HEADER HYDROLASE 11-APR-03 1P15
TITLE CRYSTAL STRUCTURE OF THE D2 DOMAIN OF RPTPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE PHOSPHATASE ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: D2 DOMAIN;
COMPND 5 SYNONYM: R-PTP- ALPHA, LCA-RELATED PHOSPHATASE;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTPRA OR LRP OR PTPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSMEMBRANE, HYDROLASE, PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.D.SONNENBURG,A.BILWES,T.HUNTER,J.P.NOEL
REVDAT 3 14-FEB-24 1P15 1 REMARK
REVDAT 2 24-FEB-09 1P15 1 VERSN
REVDAT 1 19-AUG-03 1P15 0
JRNL AUTH E.D.SONNENBURG,A.BILWES,T.HUNTER,J.P.NOEL
JRNL TITL THE STRUCTURE OF THE MEMBRANE DISTAL PHOSPHATASE DOMAIN OF
JRNL TITL 2 RPTPALPHA REVEALS INTERDOMAIN FLEXIBILITY AND AN SH2 DOMAIN
JRNL TITL 3 INTERACTION REGION.
JRNL REF BIOCHEMISTRY V. 42 7904 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12834342
JRNL DOI 10.1021/BI0340503
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 38121
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) : 0.203
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3468
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5766
REMARK 3 BIN R VALUE (WORKING SET) : 0.3490
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 630
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3974
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.90000
REMARK 3 B12 (A**2) : 2.83000
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) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.45
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
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) : 1.460 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.560 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.620 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.560 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 53.83
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1P15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000018885.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 51.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM SUCCINATE, LITHIUM
REMARK 280 SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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 50.88567
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 101.77133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 PHE A 787
REMARK 465 SER A 788
REMARK 465 ASP A 789
REMARK 465 TYR A 790
REMARK 465 ALA A 791
REMARK 465 ASN A 792
REMARK 465 PHE A 793
REMARK 465 LYS A 794
REMARK 465 ARG B 674
REMARK 465 ASP B 789
REMARK 465 TYR B 790
REMARK 465 ALA B 791
REMARK 465 ASN B 792
REMARK 465 PHE B 793
REMARK 465 LYS B 794
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU A 633 N CYS A 635 1.74
REMARK 500 O ARG A 679 N ILE A 681 2.08
REMARK 500 O GLN A 632 N LYS A 634 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 604 N - CA - C ANGL. DEV. = -19.8 DEGREES
REMARK 500 GLU A 629 N - CA - C ANGL. DEV. = -28.3 DEGREES
REMARK 500 ARG A 630 N - CA - C ANGL. DEV. = 21.1 DEGREES
REMARK 500 GLY A 631 N - CA - C ANGL. DEV. = -33.0 DEGREES
REMARK 500 ALA A 636 N - CA - C ANGL. DEV. = 23.0 DEGREES
REMARK 500 GLN A 637 N - CA - C ANGL. DEV. = -23.8 DEGREES
REMARK 500 ARG A 674 N - CA - C ANGL. DEV. = -24.5 DEGREES
REMARK 500 GLU A 675 N - CA - C ANGL. DEV. = 20.1 DEGREES
REMARK 500 SER A 715 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 GLN A 772 N - CA - C ANGL. DEV. = -22.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 573 -71.28 18.52
REMARK 500 GLU A 576 114.38 74.24
REMARK 500 ASN A 582 87.77 -65.54
REMARK 500 PRO A 601 -173.95 -56.02
REMARK 500 LEU A 603 1.89 80.90
REMARK 500 THR A 605 -4.26 -166.66
REMARK 500 GLU A 633 31.93 7.67
REMARK 500 LYS A 634 -22.43 5.29
REMARK 500 CYS A 635 -142.96 -178.44
REMARK 500 ALA A 636 -142.45 -45.01
REMARK 500 GLN A 637 48.20 96.38
REMARK 500 ASP A 642 84.19 82.33
REMARK 500 LEU A 644 75.19 110.40
REMARK 500 LEU A 654 179.26 -39.44
REMARK 500 LYS A 655 -31.36 104.31
REMARK 500 LYS A 656 38.58 -63.74
REMARK 500 CYS A 660 -165.26 -79.97
REMARK 500 GLU A 661 -78.88 -56.78
REMARK 500 ARG A 674 53.57 155.72
REMARK 500 GLU A 675 131.61 -19.56
REMARK 500 ASN A 676 109.23 -175.67
REMARK 500 ARG A 679 82.54 -4.67
REMARK 500 GLN A 680 76.49 -15.88
REMARK 500 PRO A 695 153.67 -18.85
REMARK 500 SER A 696 -95.09 -71.85
REMARK 500 GLN A 713 -82.22 -65.08
REMARK 500 SER A 715 -21.40 171.27
REMARK 500 CYS A 724 -89.90 -118.72
REMARK 500 SER A 725 -34.84 -135.86
REMARK 500 ALA A 728 -59.96 -137.00
REMARK 500 ALA A 746 -0.47 -146.97
REMARK 500 GLU A 747 -7.90 -159.18
REMARK 500 ASP A 751 57.47 -90.29
REMARK 500 VAL A 752 17.89 -59.94
REMARK 500 PHE A 753 -54.93 -134.96
REMARK 500 VAL A 767 75.63 79.16
REMARK 500 GLN A 768 -93.45 -77.90
REMARK 500 THR A 769 108.37 -39.71
REMARK 500 GLU A 771 -53.80 -147.08
REMARK 500 TYR A 773 -68.36 136.99
REMARK 500 ASP A 785 41.77 -85.17
REMARK 500 ALA B 549 -36.65 115.96
REMARK 500 ASN B 565 42.31 -158.07
REMARK 500 GLU B 576 -113.58 162.60
REMARK 500 ASN B 577 111.72 -170.55
REMARK 500 THR B 578 44.66 -175.19
REMARK 500 ASN B 582 84.93 -64.94
REMARK 500 TRP B 616 31.00 -93.85
REMARK 500 ARG B 630 25.43 43.24
REMARK 500 CYS B 635 147.04 162.99
REMARK 500
REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P13 RELATED DB: PDB
DBREF 1P15 A 542 794 UNP P18052 PTPRA_MOUSE 577 829
DBREF 1P15 B 542 794 UNP P18052 PTPRA_MOUSE 577 829
SEQRES 1 A 253 MET ARG THR GLY ASN LEU PRO ALA ASN MET LYS LYS ASN
SEQRES 2 A 253 ARG VAL LEU GLN ILE ILE PRO TYR GLU PHE ASN ARG VAL
SEQRES 3 A 253 ILE ILE PRO VAL LYS ARG GLY GLU GLU ASN THR ASP TYR
SEQRES 4 A 253 VAL ASN ALA SER PHE ILE ASP GLY TYR ARG GLN LYS ASP
SEQRES 5 A 253 SER TYR ILE ALA SER GLN GLY PRO LEU LEU HIS THR ILE
SEQRES 6 A 253 GLU ASP PHE TRP ARG MET ILE TRP GLU TRP LYS SER CYS
SEQRES 7 A 253 SER ILE VAL MET LEU THR GLU LEU GLU GLU ARG GLY GLN
SEQRES 8 A 253 GLU LYS CYS ALA GLN TYR TRP PRO SER ASP GLY LEU VAL
SEQRES 9 A 253 SER TYR GLY ASP ILE THR VAL GLU LEU LYS LYS GLU GLU
SEQRES 10 A 253 GLU CYS GLU SER TYR THR VAL ARG ASP LEU LEU VAL THR
SEQRES 11 A 253 ASN THR ARG GLU ASN LYS SER ARG GLN ILE ARG GLN PHE
SEQRES 12 A 253 HIS PHE HIS GLY TRP PRO GLU VAL GLY ILE PRO SER ASP
SEQRES 13 A 253 GLY LYS GLY MET ILE ASN ILE ILE ALA ALA VAL GLN LYS
SEQRES 14 A 253 GLN GLN GLN GLN SER GLY ASN HIS PRO ILE THR VAL HIS
SEQRES 15 A 253 CYS SER ALA GLY ALA GLY ARG THR GLY THR PHE CYS ALA
SEQRES 16 A 253 LEU SER THR VAL LEU GLU ARG VAL LYS ALA GLU GLY ILE
SEQRES 17 A 253 LEU ASP VAL PHE GLN THR VAL LYS SER LEU ARG LEU GLN
SEQRES 18 A 253 ARG PRO HIS MET VAL GLN THR LEU GLU GLN TYR GLU PHE
SEQRES 19 A 253 CYS TYR LYS VAL VAL GLN GLU TYR ILE ASP ALA PHE SER
SEQRES 20 A 253 ASP TYR ALA ASN PHE LYS
SEQRES 1 B 253 MET ARG THR GLY ASN LEU PRO ALA ASN MET LYS LYS ASN
SEQRES 2 B 253 ARG VAL LEU GLN ILE ILE PRO TYR GLU PHE ASN ARG VAL
SEQRES 3 B 253 ILE ILE PRO VAL LYS ARG GLY GLU GLU ASN THR ASP TYR
SEQRES 4 B 253 VAL ASN ALA SER PHE ILE ASP GLY TYR ARG GLN LYS ASP
SEQRES 5 B 253 SER TYR ILE ALA SER GLN GLY PRO LEU LEU HIS THR ILE
SEQRES 6 B 253 GLU ASP PHE TRP ARG MET ILE TRP GLU TRP LYS SER CYS
SEQRES 7 B 253 SER ILE VAL MET LEU THR GLU LEU GLU GLU ARG GLY GLN
SEQRES 8 B 253 GLU LYS CYS ALA GLN TYR TRP PRO SER ASP GLY LEU VAL
SEQRES 9 B 253 SER TYR GLY ASP ILE THR VAL GLU LEU LYS LYS GLU GLU
SEQRES 10 B 253 GLU CYS GLU SER TYR THR VAL ARG ASP LEU LEU VAL THR
SEQRES 11 B 253 ASN THR ARG GLU ASN LYS SER ARG GLN ILE ARG GLN PHE
SEQRES 12 B 253 HIS PHE HIS GLY TRP PRO GLU VAL GLY ILE PRO SER ASP
SEQRES 13 B 253 GLY LYS GLY MET ILE ASN ILE ILE ALA ALA VAL GLN LYS
SEQRES 14 B 253 GLN GLN GLN GLN SER GLY ASN HIS PRO ILE THR VAL HIS
SEQRES 15 B 253 CYS SER ALA GLY ALA GLY ARG THR GLY THR PHE CYS ALA
SEQRES 16 B 253 LEU SER THR VAL LEU GLU ARG VAL LYS ALA GLU GLY ILE
SEQRES 17 B 253 LEU ASP VAL PHE GLN THR VAL LYS SER LEU ARG LEU GLN
SEQRES 18 B 253 ARG PRO HIS MET VAL GLN THR LEU GLU GLN TYR GLU PHE
SEQRES 19 B 253 CYS TYR LYS VAL VAL GLN GLU TYR ILE ASP ALA PHE SER
SEQRES 20 B 253 ASP TYR ALA ASN PHE LYS
FORMUL 3 HOH *115(H2 O)
HELIX 1 1 ARG A 543 LEU A 547 5 5
HELIX 2 2 THR A 605 TRP A 616 1 12
HELIX 3 3 GLY A 700 GLN A 712 1 13
HELIX 4 4 ALA A 728 GLY A 748 1 21
HELIX 5 5 PHE A 753 LEU A 761 1 9
HELIX 6 6 TYR A 773 TYR A 783 1 11
HELIX 7 7 ASN B 550 ASN B 554 5 5
HELIX 8 8 TYR B 562 ARG B 566 5 5
HELIX 9 9 LEU B 602 HIS B 604 5 3
HELIX 10 10 THR B 605 TRP B 616 1 12
HELIX 11 11 GLY B 698 GLN B 712 1 15
HELIX 12 12 ALA B 728 GLU B 747 1 20
HELIX 13 13 ASP B 751 LEU B 761 1 11
HELIX 14 14 THR B 769 ASP B 785 1 17
SHEET 1 A 7 ALA A 583 ILE A 586 0
SHEET 2 A 7 TYR A 595 SER A 598 -1 O TYR A 595 N ILE A 586
SHEET 3 A 7 ILE A 720 HIS A 723 1 O VAL A 722 N SER A 598
SHEET 4 A 7 SER A 620 MET A 623 1 N VAL A 622 O THR A 721
SHEET 5 A 7 LYS A 677 PHE A 686 1 O PHE A 684 N ILE A 621
SHEET 6 A 7 TYR A 663 THR A 671 -1 N ARG A 666 O GLN A 683
SHEET 7 A 7 GLU A 658 GLU A 659 -1 N GLU A 658 O VAL A 665
SHEET 1 B 2 SER A 646 TYR A 647 0
SHEET 2 B 2 ILE A 650 THR A 651 -1 O ILE A 650 N TYR A 647
SHEET 1 C 8 ALA B 583 GLY B 588 0
SHEET 2 C 8 GLN B 591 SER B 598 -1 O GLN B 591 N GLY B 588
SHEET 3 C 8 ILE B 720 HIS B 723 1 O VAL B 722 N SER B 598
SHEET 4 C 8 SER B 620 MET B 623 1 N VAL B 622 O THR B 721
SHEET 5 C 8 SER B 678 PHE B 686 1 O PHE B 684 N ILE B 621
SHEET 6 C 8 TYR B 663 THR B 671 -1 N THR B 664 O HIS B 685
SHEET 7 C 8 ILE B 650 GLU B 659 -1 N THR B 651 O THR B 671
SHEET 8 C 8 LEU B 644 TYR B 647 -1 N TYR B 647 O ILE B 650
SHEET 1 D 2 GLU B 628 GLU B 629 0
SHEET 2 D 2 GLN B 632 GLU B 633 -1 O GLN B 632 N GLU B 629
CRYST1 59.101 59.101 152.657 90.00 90.00 120.00 P 31 6
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 0.016920 0.009769 0.000000 0.00000
SCALE2 0.000000 0.019538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006551 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
