMARK 3 B33 (A**2) : 14.32500
REMARK 3 B12 (A**2) : -6.70100
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.720 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.140 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.500 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT
REMARK 3 KSOL : 0.21
REMARK 3 BSOL : 10.00
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2C5D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1290026179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47655
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.43000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 1H30 AND 1RHF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 21.31700
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 42.63400
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 31.97550
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 53.29250
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 10.65850
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 257
REMARK 465 PRO A 258
REMARK 465 LEU A 259
REMARK 465 ALA A 260
REMARK 465 HIS A 261
REMARK 465 CYS A 262
REMARK 465 ASP A 263
REMARK 465 GLY A 264
REMARK 465 ARG A 265
REMARK 465 GLY A 266
REMARK 465 GLY A 267
REMARK 465 LEU A 268
REMARK 465 LYS A 269
REMARK 465 LEU A 270
REMARK 465 SER A 271
REMARK 465 GLN A 272
REMARK 465 ASP A 273
REMARK 465 MET A 274
REMARK 465 ASP A 275
REMARK 465 THR A 276
REMARK 465 CYS A 277
REMARK 465 GLU A 278
REMARK 465 ARG A 494
REMARK 465 THR A 495
REMARK 465 PRO A 496
REMARK 465 LEU A 497
REMARK 465 ASP A 498
REMARK 465 VAL A 499
REMARK 465 GLY A 500
REMARK 465 THR A 501
REMARK 465 GLU A 502
REMARK 465 SER A 503
REMARK 465 TYR A 542
REMARK 465 HIS A 543
REMARK 465 SER A 544
REMARK 465 THR A 545
REMARK 465 LYS A 546
REMARK 465 LYS A 547
REMARK 465 LEU A 548
REMARK 465 LYS A 549
REMARK 465 ALA A 678
REMARK 465 ALA B 257
REMARK 465 PRO B 258
REMARK 465 LEU B 259
REMARK 465 ALA B 260
REMARK 465 HIS B 261
REMARK 465 CYS B 262
REMARK 465 ASP B 263
REMARK 465 GLY B 264
REMARK 465 ARG B 265
REMARK 465 GLY B 266
REMARK 465 GLY B 267
REMARK 465 LEU B 268
REMARK 465 LYS B 269
REMARK 465 LEU B 270
REMARK 465 SER B 271
REMARK 465 GLN B 272
REMARK 465 ASP B 273
REMARK 465 MET B 274
REMARK 465 ASP B 275
REMARK 465 THR B 276
REMARK 465 CYS B 277
REMARK 465 GLU B 278
REMARK 465 ARG B 494
REMARK 465 THR B 495
REMARK 465 PRO B 496
REMARK 465 LEU B 497
REMARK 465 ASP B 498
REMARK 465 VAL B 499
REMARK 465 GLY B 500
REMARK 465 THR B 501
REMARK 465 GLU B 502
REMARK 465 SER B 503
REMARK 465 TYR B 542
REMARK 465 HIS B 543
REMARK 465 SER B 544
REMARK 465 THR B 545
REMARK 465 LYS B 546
REMARK 465 LYS B 547
REMARK 465 LEU B 548
REMARK 465 LYS B 549
REMARK 465 ALA B 678
REMARK 465 GLU C 26
REMARK 465 GLN C 219
REMARK 465 GLN C 220
REMARK 465 GLU D 26
REMARK 465 GLN D 219
REMARK 465 GLN D 220
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 389 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 413 CG CD OE1 OE2
REMARK 470 ALA A 677 CA C O CB
REMARK 470 ARG B 389 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 413 CG CD OE1 OE2
REMARK 470 ALA B 677 CA C O CB
REMARK 470 PRO C 218 CA C O CB CG CD
REMARK 470 PRO D 218 CA C O CB CG CD
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 VAL A 292 -17.90 -42.64
REMARK 500 SER A 343 -94.31 -101.79
REMARK 500 TYR A 361 69.41 -119.57
REMARK 500 ASN A 362 84.97 75.53
REMARK 500 VAL A 364 96.58 -68.58
REMARK 500 ARG A 366 148.37 -178.04
REMARK 500 SER A 370 -156.49 -169.17
REMARK 500 ASN A 375 44.95 -79.15
REMARK 500 GLU A 386 38.16 -97.24
REMARK 500 ALA A 388 -143.75 52.86
REMARK 500 ARG A 397 11.86 50.69
REMARK 500 LEU A 419 131.05 -170.65
REMARK 500 LEU A 433 -137.14 -61.33
REMARK 500 PRO A 436 156.16 -47.20
REMARK 500 ASN A 452 108.50 65.60
REMARK 500 ASP A 455 72.57 -22.54
REMARK 500 THR A 456 85.04 -51.74
REMARK 500 SER A 483 -5.96 -150.76
REMARK 500 VAL A 507 87.85 -161.66
REMARK 500 ARG A 514 73.22 -152.77
REMARK 500 PRO A 515 164.92 -43.85
REMARK 500 LEU A 522 -75.84 -79.10
REMARK 500 VAL A 533 67.03 -112.65
REMARK 500 SER A 536 136.78 -172.75
REMARK 500 GLN A 551 91.85 56.95
REMARK 500 VAL A 554 111.08 -161.38
REMARK 500 GLU A 558 -144.94 44.73
REMARK 500 ALA A 561 -173.51 -61.39
REMARK 500 LEU A 562 -12.34 -162.75
REMARK 500 ALA A 563 150.53 173.39
REMARK 500 MET A 565 126.38 176.98
REMARK 500 ASP A 571 14.62 -143.74
REMARK 500 ARG A 582 157.89 178.76
REMARK 500 ALA A 586 79.59 -165.23
REMARK 500 ASP A 591 32.13 72.18
REMARK 500 VAL A 599 -140.86 -93.48
REMARK 500 SER A 600 19.85 -168.14
REMARK 500 ALA A 601 -13.22 64.92
REMARK 500 ARG A 607 -66.45 -132.86
REMARK 500 PRO A 627 -177.00 -59.45
REMARK 500 ASP A 628 94.29 -69.39
REMARK 500 THR A 637 -4.05 -140.67
REMARK 500 ASN A 649 51.20 75.98
REMARK 500 ARG A 650 -1.25 67.54
REMARK 500 ALA A 658 174.15 -58.11
REMARK 500 TYR A 660 117.79 -169.68
REMARK 500 GLU A 674 104.40 -58.03
REMARK 500 VAL B 292 -18.05 -43.17
REMARK 500 SER B 343 -94.29 -101.33
REMARK 500 ASN B 362 84.89 75.47
REMARK 500
REMARK 500 THIS ENTRY HAS 119 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1677 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 329 OD1
REMARK 620 2 ASP A 329 OD2 54.4
REMARK 620 3 GLU A 331 O 58.5 89.3
REMARK 620 4 ARG A 440 O 121.6 84.1 85.5
REMARK 620 5 ASP A 656 OD2 108.8 66.5 154.4 83.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1677 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 329 OD2
REMARK 620 2 ASP B 329 OD1 50.0
REMARK 620 3 GLU B 331 O 84.5 56.6
REMARK 620 4 ARG B 440 O 82.1 117.8 86.1
REMARK 620 5 ASP B 656 OD2 64.5 102.4 148.5 84.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C1218 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 116 NE2
REMARK 620 2 HIS D 179 NE2 113.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D1218 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 179 NE2
REMARK 620 2 HIS D 116 NE2 107.3
REMARK 620 N 1
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H30 RELATED DB: PDB
REMARK 900 C-TERMINAL LG DOMAIN PAIR OF HUMAN GAS6
DBREF 2C5D A 257 260 PDB 2C5D 2C5D 257 260
DBREF 2C5D A 261 678 UNP Q14393 GAS6_HUMAN 207 624
DBREF 2C5D B 257 260 PDB 2C5D 2C5D 257 260
DBREF 2C5D B 261 678 UNP Q14393 GAS6_HUMAN 207 624
DBREF 2C5D C 26 220 UNP P30530 UFO_HUMAN 26 220
DBREF 2C5D D 26 220 UNP P30530 UFO_HUMAN 26 220
SEQRES 1 A 422 ALA PRO LEU ALA HIS CYS ASP GLY ARG GLY GLY LEU LYS
SEQRES 2 A 422 LEU SER GLN ASP MET ASP THR CYS GLU ASP ILE LEU PRO
SEQRES 3 A 422 CYS VAL PRO PHE SER VAL ALA LYS SER VAL LYS SER LEU
SEQRES 4 A 422 TYR LEU GLY ARG MET PHE SER GLY THR PRO VAL ILE ARG
SEQRES 5 A 422 LEU ARG PHE LYS ARG LEU GLN PRO THR ARG LEU VAL ALA
SEQRES 6 A 422 GLU PHE ASP PHE ARG THR PHE ASP PRO GLU GLY ILE LEU
SEQRES 7 A 422 LEU PHE ALA GLY GLY HIS GLN ASP SER THR TRP ILE VAL
SEQRES 8 A 422 LEU ALA LEU ARG ALA GLY ARG LEU GLU LEU GLN LEU ARG
SEQRES 9 A 422 TYR ASN GLY VAL GLY ARG VAL THR SER SER GLY PRO VAL
SEQRES 10 A 422 ILE ASN HIS GLY MET TRP GLN THR ILE SER VAL GLU GLU
SEQRES 11 A 422 LEU ALA ARG ASN LEU VAL ILE LYS VAL ASN ARG ASP ALA
SEQRES 12 A 422 VAL MET LYS ILE ALA VAL ALA GLY ASP LEU PHE GLN PRO
SEQRES 13 A 422 GLU ARG GLY LEU TYR HIS LEU ASN LEU THR VAL GLY GLY
SEQRES 14 A 422 ILE PRO PHE HIS GLU LYS ASP LEU VAL GLN PRO ILE ASN
SEQRES 15 A 422 PRO ARG LEU ASP GLY CYS MET ARG SER TRP ASN TRP LEU
SEQRES 16 A 422 ASN GLY GLU ASP THR THR ILE GLN GLU THR VAL LYS VAL
SEQRES 17 A 422 ASN THR ARG MET GLN CYS PHE SER VAL THR GLU ARG GLY
SEQRES 18 A 422 SER PHE TYR PRO GLY SER GLY PHE ALA PHE TYR SER LEU
SEQRES 19 A 422 ASP TYR MET ARG THR PRO LEU ASP VAL GLY THR GLU SER
SEQRES 20 A 422 THR TRP GLU VAL GLU VAL VAL ALA HIS ILE ARG PRO ALA
SEQRES 21 A 422 ALA ASP THR GLY VAL LEU PHE ALA LEU TRP ALA PRO ASP
SEQRES 22 A 422 LEU ARG ALA VAL PRO LEU SER VAL ALA LEU VAL ASP TYR
SEQRES 23 A 422 HIS SER THR LYS LYS LEU LYS LYS GLN LEU VAL VAL LEU
SEQRES 24 A 422 ALA VAL GLU HIS THR ALA LEU ALA LEU MET GLU ILE LYS
SEQRES 25 A 422 VAL CYS ASP GLY GLN GLU HIS VAL VAL THR VAL SER LEU
SEQRES 26 A 422 ARG ASP GLY GLU ALA THR LEU GLU VAL ASP GLY THR ARG
SEQRES 27 A 422 GLY GLN SER GLU VAL SER ALA ALA GLN LEU GLN GLU ARG
SEQRES 28 A 422 LEU ALA VAL LEU GLU ARG HIS LEU ARG SER PRO VAL LEU
SEQRES 29 A 422 THR PHE ALA GLY GLY LEU PRO ASP VAL PRO VAL THR SER
SEQRES 30 A 422 ALA PRO VAL THR ALA PHE TYR ARG GLY CYS MET THR LEU
SEQRES 31 A 422 GLU VAL ASN ARG ARG LEU LEU ASP LEU ASP GLU ALA ALA
SEQRES 32 A 422 TYR LYS HIS SER ASP ILE THR ALA HIS SER CYS PRO PRO
SEQRES 33 A 422 VAL GLU PRO ALA ALA ALA
SEQRES 1 B 422 ALA PRO LEU ALA HIS CYS ASP GLY ARG GLY GLY LEU LYS
SEQRES 2 B 422 LEU SER GLN ASP MET ASP THR CYS GLU ASP ILE LEU PRO
SEQRES 3 B 422 CYS VAL PRO PHE SER VAL ALA LYS SER VAL LYS SER LEU
SEQRES 4 B 422 TYR LEU GLY ARG MET PHE SER GLY THR PRO VAL ILE ARG
SEQRES 5 B 422 LEU ARG PHE LYS ARG LEU GLN PRO THR ARG LEU VAL ALA
SEQRES 6 B 422 GLU PHE ASP PHE ARG THR PHE ASP PRO GLU GLY ILE LEU
SEQRES 7 B 422 LEU PHE ALA GLY GLY HIS GLN ASP SER THR TRP ILE VAL
SEQRES 8 B 422 LEU ALA LEU ARG ALA GLY ARG LEU GLU LEU GLN LEU ARG
SEQRES 9 B 422 TYR ASN GLY VAL GLY ARG VAL THR SER SER GLY PRO VAL
SEQRES 10 B 422 ILE ASN HIS GLY MET TRP GLN THR ILE SER VAL GLU GLU
SEQRES 11 B 422 LEU ALA ARG ASN LEU VAL ILE LYS VAL ASN ARG ASP ALA
SEQRES 12 B 422 VAL MET LYS ILE ALA VAL ALA GLY ASP LEU PHE GLN PRO
SEQRES 13 B 422 GLU ARG GLY LEU TYR HIS LEU ASN LEU THR VAL GLY GLY
SEQRES 14 B 422 ILE PRO PHE HIS GLU LYS ASP LEU VAL GLN PRO ILE ASN
SEQRES 15 B 422 PRO ARG LEU ASP GLY CYS MET ARG SER TRP ASN TRP LEU
SEQRES 16 B 422 ASN GLY GLU ASP THR THR ILE GLN GLU THR VAL LYS VAL
SEQRES 17 B 422 ASN THR ARG MET GLN CYS PHE SER VAL THR GLU ARG GLY
SEQRES 18 B 422 SER PHE TYR PRO GLY SER GLY PHE ALA PHE TYR SER LEU
SEQRES 19 B 422 ASP TYR MET ARG THR PRO LEU ASP VAL GLY THR GLU SER
SEQRES 20 B 422 THR TRP GLU VAL GLU VAL VAL ALA HIS ILE ARG PRO ALA
SEQRES 21 B 422 ALA ASP THR GLY VAL LEU PHE ALA LEU TRP ALA PRO ASP
SEQRES 22 B 422 LEU ARG ALA VAL PRO LEU SER VAL ALA LEU VAL ASP TYR
SEQRES 23 B 422 HIS SER THR LYS LYS LEU LYS LYS GLN LEU VAL VAL LEU
SEQRES 24 B 422 ALA VAL GLU HIS THR ALA LEU ALA LEU MET GLU ILE LYS
SEQRES 25 B 422 VAL CYS ASP GLY GLN GLU HIS VAL VAL THR VAL SER LEU
SEQRES 26 B 422 ARG ASP GLY GLU ALA THR LEU GLU VAL ASP GLY THR ARG
SEQRES 27 B 422 GLY GLN SER GLU VAL SER ALA ALA GLN LEU GLN GLU ARG
SEQRES 28 B 422 LEU ALA VAL LEU GLU ARG HIS LEU ARG SER PRO VAL LEU
SEQRES 29 B 422 THR PHE ALA GLY GLY LEU PRO ASP VAL PRO VAL THR SER
SEQRES 30 B 422 ALA PRO VAL THR ALA PHE TYR ARG GLY CYS MET THR LEU
SEQRES 31 B 422 GLU VAL ASN ARG ARG LEU LEU ASP LEU ASP GLU ALA ALA
SEQRES 32 B 422 TYR LYS HIS SER ASP ILE THR ALA HIS SER CYS PRO PRO
SEQRES 33 B 422 VAL GLU PRO ALA ALA ALA
SEQRES 1 C 195 GLU GLU SER PRO PHE VAL GLY ASN PRO GLY ASN ILE THR
SEQRES 2 C 195 GLY ALA ARG GLY LEU THR GLY THR LEU ARG CYS GLN LEU
SEQRES 3 C 195 GLN VAL GLN GLY GLU PRO PRO GLU VAL HIS TRP LEU ARG
SEQRES 4 C 195 ASP GLY GLN ILE LEU GLU LEU ALA ASP SER THR GLN THR
SEQRES 5 C 195 GLN VAL PRO LEU GLY GLU ASP GLU GLN ASP ASP TRP ILE
SEQRES 6 C 195 VAL VAL SER GLN LEU ARG ILE THR SER LEU GLN LEU SER
SEQRES 7 C 195 ASP THR GLY GLN TYR GLN CYS LEU VAL PHE LEU GLY HIS
SEQRES 8 C 195 GLN THR PHE VAL SER GLN PRO GLY TYR VAL GLY LEU GLU
SEQRES 9 C 195 GLY LEU PRO TYR PHE LEU GLU GLU PRO GLU ASP ARG THR
SEQRES 10 C 195 VAL ALA ALA ASN THR PRO PHE ASN LEU SER CYS GLN ALA
SEQRES 11 C 195 GLN GLY PRO PRO GLU PRO VAL ASP LEU LEU TRP LEU GLN
SEQRES 12 C 195 ASP ALA VAL PRO LEU ALA THR ALA PRO GLY HIS GLY PRO
SEQRES 13 C 195 GLN ARG SER LEU HIS VAL PRO GLY LEU ASN LYS THR SER
SEQRES 14 C 195 SER PHE SER CYS GLU ALA HIS ASN ALA LYS GLY VAL THR
SEQRES 15 C 195 THR SER ARG THR ALA THR ILE THR VAL LEU PRO GLN GLN
SEQRES 1 D 195 GLU GLU SER PRO PHE VAL GLY ASN PRO GLY ASN ILE THR
SEQRES 2 D 195 GLY ALA ARG GLY LEU THR GLY THR LEU ARG CYS GLN LEU
SEQRES 3 D 195 GLN VAL GLN GLY GLU PRO PRO GLU VAL HIS TRP LEU ARG
SEQRES 4 D 195 ASP GLY GLN ILE LEU GLU LEU ALA ASP SER THR GLN THR
SEQRES 5 D 195 GLN VAL PRO LEU GLY GLU ASP GLU GLN ASP ASP TRP ILE
SEQRES 6 D 195 VAL VAL SER GLN LEU ARG ILE THR SER LEU GLN LEU SER
SEQRES 7 D 195 ASP THR GLY GLN TYR GLN CYS LEU VAL PHE LEU GLY HIS
SEQRES 8 D 195 GLN THR PHE VAL SER GLN PRO GLY TYR VAL GLY LEU GLU
SEQRES 9 D 195 GLY LEU PRO TYR PHE LEU GLU GLU PRO GLU ASP ARG THR
SEQRES 10 D 195 VAL ALA ALA ASN THR PRO PHE ASN LEU SER CYS GLN ALA
SEQRES 11 D 195 GLN GLY PRO PRO GLU PRO VAL ASP LEU LEU TRP LEU GLN
SEQRES 12 D 195 ASP ALA VAL PRO LEU ALA THR ALA PRO GLY HIS GLY PRO
SEQRES 13 D 195 GLN ARG SER LEU HIS VAL PRO GLY LEU ASN LYS THR SER
SEQRES 14 D 195 SER PHE SER CYS GLU ALA HIS ASN ALA LYS GLY VAL THR
SEQRES 15 D 195 THR SER ARG THR ALA THR ILE THR VAL LEU PRO GLN GLN
MODRES 2C5D ASN A 420 ASN GLYCOSYLATION SITE
MODRES 2C5D ASN B 420 ASN GLYCOSYLATION SITE
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET CA A1677 1
HET CA B1677 1
HET NI C1218 1
HET SO4 C1219 5
HET NI D1218 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM NI NICKEL (II) ION
HETNAM SO4 SULFATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 7 CA 2(CA 2+)
FORMUL 9 NI 2(NI 2+)
FORMUL 10 SO4 O4 S 2-
HELIX 1 1 HIS A 429 LEU A 433 5 5
HELIX 2 2 THR A 457 ASN A 465 1 9
HELIX 3 3 THR A 466 GLN A 469 5 4
HELIX 4 4 LEU A 604 LEU A 615 1 12
HELIX 5 5 PRO A 630 ALA A 634 5 5
HELIX 6 6 HIS B 429 LEU B 433 5 5
HELIX 7 7 THR B 457 ASN B 465 1 9
HELIX 8 8 THR B 466 GLN B 469 5 4
HELIX 9 9 LEU B 604 LEU B 615 1 12
HELIX 10 10 PRO B 630 ALA B 634 5 5
SHEET 1 AA 9 LEU A 295 TYR A 296 0
SHEET 2 AA 9 GLY A 443 TRP A 450 -1 O MET A 445 N LEU A 295
SHEET 3 AA 9 VAL A 320 THR A 327 -1 O GLU A 322 N ASN A 449
SHEET 4 AA 9 THR A 381 GLU A 385 -1 O ILE A 382 N PHE A 323
SHEET 5 AA 9 ASN A 390 VAL A 395 -1 O VAL A 392 N GLU A 385
SHEET 6 AA 9 ASP A 398 ALA A 404 -1 O ASP A 398 N VAL A 395
SHEET 7 AA 9 GLY D 205 THR D 208 1 O VAL D 206 N LYS A 402
SHEET 8 AA 9 SER D 194 ASN D 202 -1 O ALA D 200 N THR D 207
SHEET 9 AA 9 ASP D 163 GLN D 168 -1 O ASP D 163 N HIS D 201
SHEET 1 AB10 LEU A 295 TYR A 296 0
SHEET 2 AB10 GLY A 443 TRP A 450 -1 O MET A 445 N LEU A 295
SHEET 3 AB10 VAL A 320 THR A 327 -1 O GLU A 322 N ASN A 449
SHEET 4 AB10 THR A 381 GLU A 385 -1 O ILE A 382 N PHE A 323
SHEET 5 AB10 ASN A 390 VAL A 395 -1 O VAL A 392 N GLU A 385
SHEET 6 AB10 ASP A 398 ALA A 404 -1 O ASP A 398 N VAL A 395
SHEET 7 AB10 GLY D 205 THR D 208 1 O VAL D 206 N LYS A 402
SHEET 8 AB10 SER D 194 ASN D 202 -1 O ALA D 200 N THR D 207
SHEET 9 AB10 ALA D 212 VAL D 216 -1 O ALA D 212 N PHE D 196
SHEET 10 AB10 ARG D 141 VAL D 143 1 O ARG D 141 N THR D 215
SHEET 1 AC10 VAL A 367 SER A 370 0
SHEET 2 AC10 ARG A 354 TYR A 361 -1 O LEU A 355 N SER A 370
SHEET 3 AC10 THR A 344 ARG A 351 -1 O TRP A 345 N ARG A 360
SHEET 4 AC10 GLY A 332 GLY A 338 -1 O GLY A 332 N LEU A 350
SHEET 5 AC10 TYR A 417 VAL A 423 -1 O ASN A 420 N GLY A 338
SHEET 6 AC10 ILE A 307 ARG A 313 -1 O ILE A 307 N VAL A 423
SHEET 7 AC10 ASP C 73 PRO C 80 -1 O SER C 74 N LYS A 312
SHEET 8 AC10 ASP C 88 ILE C 97 -1 O ILE C 90 N VAL C 79
SHEET 9 AC10 GLY C 45 GLN C 54 -1 O GLY C 45 N ILE C 97
SHEET 10 AC10 PHE C 30 GLY C 32 -1 N VAL C 31 O GLN C 50
SHEET 1 AD 6 VAL A 367 SER A 370 0
SHEET 2 AD 6 ARG A 354 TYR A 361 -1 O LEU A 355 N SER A 370
SHEET 3 AD 6 THR A 344 ARG A 351 -1 O TRP A 345 N ARG A 360
SHEET 4 AD 6 GLY A 332 GLY A 338 -1 O GLY A 332 N LEU A 350
SHEET 5 AD 6 TYR A 417 VAL A 423 -1 O ASN A 420 N GLY A 338
SHEET 6 AD 6 GLN A 411 PRO A 412 -1 O GLN A 411 N HIS A 418
SHEET 1 AE 5 PHE A 479 PRO A 481 0
SHEET 2 AE 5 ARG A 641 VAL A 648 -1 O GLY A 642 N TYR A 480
SHEET 3 AE 5 VAL A 507 PRO A 515 -1 O VAL A 510 N GLU A 647
SHEET 4 AE 5 HIS A 575 ARG A 582 -1 O HIS A 575 N ILE A 513
SHEET 5 AE 5 GLU A 585 VAL A 590 -1 O GLU A 585 N ARG A 582
SHEET 1 AF 7 THR A 560 GLU A 566 0
SHEET 2 AF 7 LEU A 552 VAL A 557 -1 O VAL A 553 N MET A 565
SHEET 3 AF 7 LEU A 535 VAL A 540 -1 O SER A 536 N ALA A 556
SHEET 4 AF 7 GLY A 520 TRP A 526 -1 O GLY A 520 N LEU A 539
SHEET 5 AF 7 LEU A 620 ALA A 623 -1 O LEU A 620 N TRP A 526
SHEET 6 AF 7 ALA A 486 SER A 489 -1 O ALA A 486 N ALA A 623
SHEET 7 AF 7 TYR A 660 LYS A 661 -1 O TYR A 660 N PHE A 487
SHEET 1 BA 9 LEU B 295 TYR B 296 0
SHEET 2 BA 9 GLY B 443 TRP B 450 -1 O MET B 445 N LEU B 295
SHEET 3 BA 9 VAL B 320 THR B 327 -1 O GLU B 322 N ASN B 449
SHEET 4 BA 9 THR B 381 GLU B 385 -1 O ILE B 382 N PHE B 323
SHEET 5 BA 9 ASN B 390 VAL B 395 -1 O VAL B 392 N GLU B 385
SHEET 6 BA 9 ASP B 398 ALA B 404 -1 O ASP B 398 N VAL B 395
SHEET 7 BA 9 GLY C 205 THR C 208 1 O VAL C 206 N LYS B 402
SHEET 8 BA 9 SER C 194 ASN C 202 -1 O ALA C 200 N THR C 207
SHEET 9 BA 9 ASP C 163 GLN C 168 -1 O ASP C 163 N HIS C 201
SHEET 1 BB10 LEU B 295 TYR B 296 0
SHEET 2 BB10 GLY B 443 TRP B 450 -1 O MET B 445 N LEU B 295
SHEET 3 BB10 VAL B 320 THR B 327 -1 O GLU B 322 N ASN B 449
SHEET 4 BB10 THR B 381 GLU B 385 -1 O ILE B 382 N PHE B 323
SHEET 5 BB10 ASN B 390 VAL B 395 -1 O VAL B 392 N GLU B 385
SHEET 6 BB10 ASP B 398 ALA B 404 -1 O ASP B 398 N VAL B 395
SHEET 7 BB10 GLY C 205 THR C 208 1 O VAL C 206 N LYS B 402
SHEET 8 BB10 SER C 194 ASN C 202 -1 O ALA C 200 N THR C 207
SHEET 9 BB10 ALA C 212 VAL C 216 -1 O ALA C 212 N PHE C 196
SHEET 10 BB10 ARG C 141 VAL C 143 1 O ARG C 141 N THR C 215
SHEET 1 BC13 VAL B 367 SER B 370 0
SHEET 2 BC13 ARG B 354 TYR B 361 -1 O LEU B 355 N SER B 370
SHEET 3 BC13 THR B 344 ARG B 351 -1 O TRP B 345 N ARG B 360
SHEET 4 BC13 GLY B 332 GLY B 338 -1 O GLY B 332 N LEU B 350
SHEET 5 BC13 TYR B 417 VAL B 423 -1 O ASN B 420 N GLY B 338
SHEET 6 BC13 GLN B 411 PRO B 412 -1 O GLN B 411 N HIS B 418
SHEET 7 BC13 TYR B 417 VAL B 423 -1 O HIS B 418 N GLN B 411
SHEET 8 BC13 PHE D 30 GLY D 32 0
SHEET 9 BC13 GLY D 45 GLN D 54 -1 O GLN D 50 N VAL D 31
SHEET 10 BC13 ASP D 88 ILE D 97 -1 O TRP D 89 N VAL D 53
SHEET 11 BC13 ASP D 73 PRO D 80 -1 O ASP D 73 N ARG D 96
SHEET 12 BC13 ILE B 307 ARG B 313 -1 O ARG B 308 N GLN D 78
SHEET 13 BC13 TYR B 417 VAL B 423 -1 O TYR B 417 N ARG B 313
SHEET 1 BD 5 PHE B 479 PRO B 481 0
SHEET 2 BD 5 ARG B 641 VAL B 648 -1 O GLY B 642 N TYR B 480
SHEET 3 BD 5 VAL B 507 PRO B 515 -1 O VAL B 510 N GLU B 647
SHEET 4 BD 5 HIS B 575 ARG B 582 -1 O HIS B 575 N ILE B 513
SHEET 5 BD 5 GLU B 585 VAL B 590 -1 O GLU B 585 N ARG B 582
SHEET 1 BE 7 THR B 560 GLU B 566 0
SHEET 2 BE 7 LEU B 552 VAL B 557 -1 O VAL B 553 N MET B 565
SHEET 3 BE 7 LEU B 535 VAL B 540 -1 O SER B 536 N ALA B 556
SHEET 4 BE 7 GLY B 520 TRP B 526 -1 O GLY B 520 N LEU B 539
SHEET 5 BE 7 LEU B 620 ALA B 623 -1 O LEU B 620 N TRP B 526
SHEET 6 BE 7 ALA B 486 SER B 489 -1 O ALA B 486 N ALA B 623
SHEET 7 BE 7 TYR B 660 LYS B 661 -1 O TYR B 660 N PHE B 487
SHEET 1 CA 8 ILE C 37 GLY C 39 0
SHEET 2 CA 8 GLY C 124 LEU C 128 1 O TYR C 125 N ILE C 37
SHEET 3 CA 8 GLY C 106 LEU C 114 -1 O GLY C 106 N VAL C 126
SHEET 4 CA 8 GLN C 67 ILE C 68 0
SHEET 5 CA 8 HIS C 61 ARG C 64 -1 O ARG C 64 N GLN C 67
SHEET 6 CA 8 GLY C 106 LEU C 114 -1 O GLN C 109 N LEU C 63
SHEET 7 CA 8 GLN C 117 VAL C 120 -1 O GLN C 117 N LEU C 114
SHEET 8 CA 8 GLY C 106 LEU C 114 -1 O VAL C 112 N PHE C 119
SHEET 1 CB 3 TYR C 133 GLU C 136 0
SHEET 2 CB 3 PHE C 149 GLN C 156 -1 O GLN C 154 N LEU C 135
SHEET 3 CB 3 ARG C 183 VAL C 187 -1 O ARG C 183 N CYS C 153
SHEET 1 DA 8 ILE D 37 GLY D 39 0
SHEET 2 DA 8 GLY D 124 LEU D 128 1 O TYR D 125 N ILE D 37
SHEET 3 DA 8 GLY D 106 LEU D 114 -1 O GLY D 106 N VAL D 126
SHEET 4 DA 8 GLN D 67 ILE D 68 0
SHEET 5 DA 8 HIS D 61 ARG D 64 -1 O ARG D 64 N GLN D 67
SHEET 6 DA 8 GLY D 106 LEU D 114 -1 O GLN D 109 N LEU D 63
SHEET 7 DA 8 GLN D 117 VAL D 120 -1 O GLN D 117 N LEU D 114
SHEET 8 DA 8 GLY D 106 LEU D 114 -1 O VAL D 112 N PHE D 119
SHEET 1 DB 3 TYR D 133 GLU D 136 0
SHEET 2 DB 3 PHE D 149 GLN D 156 -1 O GLN D 154 N LEU D 135
SHEET 3 DB 3 ARG D 183 VAL D 187 -1 O ARG D 183 N CYS D 153
SSBOND 1 CYS A 283 CYS A 570 1555 1555 2.04
SSBOND 2 CYS A 444 CYS A 470 1555 1555 2.04
SSBOND 3 CYS A 643 CYS A 670 1555 1555 2.05
SSBOND 4 CYS B 283 CYS B 570 1555 1555 2.04
SSBOND 5 CYS B 444 CYS B 470 1555 1555 2.04
SSBOND 6 CYS B 643 CYS B 670 1555 1555 2.05
SSBOND 7 CYS C 49 CYS C 110 1555 1555 2.03
SSBOND 8 CYS C 153 CYS C 198 1555 1555 2.03
SSBOND 9 CYS D 49 CYS D 110 1555 1555 2.03
SSBOND 10 CYS D 153 CYS D 198 1555 1555 2.03
LINK ND2 ASN A 420 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 420 C1 NAG F 1 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.40
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.39
LINK OD1 ASP A 329 CA CA A1677 1555 1555 2.48
LINK OD2 ASP A 329 CA CA A1677 1555 1555 2.31
LINK O GLU A 331 CA CA A1677 1555 1555 2.22
LINK O ARG A 440 CA CA A1677 1555 1555 2.44
LINK OD2 ASP A 656 CA CA A1677 1555 1555 2.76
LINK OD2 ASP B 329 CA CA B1677 1555 1555 2.49
LINK OD1 ASP B 329 CA CA B1677 1555 1555 2.68
LINK O GLU B 331 CA CA B1677 1555 1555 2.26
LINK O ARG B 440 CA CA B1677 1555 1555 2.36
LINK OD2 ASP B 656 CA CA B1677 1555 1555 2.80
LINK NE2 HIS C 116 NI NI C1218 1555 1555 2.05
LINK NE2 HIS C 179 NI NI D1218 1554 1555 2.35
LINK NI NI C1218 NE2 HIS D 179 1555 1556 2.17
LINK NE2 HIS D 116 NI NI D1218 1555 1555 1.73
CISPEP 1 GLY C 157 PRO C 158 0 0.23
CISPEP 2 PRO C 158 PRO C 159 0 -0.41
CISPEP 3 GLU C 160 PRO C 161 0 0.03
CISPEP 4 GLY D 157 PRO D 158 0 0.30
CISPEP 5 PRO D 158 PRO D 159 0 -0.33
CISPEP 6 GLU D 160 PRO D 161 0 0.09
CRYST1 292.951 292.951 63.951 90.00 90.00 120.00 P 61 12
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 0.003414 0.001971 0.000000 0.00000
SCALE2 0.000000 0.003942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015637 0.00000
MTRIX1 1 0.071220 0.997360 0.013920 -1.68797 1
MTRIX2 1 0.997450 -0.071150 -0.005200 1.21185 1
MTRIX3 1 -0.004190 0.014260 -0.999890 183.00417 1
MTRIX1 2 0.071220 0.997360 0.013920 -1.68797 1
MTRIX2 2 0.997450 -0.071150 -0.005200 1.21185 1
MTRIX3 2 -0.004190 0.014260 -0.999890 183.00417 1
(ATOM LINES ARE NOT SHOWN.)
END
