HEADER SIGNALING PROTEIN/RECEPTOR 02-MAY-07 2UZX
TITLE STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH
TITLE 2 THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: CRYSTAL FORM I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERNALIN B;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: INTERNALIN DOMAIN (CAP, LRR, IR), INLB321, RESIDUES 36-320;
COMPND 5 SYNONYM: INLB;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HEPATOCYTE GROWTH FACTOR RECEPTOR;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: SEMA, PSI, IG1, MET741, RESIDUES 25-740;
COMPND 11 SYNONYM: HGF RECEPTOR, SCATTER FACTOR RECEPTOR, SF RECEPTOR, HGF/SF
COMPND 12 RECEPTOR, MET PROTO-ONCOGENE TYROSINE KINASE, C-MET;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: CONTAINS IG2 AND 6HIS TAG, WHICH ARE POORLY ORDERED
COMPND 15 AND NOT MODELED, MET WAS ENZYMATICALLY DEGLYCOSYLATED WITH ENDOH
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: EGD-E;
SOURCE 5 VARIANT: SEROVAR 12A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 CODONPLUS (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM30;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: CHO LEC 3.2.8.1;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PA71D
KEYWDS SIGNALING PROTEIN/RECEPTOR, LEUCINE RICH REPEAT, RECEPTOR ECTODOMAIN,
KEYWDS 2 HEPATOCYTE GROWTH FACTOR RECEPTOR, SIGNALING PROTEIN, ATP-BINDING,
KEYWDS 3 TRANSFERASE, POLYMORPHISM, GLYCOPROTEIN, VIRULENCE FACTOR, DISEASE
KEYWDS 4 MUTATION, NUCLEOTIDE-BINDING, TRANSMEMBRANE, PROTO-ONCOGENE,
KEYWDS 5 PHOSPHORYLATION, LEUCINE-RICH REPEAT, ALTERNATIVE SPLICING,
KEYWDS 6 TYROSINE-PROTEIN KINASE, CHROMOSOMAL REARRANGEMENT, LRR, HGFR,
KEYWDS 7 KINASE, MEMBRANE, RECEPTOR, INTERNALIN, SIGNALING PROTEIN-RECEPTOR
KEYWDS 8 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.H.NIEMANN,V.JAGER,P.J.G.BUTLER,J.VAN DEN HEUVEL,S.SCHMIDT,
AUTHOR 2 D.FERRARIS,E.GHERARDI,D.W.HEINZ
REVDAT 5 13-DEC-23 2UZX 1 REMARK
REVDAT 4 08-MAY-19 2UZX 1 REMARK
REVDAT 3 06-MAR-19 2UZX 1 REMARK
REVDAT 2 24-FEB-09 2UZX 1 VERSN
REVDAT 1 07-AUG-07 2UZX 0
JRNL AUTH H.H.NIEMANN,V.JAGER,P.J.G.BUTLER,J.VAN DEN HEUVEL,S.SCHMIDT,
JRNL AUTH 2 D.FERRARIS,E.GHERARDI,D.W.HEINZ
JRNL TITL STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN
JRNL TITL 2 COMPLEX WITH THE LISTERIA INVASION PROTEIN INLB
JRNL REF CELL(CAMBRIDGE,MASS.) V. 130 235 2007
JRNL REFN ISSN 0092-8674
JRNL PMID 17662939
JRNL DOI 10.1016/J.CELL.2007.05.037
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 51852
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2471
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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: B-FACTORS MODELED SOLELY BY TLS. TOTAL
REMARK 3 ISOTROPIC B-FACTORS GIVEN. TIGHT NCS ON INDIVIDUAL DOMAINS
REMARK 3 EMPLOYED THROUGHOUT REFINEMENT.
REMARK 4
REMARK 4 2UZX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1290032354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8730
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51852
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.23000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.25
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.680
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 1H6T, 1SHY, 1UX3, 2CEW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 DEG C VAPOR DIFFUSION. 2 UL PROTEIN
REMARK 280 (5 MG/ML) PLUS 1 UL RESERVOIR CONSISTING OF 16.5% PEG 1500, 4.4%
REMARK 280 MPD, 0.1 M TRIS, PH8.5. RESERVOIR WAS COVERED WITH ALS OIL.,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 107.25000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.25000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.35000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.4 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 400
REMARK 400 COMPOUND
REMARK 400 MEDIATES THE ENTRY OF LISTERIA MONOCYTOGENES INTO CELLS.
REMARK 400 RECEPTOR FOR HEPATOCYTE GROWTH FACTOR AND SCATTER FACTOR
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 GLY A 33
REMARK 465 GLU A 321
REMARK 465 GLU B 22
REMARK 465 THR B 23
REMARK 465 ARG B 24
REMARK 465 GLU B 25
REMARK 465 CYS B 26
REMARK 465 LYS B 27
REMARK 465 GLU B 28
REMARK 465 ALA B 29
REMARK 465 LEU B 30
REMARK 465 ALA B 31
REMARK 465 LYS B 32
REMARK 465 SER B 33
REMARK 465 GLU B 34
REMARK 465 MET B 35
REMARK 465 ASN B 36
REMARK 465 VAL B 37
REMARK 465 ASN B 38
REMARK 465 MET B 39
REMARK 465 LYS B 40
REMARK 465 CYS B 41
REMARK 465 HIS B 92
REMARK 465 PRO B 93
REMARK 465 ASP B 94
REMARK 465 CYS B 95
REMARK 465 PHE B 96
REMARK 465 PRO B 97
REMARK 465 CYS B 98
REMARK 465 GLN B 99
REMARK 465 ASP B 100
REMARK 465 CYS B 101
REMARK 465 SER B 102
REMARK 465 SER B 103
REMARK 465 LYS B 104
REMARK 465 ALA B 105
REMARK 465 ASN B 106
REMARK 465 LEU B 107
REMARK 465 SER B 108
REMARK 465 GLY B 109
REMARK 465 GLY B 110
REMARK 465 THR B 151
REMARK 465 ALA B 152
REMARK 465 ASP B 153
REMARK 465 ILE B 154
REMARK 465 GLN B 155
REMARK 465 PRO B 164
REMARK 465 GLN B 165
REMARK 465 ILE B 166
REMARK 465 GLU B 167
REMARK 465 PHE B 206
REMARK 465 PRO B 207
REMARK 465 ASP B 208
REMARK 465 HIS B 209
REMARK 465 GLU B 302
REMARK 465 LYS B 303
REMARK 465 ARG B 304
REMARK 465 LYS B 305
REMARK 465 LYS B 306
REMARK 465 ARG B 307
REMARK 465 SER B 308
REMARK 465 THR B 309
REMARK 465 LYS B 310
REMARK 465 VAL B 378
REMARK 465 ASN B 379
REMARK 465 LYS B 380
REMARK 465 ASN B 381
REMARK 465 HIS B 394
REMARK 465 GLU B 395
REMARK 465 HIS B 396
REMARK 465 CYS B 397
REMARK 465 PHE B 398
REMARK 465 ASN B 399
REMARK 465 ARG B 400
REMARK 465 THR B 401
REMARK 465 LEU B 402
REMARK 465 LEU B 403
REMARK 465 ARG B 404
REMARK 465 ASN B 405
REMARK 465 SER B 406
REMARK 465 SER B 407
REMARK 465 GLY B 408
REMARK 465 CYS B 409
REMARK 465 GLU B 410
REMARK 465 ALA B 411
REMARK 465 ARG B 412
REMARK 465 ARG B 413
REMARK 465 ALA B 629
REMARK 465 MET B 630
REMARK 465 ASN B 631
REMARK 465 LYS B 632
REMARK 465 HIS B 633
REMARK 465 ILE B 659
REMARK 465 THR B 660
REMARK 465 SER B 661
REMARK 465 ILE B 662
REMARK 465 SER B 663
REMARK 465 PRO B 664
REMARK 465 LYS B 665
REMARK 465 TYR B 666
REMARK 465 GLY B 667
REMARK 465 PRO B 668
REMARK 465 MET B 669
REMARK 465 ALA B 670
REMARK 465 GLY B 671
REMARK 465 GLY B 672
REMARK 465 THR B 673
REMARK 465 LEU B 674
REMARK 465 LEU B 675
REMARK 465 THR B 676
REMARK 465 LEU B 677
REMARK 465 THR B 678
REMARK 465 GLY B 679
REMARK 465 ASN B 680
REMARK 465 TYR B 681
REMARK 465 LEU B 682
REMARK 465 ASN B 683
REMARK 465 SER B 684
REMARK 465 GLY B 685
REMARK 465 ASN B 686
REMARK 465 SER B 687
REMARK 465 ARG B 688
REMARK 465 HIS B 689
REMARK 465 ILE B 690
REMARK 465 SER B 691
REMARK 465 ILE B 692
REMARK 465 GLY B 693
REMARK 465 GLY B 694
REMARK 465 LYS B 695
REMARK 465 THR B 696
REMARK 465 CYS B 697
REMARK 465 THR B 698
REMARK 465 LEU B 699
REMARK 465 LYS B 700
REMARK 465 SER B 701
REMARK 465 VAL B 702
REMARK 465 SER B 703
REMARK 465 ASN B 704
REMARK 465 SER B 705
REMARK 465 ILE B 706
REMARK 465 LEU B 707
REMARK 465 GLU B 708
REMARK 465 CYS B 709
REMARK 465 TYR B 710
REMARK 465 THR B 711
REMARK 465 PRO B 712
REMARK 465 ALA B 713
REMARK 465 GLN B 714
REMARK 465 THR B 715
REMARK 465 ILE B 716
REMARK 465 SER B 717
REMARK 465 THR B 718
REMARK 465 GLU B 719
REMARK 465 PHE B 720
REMARK 465 ALA B 721
REMARK 465 VAL B 722
REMARK 465 LYS B 723
REMARK 465 LEU B 724
REMARK 465 LYS B 725
REMARK 465 ILE B 726
REMARK 465 ASP B 727
REMARK 465 LEU B 728
REMARK 465 ALA B 729
REMARK 465 ASN B 730
REMARK 465 ARG B 731
REMARK 465 GLU B 732
REMARK 465 THR B 733
REMARK 465 SER B 734
REMARK 465 ILE B 735
REMARK 465 PHE B 736
REMARK 465 SER B 737
REMARK 465 TYR B 738
REMARK 465 ARG B 739
REMARK 465 GLU B 740
REMARK 465 ASP B 741
REMARK 465 LEU B 742
REMARK 465 HIS B 743
REMARK 465 HIS B 744
REMARK 465 HIS B 745
REMARK 465 HIS B 746
REMARK 465 HIS B 747
REMARK 465 HIS B 748
REMARK 465 GLY C 33
REMARK 465 GLU C 321
REMARK 465 GLU D 22
REMARK 465 THR D 23
REMARK 465 ARG D 24
REMARK 465 GLU D 25
REMARK 465 CYS D 26
REMARK 465 LYS D 27
REMARK 465 GLU D 28
REMARK 465 ALA D 29
REMARK 465 LEU D 30
REMARK 465 ALA D 31
REMARK 465 LYS D 32
REMARK 465 SER D 33
REMARK 465 GLU D 34
REMARK 465 MET D 35
REMARK 465 ASN D 36
REMARK 465 VAL D 37
REMARK 465 ASN D 38
REMARK 465 MET D 39
REMARK 465 LYS D 40
REMARK 465 CYS D 41
REMARK 465 HIS D 92
REMARK 465 PRO D 93
REMARK 465 ASP D 94
REMARK 465 CYS D 95
REMARK 465 PHE D 96
REMARK 465 PRO D 97
REMARK 465 CYS D 98
REMARK 465 GLN D 99
REMARK 465 ASP D 100
REMARK 465 CYS D 101
REMARK 465 SER D 102
REMARK 465 SER D 103
REMARK 465 LYS D 104
REMARK 465 ALA D 105
REMARK 465 ASN D 106
REMARK 465 LEU D 107
REMARK 465 SER D 108
REMARK 465 GLY D 109
REMARK 465 GLY D 110
REMARK 465 THR D 151
REMARK 465 ALA D 152
REMARK 465 ASP D 153
REMARK 465 ILE D 154
REMARK 465 GLN D 155
REMARK 465 PRO D 164
REMARK 465 GLN D 165
REMARK 465 ILE D 166
REMARK 465 GLU D 167
REMARK 465 PHE D 206
REMARK 465 PRO D 207
REMARK 465 ASP D 208
REMARK 465 HIS D 209
REMARK 465 GLU D 302
REMARK 465 LYS D 303
REMARK 465 ARG D 304
REMARK 465 LYS D 305
REMARK 465 LYS D 306
REMARK 465 ARG D 307
REMARK 465 SER D 308
REMARK 465 THR D 309
REMARK 465 LYS D 310
REMARK 465 VAL D 378
REMARK 465 ASN D 379
REMARK 465 LYS D 380
REMARK 465 ASN D 381
REMARK 465 HIS D 394
REMARK 465 GLU D 395
REMARK 465 HIS D 396
REMARK 465 CYS D 397
REMARK 465 PHE D 398
REMARK 465 ASN D 399
REMARK 465 ARG D 400
REMARK 465 THR D 401
REMARK 465 LEU D 402
REMARK 465 LEU D 403
REMARK 465 ARG D 404
REMARK 465 ASN D 405
REMARK 465 SER D 406
REMARK 465 SER D 407
REMARK 465 GLY D 408
REMARK 465 CYS D 409
REMARK 465 GLU D 410
REMARK 465 ALA D 411
REMARK 465 ARG D 412
REMARK 465 ARG D 413
REMARK 465 ALA D 629
REMARK 465 MET D 630
REMARK 465 ASN D 631
REMARK 465 LYS D 632
REMARK 465 HIS D 633
REMARK 465 ILE D 659
REMARK 465 THR D 660
REMARK 465 SER D 661
REMARK 465 ILE D 662
REMARK 465 SER D 663
REMARK 465 PRO D 664
REMARK 465 LYS D 665
REMARK 465 TYR D 666
REMARK 465 GLY D 667
REMARK 465 PRO D 668
REMARK 465 MET D 669
REMARK 465 ALA D 670
REMARK 465 GLY D 671
REMARK 465 GLY D 672
REMARK 465 THR D 673
REMARK 465 LEU D 674
REMARK 465 LEU D 675
REMARK 465 THR D 676
REMARK 465 LEU D 677
REMARK 465 THR D 678
REMARK 465 GLY D 679
REMARK 465 ASN D 680
REMARK 465 TYR D 681
REMARK 465 LEU D 682
REMARK 465 ASN D 683
REMARK 465 SER D 684
REMARK 465 GLY D 685
REMARK 465 ASN D 686
REMARK 465 SER D 687
REMARK 465 ARG D 688
REMARK 465 HIS D 689
REMARK 465 ILE D 690
REMARK 465 SER D 691
REMARK 465 ILE D 692
REMARK 465 GLY D 693
REMARK 465 GLY D 694
REMARK 465 LYS D 695
REMARK 465 THR D 696
REMARK 465 CYS D 697
REMARK 465 THR D 698
REMARK 465 LEU D 699
REMARK 465 LYS D 700
REMARK 465 SER D 701
REMARK 465 VAL D 702
REMARK 465 SER D 703
REMARK 465 ASN D 704
REMARK 465 SER D 705
REMARK 465 ILE D 706
REMARK 465 LEU D 707
REMARK 465 GLU D 708
REMARK 465 CYS D 709
REMARK 465 TYR D 710
REMARK 465 THR D 711
REMARK 465 PRO D 712
REMARK 465 ALA D 713
REMARK 465 GLN D 714
REMARK 465 THR D 715
REMARK 465 ILE D 716
REMARK 465 SER D 717
REMARK 465 THR D 718
REMARK 465 GLU D 719
REMARK 465 PHE D 720
REMARK 465 ALA D 721
REMARK 465 VAL D 722
REMARK 465 LYS D 723
REMARK 465 LEU D 724
REMARK 465 LYS D 725
REMARK 465 ILE D 726
REMARK 465 ASP D 727
REMARK 465 LEU D 728
REMARK 465 ALA D 729
REMARK 465 ASN D 730
REMARK 465 ARG D 731
REMARK 465 GLU D 732
REMARK 465 THR D 733
REMARK 465 SER D 734
REMARK 465 ILE D 735
REMARK 465 PHE D 736
REMARK 465 SER D 737
REMARK 465 TYR D 738
REMARK 465 ARG D 739
REMARK 465 GLU D 740
REMARK 465 ASP D 741
REMARK 465 LEU D 742
REMARK 465 HIS D 743
REMARK 465 HIS D 744
REMARK 465 HIS D 745
REMARK 465 HIS D 746
REMARK 465 HIS D 747
REMARK 465 HIS D 748
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 VAL B 658 CA C O CB CG1 CG2
REMARK 470 VAL D 658 CA C O CB CG1 CG2
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 THR A 37 146.83 179.35
REMARK 500 VAL A 91 42.53 -95.68
REMARK 500 ASN A 130 -158.88 -98.67
REMARK 500 LYS A 139 -18.12 -50.00
REMARK 500 LEU A 149 52.43 -146.97
REMARK 500 ASN A 174 -148.09 -131.90
REMARK 500 ASP A 195 38.92 73.75
REMARK 500 ASN A 196 -130.01 -120.65
REMARK 500 GLN A 197 26.43 -146.94
REMARK 500 ASN A 218 -147.66 -118.81
REMARK 500 ASP A 233 -33.09 -131.06
REMARK 500 LEU A 237 28.16 -158.08
REMARK 500 LYS A 280 133.79 -20.42
REMARK 500 LEU A 287 74.58 -116.37
REMARK 500 SER A 295 160.00 179.29
REMARK 500 GLU B 59 68.04 39.11
REMARK 500 ASN B 68 -3.97 81.70
REMARK 500 ASN B 115 78.82 -100.70
REMARK 500 TYR B 126 -81.15 -70.03
REMARK 500 VAL B 136 -62.34 -105.90
REMARK 500 HIS B 148 -130.54 91.96
REMARK 500 GLU B 157 76.75 -102.48
REMARK 500 PHE B 162 119.15 -173.94
REMARK 500 PRO B 169 64.30 -67.94
REMARK 500 SER B 186 117.09 -162.72
REMARK 500 ASP B 190 73.56 58.07
REMARK 500 ARG B 191 -7.05 66.82
REMARK 500 ASN B 202 -148.83 -118.30
REMARK 500 SER B 204 154.90 165.32
REMARK 500 LEU B 229 -67.04 -96.04
REMARK 500 ASP B 236 -169.30 -128.25
REMARK 500 SER B 255 141.82 -170.44
REMARK 500 ARG B 266 148.87 -37.29
REMARK 500 ASN B 285 -75.58 67.91
REMARK 500 SER B 286 58.85 -148.86
REMARK 500 SER B 290 65.68 -114.87
REMARK 500 SER B 323 -166.96 -162.40
REMARK 500 ASP B 352 38.71 39.47
REMARK 500 LEU B 386 100.28 -12.40
REMARK 500 MET B 431 44.63 39.18
REMARK 500 SER B 441 137.93 -170.85
REMARK 500 ASN B 478 91.17 179.15
REMARK 500 ASP B 482 173.38 -51.74
REMARK 500 HIS B 542 -61.97 71.02
REMARK 500 SER B 548 -74.95 -59.18
REMARK 500 LEU B 552 -93.21 -71.84
REMARK 500 THR B 555 29.71 -147.74
REMARK 500 LYS B 567 173.05 165.19
REMARK 500 ALA B 573 135.44 -170.37
REMARK 500 LEU B 575 -71.50 -49.98
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU B 168 PRO B 169 -149.86
REMARK 500 PRO B 210 LEU B 211 148.02
REMARK 500 GLY B 627 PRO B 628 58.44
REMARK 500 GLU D 168 PRO D 169 -149.83
REMARK 500 PRO D 210 LEU D 211 148.13
REMARK 500 GLY D 627 PRO D 628 67.43
REMARK 500
REMARK 500 REMARK: NULL
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: 1D0B RELATED DB: PDB
REMARK 900 INTERNALIN B LEUCINE RICH REPEAT DOMAIN
REMARK 900 RELATED ID: 1FYR RELATED DB: PDB
REMARK 900 DIMER FORMATION THROUGH DOMAIN SWAPPING IN THE CRYSTALSTRUCTURE OF
REMARK 900 THE GRB2-SH2 AC- PYVNV COMPLEX
REMARK 900 RELATED ID: 1H6T RELATED DB: PDB
REMARK 900 INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N- TERMINAL DOMAINS.
REMARK 900 RELATED ID: 1M9S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF INTERNALIN B (INLB), A LISTERIAMONOCYTOGENES
REMARK 900 VIRULENCE PROTEIN CONTAINING SH3-LIKEDOMAINS.
REMARK 900 RELATED ID: 1OTM RELATED DB: PDB
REMARK 900 CALCIUM-BINDING MUTANT OF THE INTERNALIN B LRR DOMAIN
REMARK 900 RELATED ID: 1OTN RELATED DB: PDB
REMARK 900 CALCIUM-BINDING MUTANT OF THE INTERNALIN B LRR DOMAIN
REMARK 900 RELATED ID: 1OTO RELATED DB: PDB
REMARK 900 CALCIUM-BINDING MUTANT OF THE INTERNALIN B LRR DOMAIN
REMARK 900 RELATED ID: 1R0P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THEHEPATOCYTE
REMARK 900 GROWTH FACTOR RECEPTOR C-MET IN COMPLEX WITHTHE MICROBIAL ALKALOID
REMARK 900 K-252A
REMARK 900 RELATED ID: 1R1W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THEHEPATOCYTE
REMARK 900 GROWTH FACTOR RECEPTOR C-MET
REMARK 900 RELATED ID: 1SHY RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF HGF BETA-CHAIN IN COMPLEX WITH THESEMA
REMARK 900 DOMAIN OF THE MET RECEPTOR.
REMARK 900 RELATED ID: 1SSL RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PSI DOMAIN FROM THE MET RECEPTOR
REMARK 900 RELATED ID: 1UX3 RELATED DB: PDB
REMARK 900 3D STRUCTURE PREDICTION OF AMINO ACIDS 25 TO 656 OF HUMAN
REMARK 900 HEPATOCYTE GROWTH FACTOR/ SCATTER FACTOR (MET) RECEPTOR
REMARK 900 RELATED ID: 2CEW RELATED DB: PDB
REMARK 900 3D STRUCTURE PREDICTION OF THE IG2-IG4 DOMAINS OF THE ECTODOMAIN
REMARK 900 REGION OF THE HUMAN HEPATOCYTE GROWTH FACTOR-SCATTER FACTOR
REMARK 900 RECEPTOR, MET
REMARK 900 RELATED ID: 2G15 RELATED DB: PDB
REMARK 900 STRUCTURAL CHARACTERIZATION OF AUTOINHIBITED C- MET KINASE
REMARK 900 RELATED ID: 2UZY RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HUMAN RECEPTOR TYROSINE KINASE MET IN COMPLEX WITH
REMARK 900 THE LISTERIA MONOCYTOGENES INVASION PROTEIN INLB: LOW RESOLUTION,
REMARK 900 CRYSTAL FORM II
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CHAIN A+C: RESIDUE 33-35 (GAM) REMAIN AFTER TEV CLEAVAGE
REMARK 999 CHAIN B+D: Y41C AND G344A PROBABLY DUE TO PCR ERROR. N-TERMINAL
REMARK 999 ETR LEFT AFTER PROCESSING OF IG-LEADER SEQUENCE. C-TERMINAL
REMARK 999 DLHHHHHH DUE TO CLONING AND HIS6 TAG.
DBREF 2UZX A 33 35 PDB 2UZX 2UZX 33 35
DBREF 2UZX A 36 321 UNP P25147 INLB_LISMO 36 321
DBREF 2UZX B 22 24 PDB 2UZX 2UZX 22 24
DBREF 2UZX B 25 740 UNP P08581 MET_HUMAN 25 740
DBREF 2UZX B 741 748 PDB 2UZX 2UZX 741 748
DBREF 2UZX C 33 35 PDB 2UZX 2UZX 33 35
DBREF 2UZX C 36 321 UNP P25147 INLB_LISMO 36 321
DBREF 2UZX D 22 24 PDB 2UZX 2UZX 22 24
DBREF 2UZX D 25 740 UNP P08581 MET_HUMAN 25 740
DBREF 2UZX D 741 748 PDB 2UZX 2UZX 741 748
SEQADV 2UZX CYS B 41 UNP P08581 TYR 41 CONFLICT
SEQADV 2UZX ALA B 344 UNP P08581 GLY 344 CONFLICT
SEQADV 2UZX CYS D 41 UNP P08581 TYR 41 CONFLICT
SEQADV 2UZX ALA D 344 UNP P08581 GLY 344 CONFLICT
SEQRES 1 A 289 GLY ALA MET GLU THR ILE THR VAL PRO THR PRO ILE LYS
SEQRES 2 A 289 GLN ILE PHE SER ASP ASP ALA PHE ALA GLU THR ILE LYS
SEQRES 3 A 289 ASP ASN LEU LYS LYS LYS SER VAL THR ASP ALA VAL THR
SEQRES 4 A 289 GLN ASN GLU LEU ASN SER ILE ASP GLN ILE ILE ALA ASN
SEQRES 5 A 289 ASN SER ASP ILE LYS SER VAL GLN GLY ILE GLN TYR LEU
SEQRES 6 A 289 PRO ASN VAL THR LYS LEU PHE LEU ASN GLY ASN LYS LEU
SEQRES 7 A 289 THR ASP ILE LYS PRO LEU ALA ASN LEU LYS ASN LEU GLY
SEQRES 8 A 289 TRP LEU PHE LEU ASP GLU ASN LYS VAL LYS ASP LEU SER
SEQRES 9 A 289 SER LEU LYS ASP LEU LYS LYS LEU LYS SER LEU SER LEU
SEQRES 10 A 289 GLU HIS ASN GLY ILE SER ASP ILE ASN GLY LEU VAL HIS
SEQRES 11 A 289 LEU PRO GLN LEU GLU SER LEU TYR LEU GLY ASN ASN LYS
SEQRES 12 A 289 ILE THR ASP ILE THR VAL LEU SER ARG LEU THR LYS LEU
SEQRES 13 A 289 ASP THR LEU SER LEU GLU ASP ASN GLN ILE SER ASP ILE
SEQRES 14 A 289 VAL PRO LEU ALA GLY LEU THR LYS LEU GLN ASN LEU TYR
SEQRES 15 A 289 LEU SER LYS ASN HIS ILE SER ASP LEU ARG ALA LEU ALA
SEQRES 16 A 289 GLY LEU LYS ASN LEU ASP VAL LEU GLU LEU PHE SER GLN
SEQRES 17 A 289 GLU CYS LEU ASN LYS PRO ILE ASN HIS GLN SER ASN LEU
SEQRES 18 A 289 VAL VAL PRO ASN THR VAL LYS ASN THR ASP GLY SER LEU
SEQRES 19 A 289 VAL THR PRO GLU ILE ILE SER ASP ASP GLY ASP TYR GLU
SEQRES 20 A 289 LYS PRO ASN VAL LYS TRP HIS LEU PRO GLU PHE THR ASN
SEQRES 21 A 289 GLU VAL SER PHE ILE PHE TYR GLN PRO VAL THR ILE GLY
SEQRES 22 A 289 LYS ALA LYS ALA ARG PHE HIS GLY ARG VAL THR GLN PRO
SEQRES 23 A 289 LEU LYS GLU
SEQRES 1 B 727 GLU THR ARG GLU CYS LYS GLU ALA LEU ALA LYS SER GLU
SEQRES 2 B 727 MET ASN VAL ASN MET LYS CYS GLN LEU PRO ASN PHE THR
SEQRES 3 B 727 ALA GLU THR PRO ILE GLN ASN VAL ILE LEU HIS GLU HIS
SEQRES 4 B 727 HIS ILE PHE LEU GLY ALA THR ASN TYR ILE TYR VAL LEU
SEQRES 5 B 727 ASN GLU GLU ASP LEU GLN LYS VAL ALA GLU TYR LYS THR
SEQRES 6 B 727 GLY PRO VAL LEU GLU HIS PRO ASP CYS PHE PRO CYS GLN
SEQRES 7 B 727 ASP CYS SER SER LYS ALA ASN LEU SER GLY GLY VAL TRP
SEQRES 8 B 727 LYS ASP ASN ILE ASN MET ALA LEU VAL VAL ASP THR TYR
SEQRES 9 B 727 TYR ASP ASP GLN LEU ILE SER CYS GLY SER VAL ASN ARG
SEQRES 10 B 727 GLY THR CYS GLN ARG HIS VAL PHE PRO HIS ASN HIS THR
SEQRES 11 B 727 ALA ASP ILE GLN SER GLU VAL HIS CYS ILE PHE SER PRO
SEQRES 12 B 727 GLN ILE GLU GLU PRO SER GLN CYS PRO ASP CYS VAL VAL
SEQRES 13 B 727 SER ALA LEU GLY ALA LYS VAL LEU SER SER VAL LYS ASP
SEQRES 14 B 727 ARG PHE ILE ASN PHE PHE VAL GLY ASN THR ILE ASN SER
SEQRES 15 B 727 SER TYR PHE PRO ASP HIS PRO LEU HIS SER ILE SER VAL
SEQRES 16 B 727 ARG ARG LEU LYS GLU THR LYS ASP GLY PHE MET PHE LEU
SEQRES 17 B 727 THR ASP GLN SER TYR ILE ASP VAL LEU PRO GLU PHE ARG
SEQRES 18 B 727 ASP SER TYR PRO ILE LYS TYR VAL HIS ALA PHE GLU SER
SEQRES 19 B 727 ASN ASN PHE ILE TYR PHE LEU THR VAL GLN ARG GLU THR
SEQRES 20 B 727 LEU ASP ALA GLN THR PHE HIS THR ARG ILE ILE ARG PHE
SEQRES 21 B 727 CYS SER ILE ASN SER GLY LEU HIS SER TYR MET GLU MET
SEQRES 22 B 727 PRO LEU GLU CYS ILE LEU THR GLU LYS ARG LYS LYS ARG
SEQRES 23 B 727 SER THR LYS LYS GLU VAL PHE ASN ILE LEU GLN ALA ALA
SEQRES 24 B 727 TYR VAL SER LYS PRO GLY ALA GLN LEU ALA ARG GLN ILE
SEQRES 25 B 727 GLY ALA SER LEU ASN ASP ASP ILE LEU PHE ALA VAL PHE
SEQRES 26 B 727 ALA GLN SER LYS PRO ASP SER ALA GLU PRO MET ASP ARG
SEQRES 27 B 727 SER ALA MET CYS ALA PHE PRO ILE LYS TYR VAL ASN ASP
SEQRES 28 B 727 PHE PHE ASN LYS ILE VAL ASN LYS ASN ASN VAL ARG CYS
SEQRES 29 B 727 LEU GLN HIS PHE TYR GLY PRO ASN HIS GLU HIS CYS PHE
SEQRES 30 B 727 ASN ARG THR LEU LEU ARG ASN SER SER GLY CYS GLU ALA
SEQRES 31 B 727 ARG ARG ASP GLU TYR ARG THR GLU PHE THR THR ALA LEU
SEQRES 32 B 727 GLN ARG VAL ASP LEU PHE MET GLY GLN PHE SER GLU VAL
SEQRES 33 B 727 LEU LEU THR SER ILE SER THR PHE ILE LYS GLY ASP LEU
SEQRES 34 B 727 THR ILE ALA ASN LEU GLY THR SER GLU GLY ARG PHE MET
SEQRES 35 B 727 GLN VAL VAL VAL SER ARG SER GLY PRO SER THR PRO HIS
SEQRES 36 B 727 VAL ASN PHE LEU LEU ASP SER HIS PRO VAL SER PRO GLU
SEQRES 37 B 727 VAL ILE VAL GLU HIS THR LEU ASN GLN ASN GLY TYR THR
SEQRES 38 B 727 LEU VAL ILE THR GLY LYS LYS ILE THR LYS ILE PRO LEU
SEQRES 39 B 727 ASN GLY LEU GLY CYS ARG HIS PHE GLN SER CYS SER GLN
SEQRES 40 B 727 CYS LEU SER ALA PRO PRO PHE VAL GLN CYS GLY TRP CYS
SEQRES 41 B 727 HIS ASP LYS CYS VAL ARG SER GLU GLU CYS LEU SER GLY
SEQRES 42 B 727 THR TRP THR GLN GLN ILE CYS LEU PRO ALA ILE TYR LYS
SEQRES 43 B 727 VAL PHE PRO ASN SER ALA PRO LEU GLU GLY GLY THR ARG
SEQRES 44 B 727 LEU THR ILE CYS GLY TRP ASP PHE GLY PHE ARG ARG ASN
SEQRES 45 B 727 ASN LYS PHE ASP LEU LYS LYS THR ARG VAL LEU LEU GLY
SEQRES 46 B 727 ASN GLU SER CYS THR LEU THR LEU SER GLU SER THR MET
SEQRES 47 B 727 ASN THR LEU LYS CYS THR VAL GLY PRO ALA MET ASN LYS
SEQRES 48 B 727 HIS PHE ASN MET SER ILE ILE ILE SER ASN GLY HIS GLY
SEQRES 49 B 727 THR THR GLN TYR SER THR PHE SER TYR VAL ASP PRO VAL
SEQRES 50 B 727 ILE THR SER ILE SER PRO LYS TYR GLY PRO MET ALA GLY
SEQRES 51 B 727 GLY THR LEU LEU THR LEU THR GLY ASN TYR LEU ASN SER
SEQRES 52 B 727 GLY ASN SER ARG HIS ILE SER ILE GLY GLY LYS THR CYS
SEQRES 53 B 727 THR LEU LYS SER VAL SER ASN SER ILE LEU GLU CYS TYR
SEQRES 54 B 727 THR PRO ALA GLN THR ILE SER THR GLU PHE ALA VAL LYS
SEQRES 55 B 727 LEU LYS ILE ASP LEU ALA ASN ARG GLU THR SER ILE PHE
SEQRES 56 B 727 SER TYR ARG GLU ASP LEU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 289 GLY ALA MET GLU THR ILE THR VAL PRO THR PRO ILE LYS
SEQRES 2 C 289 GLN ILE PHE SER ASP ASP ALA PHE ALA GLU THR ILE LYS
SEQRES 3 C 289 ASP ASN LEU LYS LYS LYS SER VAL THR ASP ALA VAL THR
SEQRES 4 C 289 GLN ASN GLU LEU ASN SER ILE ASP GLN ILE ILE ALA ASN
SEQRES 5 C 289 ASN SER ASP ILE LYS SER VAL GLN GLY ILE GLN TYR LEU
SEQRES 6 C 289 PRO ASN VAL THR LYS LEU PHE LEU ASN GLY ASN LYS LEU
SEQRES 7 C 289 THR ASP ILE LYS PRO LEU ALA ASN LEU LYS ASN LEU GLY
SEQRES 8 C 289 TRP LEU PHE LEU ASP GLU ASN LYS VAL LYS ASP LEU SER
SEQRES 9 C 289 SER LEU LYS ASP LEU LYS LYS LEU LYS SER LEU SER LEU
SEQRES 10 C 289 GLU HIS ASN GLY ILE SER ASP ILE ASN GLY LEU VAL HIS
SEQRES 11 C 289 LEU PRO GLN LEU GLU SER LEU TYR LEU GLY ASN ASN LYS
SEQRES 12 C 289 ILE THR ASP ILE THR VAL LEU SER ARG LEU THR LYS LEU
SEQRES 13 C 289 ASP THR LEU SER LEU GLU ASP ASN GLN ILE SER ASP ILE
SEQRES 14 C 289 VAL PRO LEU ALA GLY LEU THR LYS LEU GLN ASN LEU TYR
SEQRES 15 C 289 LEU SER LYS ASN HIS ILE SER ASP LEU ARG ALA LEU ALA
SEQRES 16 C 289 GLY LEU LYS ASN LEU ASP VAL LEU GLU LEU PHE SER GLN
SEQRES 17 C 289 GLU CYS LEU ASN LYS PRO ILE ASN HIS GLN SER ASN LEU
SEQRES 18 C 289 VAL VAL PRO ASN THR VAL LYS ASN THR ASP GLY SER LEU
SEQRES 19 C 289 VAL THR PRO GLU ILE ILE SER ASP ASP GLY ASP TYR GLU
SEQRES 20 C 289 LYS PRO ASN VAL LYS TRP HIS LEU PRO GLU PHE THR ASN
SEQRES 21 C 289 GLU VAL SER PHE ILE PHE TYR GLN PRO VAL THR ILE GLY
SEQRES 22 C 289 LYS ALA LYS ALA ARG PHE HIS GLY ARG VAL THR GLN PRO
SEQRES 23 C 289 LEU LYS GLU
SEQRES 1 D 727 GLU THR ARG GLU CYS LYS GLU ALA LEU ALA LYS SER GLU
SEQRES 2 D 727 MET ASN VAL ASN MET LYS CYS GLN LEU PRO ASN PHE THR
SEQRES 3 D 727 ALA GLU THR PRO ILE GLN ASN VAL ILE LEU HIS GLU HIS
SEQRES 4 D 727 HIS ILE PHE LEU GLY ALA THR ASN TYR ILE TYR VAL LEU
SEQRES 5 D 727 ASN GLU GLU ASP LEU GLN LYS VAL ALA GLU TYR LYS THR
SEQRES 6 D 727 GLY PRO VAL LEU GLU HIS PRO ASP CYS PHE PRO CYS GLN
SEQRES 7 D 727 ASP CYS SER SER LYS ALA ASN LEU SER GLY GLY VAL TRP
SEQRES 8 D 727 LYS ASP ASN ILE ASN MET ALA LEU VAL VAL ASP THR TYR
SEQRES 9 D 727 TYR ASP ASP GLN LEU ILE SER CYS GLY SER VAL ASN ARG
SEQRES 10 D 727 GLY THR CYS GLN ARG HIS VAL PHE PRO HIS ASN HIS THR
SEQRES 11 D 727 ALA ASP ILE GLN SER GLU VAL HIS CYS ILE PHE SER PRO
SEQRES 12 D 727 GLN ILE GLU GLU PRO SER GLN CYS PRO ASP CYS VAL VAL
SEQRES 13 D 727 SER ALA LEU GLY ALA LYS VAL LEU SER SER VAL LYS ASP
SEQRES 14 D 727 ARG PHE ILE ASN PHE PHE VAL GLY ASN THR ILE ASN SER
SEQRES 15 D 727 SER TYR PHE PRO ASP HIS PRO LEU HIS SER ILE SER VAL
SEQRES 16 D 727 ARG ARG LEU LYS GLU THR LYS ASP GLY PHE MET PHE LEU
SEQRES 17 D 727 THR ASP GLN SER TYR ILE ASP VAL LEU PRO GLU PHE ARG
SEQRES 18 D 727 ASP SER TYR PRO ILE LYS TYR VAL HIS ALA PHE GLU SER
SEQRES 19 D 727 ASN ASN PHE ILE TYR PHE LEU THR VAL GLN ARG GLU THR
SEQRES 20 D 727 LEU ASP ALA GLN THR PHE HIS THR ARG ILE ILE ARG PHE
SEQRES 21 D 727 CYS SER ILE ASN SER GLY LEU HIS SER TYR MET GLU MET
SEQRES 22 D 727 PRO LEU GLU CYS ILE LEU THR GLU LYS ARG LYS LYS ARG
SEQRES 23 D 727 SER THR LYS LYS GLU VAL PHE ASN ILE LEU GLN ALA ALA
SEQRES 24 D 727 TYR VAL SER LYS PRO GLY ALA GLN LEU ALA ARG GLN ILE
SEQRES 25 D 727 GLY ALA SER LEU ASN ASP ASP ILE LEU PHE ALA VAL PHE
SEQRES 26 D 727 ALA GLN SER LYS PRO ASP SER ALA GLU PRO MET ASP ARG
SEQRES 27 D 727 SER ALA MET CYS ALA PHE PRO ILE LYS TYR VAL ASN ASP
SEQRES 28 D 727 PHE PHE ASN LYS ILE VAL ASN LYS ASN ASN VAL ARG CYS
SEQRES 29 D 727 LEU GLN HIS PHE TYR GLY PRO ASN HIS GLU HIS CYS PHE
SEQRES 30 D 727 ASN ARG THR LEU LEU ARG ASN SER SER GLY CYS GLU ALA
SEQRES 31 D 727 ARG ARG ASP GLU TYR ARG THR GLU PHE THR THR ALA LEU
SEQRES 32 D 727 GLN ARG VAL ASP LEU PHE MET GLY GLN PHE SER GLU VAL
SEQRES 33 D 727 LEU LEU THR SER ILE SER THR PHE ILE LYS GLY ASP LEU
SEQRES 34 D 727 THR ILE ALA ASN LEU GLY THR SER GLU GLY ARG PHE MET
SEQRES 35 D 727 GLN VAL VAL VAL SER ARG SER GLY PRO SER THR PRO HIS
SEQRES 36 D 727 VAL ASN PHE LEU LEU ASP SER HIS PRO VAL SER PRO GLU
SEQRES 37 D 727 VAL ILE VAL GLU HIS THR LEU ASN GLN ASN GLY TYR THR
SEQRES 38 D 727 LEU VAL ILE THR GLY LYS LYS ILE THR LYS ILE PRO LEU
SEQRES 39 D 727 ASN GLY LEU GLY CYS ARG HIS PHE GLN SER CYS SER GLN
SEQRES 40 D 727 CYS LEU SER ALA PRO PRO PHE VAL GLN CYS GLY TRP CYS
SEQRES 41 D 727 HIS ASP LYS CYS VAL ARG SER GLU GLU CYS LEU SER GLY
SEQRES 42 D 727 THR TRP THR GLN GLN ILE CYS LEU PRO ALA ILE TYR LYS
SEQRES 43 D 727 VAL PHE PRO ASN SER ALA PRO LEU GLU GLY GLY THR ARG
SEQRES 44 D 727 LEU THR ILE CYS GLY TRP ASP PHE GLY PHE ARG ARG ASN
SEQRES 45 D 727 ASN LYS PHE ASP LEU LYS LYS THR ARG VAL LEU LEU GLY
SEQRES 46 D 727 ASN GLU SER CYS THR LEU THR LEU SER GLU SER THR MET
SEQRES 47 D 727 ASN THR LEU LYS CYS THR VAL GLY PRO ALA MET ASN LYS
SEQRES 48 D 727 HIS PHE ASN MET SER ILE ILE ILE SER ASN GLY HIS GLY
SEQRES 49 D 727 THR THR GLN TYR SER THR PHE SER TYR VAL ASP PRO VAL
SEQRES 50 D 727 ILE THR SER ILE SER PRO LYS TYR GLY PRO MET ALA GLY
SEQRES 51 D 727 GLY THR LEU LEU THR LEU THR GLY ASN TYR LEU ASN SER
SEQRES 52 D 727 GLY ASN SER ARG HIS ILE SER ILE GLY GLY LYS THR CYS
SEQRES 53 D 727 THR LEU LYS SER VAL SER ASN SER ILE LEU GLU CYS TYR
SEQRES 54 D 727 THR PRO ALA GLN THR ILE SER THR GLU PHE ALA VAL LYS
SEQRES 55 D 727 LEU LYS ILE ASP LEU ALA ASN ARG GLU THR SER ILE PHE
SEQRES 56 D 727 SER TYR ARG GLU ASP LEU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ILE A 44 PHE A 48 1 5
HELIX 2 2 ASP A 50 LEU A 61 1 12
HELIX 3 3 THR A 71 SER A 77 1 7
HELIX 4 4 GLY A 93 LEU A 97 5 5
HELIX 5 5 ILE A 113 ALA A 117 5 5
HELIX 6 6 ASP A 134 LYS A 139 5 6
HELIX 7 7 ILE A 157 LEU A 163 5 7
HELIX 8 8 ILE A 179 ARG A 184 5 6
HELIX 9 9 ILE A 201 ALA A 205 5 5
HELIX 10 10 LEU A 223 LEU A 229 5 7
HELIX 11 11 THR B 230 GLN B 232 5 3
HELIX 12 12 LEU B 238 ARG B 242 5 5
HELIX 13 13 GLY B 326 GLY B 334 1 9
HELIX 14 14 ILE B 367 ASN B 375 1 9
HELIX 15 15 LEU B 386 GLY B 391 1 6
HELIX 16 16 SER B 525 ALA B 532 1 8
HELIX 17 17 PRO B 533 VAL B 536 5 4
HELIX 18 18 LEU B 614 SER B 617 5 4
HELIX 19 19 ILE C 44 PHE C 48 1 5
HELIX 20 20 ASP C 50 LEU C 61 1 12
HELIX 21 21 THR C 71 SER C 77 1 7
HELIX 22 22 GLY C 93 LEU C 97 5 5
HELIX 23 23 ILE C 113 ALA C 117 5 5
HELIX 24 24 ASP C 134 LYS C 139 5 6
HELIX 25 25 ILE C 157 LEU C 163 5 7
HELIX 26 26 ILE C 179 ARG C 184 5 6
HELIX 27 27 ILE C 201 ALA C 205 5 5
HELIX 28 28 LEU C 223 LEU C 229 5 7
HELIX 29 29 THR D 230 GLN D 232 5 3
HELIX 30 30 LEU D 238 ARG D 242 5 5
HELIX 31 31 GLY D 326 GLY D 334 1 9
HELIX 32 32 ILE D 367 ASN D 375 1 9
HELIX 33 33 LEU D 386 GLY D 391 1 6
HELIX 34 34 SER D 525 ALA D 532 1 8
HELIX 35 35 PRO D 533 VAL D 536 5 4
HELIX 36 36 LEU D 614 SER D 617 5 4
SHEET 1 AA 2 THR A 42 PRO A 43 0
SHEET 2 AA 2 ALA A 69 VAL A 70 -1 O VAL A 70 N THR A 42
SHEET 1 AB 8 GLN A 80 ILE A 82 0
SHEET 2 AB 8 LYS A 102 PHE A 104 1 O LYS A 102 N ILE A 81
SHEET 3 AB 8 TRP A 124 PHE A 126 1 O TRP A 124 N LEU A 103
SHEET 4 AB 8 SER A 146 SER A 148 1 O SER A 146 N LEU A 125
SHEET 5 AB 8 SER A 168 TYR A 170 1 O SER A 168 N LEU A 147
SHEET 6 AB 8 THR A 190 SER A 192 1 O THR A 190 N LEU A 169
SHEET 7 AB 8 ASN A 212 TYR A 214 1 O ASN A 212 N LEU A 191
SHEET 8 AB 8 VAL A 234 GLU A 236 1 O VAL A 234 N LEU A 213
SHEET 1 AC 4 ILE A 247 ASN A 248 0
SHEET 2 AC 4 ALA A 307 LYS A 320 1 O PRO A 318 N ILE A 247
SHEET 3 AC 4 GLU A 293 ILE A 304 -1 O VAL A 294 N GLN A 317
SHEET 4 AC 4 ILE A 271 ILE A 272 -1 O ILE A 271 N ILE A 297
SHEET 1 AD 3 VAL A 254 PRO A 256 0
SHEET 2 AD 3 ASN A 282 LYS A 284 -1 O VAL A 283 N VAL A 255
SHEET 3 AD 3 ASP A 277 GLU A 279 -1 O ASP A 277 N LYS A 284
SHEET 1 BA 4 ASN B 45 THR B 47 0
SHEET 2 BA 4 LYS B 509 PRO B 514 -1 O ILE B 510 N PHE B 46
SHEET 3 BA 4 TYR B 501 THR B 506 -1 O THR B 502 N ILE B 513
SHEET 4 BA 4 VAL B 490 GLU B 493 -1 O ILE B 491 N LEU B 503
SHEET 1 BB 4 ILE B 52 HIS B 58 0
SHEET 2 BB 4 HIS B 61 ALA B 66 -1 O HIS B 61 N HIS B 58
SHEET 3 BB 4 TYR B 69 ASN B 74 -1 O TYR B 69 N ALA B 66
SHEET 4 BB 4 LYS B 80 TYR B 84 -1 N VAL B 81 O VAL B 72
SHEET 1 BC 4 ALA B 119 ASP B 123 0
SHEET 2 BC 4 GLN B 129 CYS B 133 -1 O GLN B 129 N ASP B 123
SHEET 3 BC 4 CYS B 141 VAL B 145 -1 O GLN B 142 N SER B 132
SHEET 4 BC 4 GLU B 157 VAL B 158 -1 O GLU B 157 N VAL B 145
SHEET 1 BD 4 ALA B 182 LYS B 189 0
SHEET 2 BD 4 PHE B 192 ASN B 199 -1 O PHE B 192 N LYS B 189
SHEET 3 BD 4 ILE B 214 LEU B 219 -1 O SER B 215 N VAL B 197
SHEET 4 BD 4 TYR B 234 ILE B 235 -1 O ILE B 235 N ILE B 214
SHEET 1 BE 4 ALA B 182 LYS B 189 0
SHEET 2 BE 4 PHE B 192 ASN B 199 -1 O PHE B 192 N LYS B 189
SHEET 3 BE 4 ILE B 214 LEU B 219 -1 O SER B 215 N VAL B 197
SHEET 4 BE 4 PHE B 226 MET B 227 -1 O MET B 227 N ARG B 218
SHEET 1 BF 6 ILE B 247 SER B 255 0
SHEET 2 BF 6 PHE B 258 GLN B 265 -1 O PHE B 258 N SER B 255
SHEET 3 BF 6 ARG B 277 PHE B 281 -1 O ARG B 277 N THR B 263
SHEET 4 BF 6 MET B 292 LEU B 300 -1 O MET B 292 N ARG B 280
SHEET 5 BF 6 THR B 418 PHE B 420 1 O THR B 418 N GLU B 293
SHEET 6 BF 6 VAL B 383 ARG B 384 -1 O ARG B 384 N GLU B 419
SHEET 1 BG 5 ILE B 247 SER B 255 0
SHEET 2 BG 5 PHE B 258 GLN B 265 -1 O PHE B 258 N SER B 255
SHEET 3 BG 5 ARG B 277 PHE B 281 -1 O ARG B 277 N THR B 263
SHEET 4 BG 5 MET B 292 LEU B 300 -1 O MET B 292 N ARG B 280
SHEET 5 BG 5 LEU B 424 VAL B 427 1 O LEU B 424 N GLU B 297
SHEET 1 BH 3 ILE B 316 SER B 323 0
SHEET 2 BH 3 ILE B 341 SER B 349 -1 O ILE B 341 N SER B 323
SHEET 3 BH 3 PRO B 356 PRO B 366 -1 N MET B 357 O GLN B 348
SHEET 1 BI 3 LEU B 439 LYS B 447 0
SHEET 2 BI 3 LEU B 450 THR B 457 -1 O LEU B 450 N LYS B 447
SHEET 3 BI 3 PHE B 462 VAL B 466 -1 O MET B 463 N LEU B 455
SHEET 1 BJ 2 CYS B 538 TRP B 540 0
SHEET 2 BJ 2 CYS B 545 ARG B 547 -1 O VAL B 546 N GLY B 539
SHEET 1 BK 4 ALA B 564 PHE B 569 0
SHEET 2 BK 4 ARG B 580 TRP B 586 -1 O THR B 582 N PHE B 569
SHEET 3 BK 4 THR B 621 THR B 625 -1 O LEU B 622 N ILE B 583
SHEET 4 BK 4 THR B 611 LEU B 612 -1 O THR B 611 N THR B 625
SHEET 1 BL 2 PHE B 590 ARG B 592 0
SHEET 2 BL 2 LYS B 595 ASP B 597 -1 O LYS B 595 N ARG B 592
SHEET 1 BM 4 GLU B 608 SER B 609 0
SHEET 2 BM 4 ARG B 602 LEU B 605 -1 N LEU B 605 O GLU B 608
SHEET 3 BM 4 SER B 637 SER B 641 -1 O ILE B 639 N LEU B 604
SHEET 4 BM 4 THR B 646 SER B 650 -1 O THR B 647 N ILE B 640
SHEET 1 CA 2 THR C 42 PRO C 43 0
SHEET 2 CA 2 ALA C 69 VAL C 70 -1 O VAL C 70 N THR C 42
SHEET 1 CB 8 GLN C 80 ILE C 82 0
SHEET 2 CB 8 LYS C 102 PHE C 104 1 O LYS C 102 N ILE C 81
SHEET 3 CB 8 TRP C 124 PHE C 126 1 O TRP C 124 N LEU C 103
SHEET 4 CB 8 SER C 146 SER C 148 1 O SER C 146 N LEU C 125
SHEET 5 CB 8 SER C 168 TYR C 170 1 O SER C 168 N LEU C 147
SHEET 6 CB 8 THR C 190 SER C 192 1 O THR C 190 N LEU C 169
SHEET 7 CB 8 ASN C 212 TYR C 214 1 O ASN C 212 N LEU C 191
SHEET 8 CB 8 VAL C 234 GLU C 236 1 O VAL C 234 N LEU C 213
SHEET 1 CC 4 ILE C 247 ASN C 248 0
SHEET 2 CC 4 ALA C 307 LYS C 320 1 O PRO C 318 N ILE C 247
SHEET 3 CC 4 GLU C 293 ILE C 304 -1 O VAL C 294 N GLN C 317
SHEET 4 CC 4 ILE C 271 ILE C 272 -1 O ILE C 271 N ILE C 297
SHEET 1 CD 3 VAL C 254 PRO C 256 0
SHEET 2 CD 3 ASN C 282 LYS C 284 -1 O VAL C 283 N VAL C 255
SHEET 3 CD 3 ASP C 277 GLU C 279 -1 O ASP C 277 N LYS C 284
SHEET 1 DA 4 ASN D 45 THR D 47 0
SHEET 2 DA 4 LYS D 509 PRO D 514 -1 O ILE D 510 N PHE D 46
SHEET 3 DA 4 TYR D 501 THR D 506 -1 O THR D 502 N ILE D 513
SHEET 4 DA 4 VAL D 490 GLU D 493 -1 O ILE D 491 N LEU D 503
SHEET 1 DB 4 ILE D 52 HIS D 58 0
SHEET 2 DB 4 HIS D 61 ALA D 66 -1 O HIS D 61 N HIS D 58
SHEET 3 DB 4 TYR D 69 ASN D 74 -1 O TYR D 69 N ALA D 66
SHEET 4 DB 4 LYS D 80 TYR D 84 -1 N VAL D 81 O VAL D 72
SHEET 1 DC 4 ALA D 119 ASP D 123 0
SHEET 2 DC 4 GLN D 129 CYS D 133 -1 O GLN D 129 N ASP D 123
SHEET 3 DC 4 CYS D 141 VAL D 145 -1 O GLN D 142 N SER D 132
SHEET 4 DC 4 GLU D 157 VAL D 158 -1 O GLU D 157 N VAL D 145
SHEET 1 DD 4 ALA D 182 LYS D 189 0
SHEET 2 DD 4 PHE D 192 ASN D 199 -1 O PHE D 192 N LYS D 189
SHEET 3 DD 4 ILE D 214 LEU D 219 -1 O SER D 215 N VAL D 197
SHEET 4 DD 4 TYR D 234 ILE D 235 -1 O ILE D 235 N ILE D 214
SHEET 1 DE 4 ALA D 182 LYS D 189 0
SHEET 2 DE 4 PHE D 192 ASN D 199 -1 O PHE D 192 N LYS D 189
SHEET 3 DE 4 ILE D 214 LEU D 219 -1 O SER D 215 N VAL D 197
SHEET 4 DE 4 PHE D 226 MET D 227 -1 O MET D 227 N ARG D 218
SHEET 1 DF11 ILE D 247 SER D 255 0
SHEET 2 DF11 PHE D 258 GLN D 265 -1 O PHE D 258 N SER D 255
SHEET 3 DF11 ARG D 277 PHE D 281 -1 O ARG D 277 N THR D 263
SHEET 4 DF11 MET D 292 LEU D 300 -1 O MET D 292 N ARG D 280
SHEET 5 DF11 GLU D 312 PHE D 314 -1 O GLU D 312 N LEU D 300
SHEET 6 DF11 MET D 292 LEU D 300 -1 O CYS D 298 N PHE D 314
SHEET 7 DF11 VAL D 383 ARG D 384 0
SHEET 8 DF11 THR D 418 PHE D 420 -1 O GLU D 419 N ARG D 384
SHEET 9 DF11 MET D 292 LEU D 300 1 O GLU D 293 N PHE D 420
SHEET 10 DF11 LEU D 424 VAL D 427 1 O LEU D 424 N GLU D 297
SHEET 11 DF11 MET D 292 LEU D 300 1 O PRO D 295 N LEU D 424
SHEET 1 DG 3 ILE D 316 SER D 323 0
SHEET 2 DG 3 ILE D 341 SER D 349 -1 O ILE D 341 N SER D 323
SHEET 3 DG 3 PRO D 356 PRO D 366 -1 N MET D 357 O GLN D 348
SHEET 1 DH 3 LEU D 439 LYS D 447 0
SHEET 2 DH 3 LEU D 450 THR D 457 -1 O LEU D 450 N LYS D 447
SHEET 3 DH 3 PHE D 462 VAL D 466 -1 O MET D 463 N LEU D 455
SHEET 1 DI 2 CYS D 538 TRP D 540 0
SHEET 2 DI 2 CYS D 545 ARG D 547 -1 O VAL D 546 N GLY D 539
SHEET 1 DJ 4 ALA D 564 PHE D 569 0
SHEET 2 DJ 4 ARG D 580 TRP D 586 -1 O THR D 582 N PHE D 569
SHEET 3 DJ 4 THR D 621 THR D 625 -1 O LEU D 622 N ILE D 583
SHEET 4 DJ 4 THR D 611 LEU D 612 -1 O THR D 611 N THR D 625
SHEET 1 DK 2 PHE D 590 ARG D 592 0
SHEET 2 DK 2 LYS D 595 ASP D 597 -1 O LYS D 595 N ARG D 592
SHEET 1 DL 4 GLU D 608 SER D 609 0
SHEET 2 DL 4 ARG D 602 LEU D 605 -1 N LEU D 605 O GLU D 608
SHEET 3 DL 4 SER D 637 SER D 641 -1 O ILE D 639 N LEU D 604
SHEET 4 DL 4 THR D 646 SER D 650 -1 O THR D 647 N ILE D 640
SSBOND 1 CYS B 133 CYS B 141 1555 1555 2.04
SSBOND 2 CYS B 172 CYS B 175 1555 1555 2.04
SSBOND 3 CYS B 298 CYS B 363 1555 1555 2.05
SSBOND 4 CYS B 520 CYS B 538 1555 1555 2.03
SSBOND 5 CYS B 526 CYS B 561 1555 1555 2.02
SSBOND 6 CYS B 529 CYS B 545 1555 1555 2.03
SSBOND 7 CYS B 541 CYS B 551 1555 1555 2.04
SSBOND 8 CYS B 610 CYS B 624 1555 1555 2.03
SSBOND 9 CYS D 133 CYS D 141 1555 1555 2.04
SSBOND 10 CYS D 172 CYS D 175 1555 1555 2.04
SSBOND 11 CYS D 298 CYS D 363 1555 1555 2.05
SSBOND 12 CYS D 520 CYS D 538 1555 1555 2.04
SSBOND 13 CYS D 526 CYS D 561 1555 1555 2.03
SSBOND 14 CYS D 529 CYS D 545 1555 1555 2.03
SSBOND 15 CYS D 541 CYS D 551 1555 1555 2.04
SSBOND 16 CYS D 610 CYS D 624 1555 1555 2.03
CISPEP 1 LYS A 280 PRO A 281 0 2.71
CISPEP 2 PHE B 569 PRO B 570 0 -1.79
CISPEP 3 LYS C 280 PRO C 281 0 2.68
CISPEP 4 PHE D 569 PRO D 570 0 -1.82
CRYST1 214.500 66.700 181.500 90.00 123.30 90.00 C 1 2 1 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 0.004662 0.000000 0.003062 0.00000
SCALE2 0.000000 0.014993 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006592 0.00000
MTRIX1 1 -0.998680 -0.051250 0.003880 56.01252 1
MTRIX2 1 -0.051390 0.997280 -0.052890 3.11825 1
MTRIX3 1 -0.001160 -0.053020 -0.998590 74.68121 1
MTRIX1 2 -0.999330 -0.036650 -0.000660 56.52769 1
MTRIX2 2 -0.036580 0.998360 -0.044140 2.51149 1
MTRIX3 2 0.002280 -0.044090 -0.999020 74.79391 1
(ATOM LINES ARE NOT SHOWN.)
END
