HEADER HYDROLASE 07-JUL-11 3SR9
TITLE CRYSTAL STRUCTURE OF MOUSE PTPSIGMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE S;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1326-1901;
COMPND 5 SYNONYM: R-PTP-S, PTPNU-3, RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE
COMPND 6 SIGMA, R-PTP-SIGMA;
COMPND 7 EC: 3.1.3.48;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTPRS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS TYROSINE PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WANG,L.HOU,J.LI,J.DING
REVDAT 2 01-NOV-23 3SR9 1 SEQADV
REVDAT 1 30-MAY-12 3SR9 0
JRNL AUTH L.HOU,J.WANG,Y.ZHOU,J.LI,Y.ZANG,J.LI
JRNL TITL STRUCTURAL INSIGHTS INTO THE HOMOLOGY AND DIFFERENCES
JRNL TITL 2 BETWEEN MOUSE PROTEIN TYROSINE PHOSPHATASE-SIGMA AND HUMAN
JRNL TITL 3 PROTEIN TYROSINE PHOSPHATASE-SIGMA
JRNL REF ACTA BIOCHIM.BIOPHYS.SIN. V. 43 977 2011
JRNL REFN ISSN 1672-9145
JRNL PMID 22027896
JRNL DOI 10.1093/ABBS/GMR095
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 3 NUMBER OF REFLECTIONS : 21203
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 + TEST SET) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1117
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1576
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4597
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 89
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.08000
REMARK 3 B12 (A**2) : 0.03000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.323
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4711 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6384 ; 0.973 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 566 ; 5.129 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;36.235 ;23.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 795 ;16.224 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;15.893 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 678 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3657 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2831 ; 1.061 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4591 ; 1.951 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1880 ; 1.283 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1793 ; 2.357 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3SR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066553.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22320
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2FH7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% POLYETHYLENE GLYCOL 3350, 0.08M
REMARK 280 MALIC ACID, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 277K
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 41.40033
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 82.80067
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 62.10050
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 103.50083
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 20.70017
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1319
REMARK 465 HIS A 1320
REMARK 465 HIS A 1321
REMARK 465 HIS A 1322
REMARK 465 HIS A 1323
REMARK 465 HIS A 1324
REMARK 465 HIS A 1325
REMARK 465 SER A 1648
REMARK 465 SER A 1649
REMARK 465 LYS A 1650
REMARK 465 ALA A 1651
REMARK 465 HIS A 1652
REMARK 465 THR A 1653
REMARK 465 SER A 1654
REMARK 465 ARG A 1655
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 A1335 -4.99 76.74
REMARK 500 TRP A1367 43.76 -147.29
REMARK 500 SER A1456 4.68 59.17
REMARK 500 ASN A1498 105.73 -50.97
REMARK 500 SER A1500 122.58 -21.32
REMARK 500 CYS A1548 -86.87 -119.80
REMARK 500 SER A1549 -61.66 -120.18
REMARK 500 VAL A1591 81.49 64.67
REMARK 500 PRO A1662 -6.84 -55.41
REMARK 500 GLN A1762 -121.16 49.34
REMARK 500 CYS A1839 -73.53 -128.62
REMARK 500 SER A1840 -66.75 -132.73
REMARK 500 VAL A1843 -47.59 -133.72
REMARK 500 VAL A1882 81.35 67.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3SR9 A 1326 1901 UNP B0V2N1 PTPRS_MOUSE 1326 1901
SEQADV 3SR9 MET A 1319 UNP B0V2N1 EXPRESSION TAG
SEQADV 3SR9 HIS A 1320 UNP B0V2N1 EXPRESSION TAG
SEQADV 3SR9 HIS A 1321 UNP B0V2N1 EXPRESSION TAG
SEQADV 3SR9 HIS A 1322 UNP B0V2N1 EXPRESSION TAG
SEQADV 3SR9 HIS A 1323 UNP B0V2N1 EXPRESSION TAG
SEQADV 3SR9 HIS A 1324 UNP B0V2N1 EXPRESSION TAG
SEQADV 3SR9 HIS A 1325 UNP B0V2N1 EXPRESSION TAG
SEQRES 1 A 583 MET HIS HIS HIS HIS HIS HIS MET LEU SER HIS PRO PRO
SEQRES 2 A 583 ILE PRO ILE THR ASP MET ALA GLU HIS MET GLU ARG LEU
SEQRES 3 A 583 LYS ALA ASN ASP SER LEU LYS LEU SER GLN GLU TYR GLU
SEQRES 4 A 583 SER ILE ASP PRO GLY GLN GLN PHE THR TRP GLU HIS SER
SEQRES 5 A 583 ASN LEU GLU ALA ASN LYS PRO LYS ASN ARG TYR ALA ASN
SEQRES 6 A 583 VAL ILE ALA TYR ASP HIS SER ARG VAL ILE LEU GLN PRO
SEQRES 7 A 583 LEU GLU GLY ILE MET GLY SER ASP TYR ILE ASN ALA ASN
SEQRES 8 A 583 TYR VAL ASP GLY TYR ARG ARG GLN ASN ALA TYR ILE ALA
SEQRES 9 A 583 THR GLN GLY PRO LEU PRO GLU THR PHE GLY ASP PHE TRP
SEQRES 10 A 583 ARG MET VAL TRP GLU GLN ARG SER ALA THR VAL VAL MET
SEQRES 11 A 583 MET THR ARG LEU GLU GLU LYS SER ARG ILE LYS CYS ASP
SEQRES 12 A 583 GLN TYR TRP PRO ASN ARG GLY THR GLU THR TYR GLY PHE
SEQRES 13 A 583 ILE GLN VAL THR LEU LEU ASP THR MET GLU LEU ALA THR
SEQRES 14 A 583 PHE CYS VAL ARG THR PHE SER LEU HIS LYS ASN GLY SER
SEQRES 15 A 583 SER GLU LYS ARG GLU VAL ARG HIS PHE GLN PHE THR ALA
SEQRES 16 A 583 TRP PRO ASP HIS GLY VAL PRO GLU TYR PRO THR PRO PHE
SEQRES 17 A 583 LEU ALA PHE LEU ARG ARG VAL LYS THR CYS ASN PRO PRO
SEQRES 18 A 583 ASP ALA GLY PRO ILE VAL VAL HIS CYS SER ALA GLY VAL
SEQRES 19 A 583 GLY ARG THR GLY CYS PHE ILE VAL ILE ASP ALA MET LEU
SEQRES 20 A 583 GLU ARG ILE LYS THR GLU LYS THR VAL ASP VAL TYR GLY
SEQRES 21 A 583 HIS VAL THR LEU MET ARG SER GLN ARG ASN TYR MET VAL
SEQRES 22 A 583 GLN THR GLU ASP GLN TYR GLY PHE ILE HIS GLU ALA LEU
SEQRES 23 A 583 LEU GLU ALA VAL GLY CYS GLY ASN THR GLU VAL PRO ALA
SEQRES 24 A 583 ARG SER LEU TYR THR TYR ILE GLN LYS LEU ALA GLN VAL
SEQRES 25 A 583 GLU PRO GLY GLU HIS VAL THR GLY MET GLU LEU GLU PHE
SEQRES 26 A 583 LYS ARG LEU ALA SER SER LYS ALA HIS THR SER ARG PHE
SEQRES 27 A 583 ILE THR ALA SER LEU PRO CYS ASN LYS PHE LYS ASN ARG
SEQRES 28 A 583 LEU VAL ASN ILE LEU PRO TYR GLU SER SER ARG VAL CYS
SEQRES 29 A 583 LEU GLN PRO ILE ARG GLY VAL GLU GLY SER ASP TYR ILE
SEQRES 30 A 583 ASN ALA SER PHE ILE ASP GLY TYR ARG GLN GLN LYS ALA
SEQRES 31 A 583 TYR ILE ALA THR GLN GLY PRO LEU ALA GLU THR THR GLU
SEQRES 32 A 583 ASP PHE TRP ARG ALA LEU TRP GLU ASN ASN SER THR ILE
SEQRES 33 A 583 VAL VAL MET LEU THR LYS LEU ARG GLU MET GLY ARG GLU
SEQRES 34 A 583 LYS CYS HIS GLN TYR TRP PRO ALA GLU ARG SER ALA ARG
SEQRES 35 A 583 TYR GLN TYR PHE VAL VAL ASP PRO MET ALA GLU TYR ASN
SEQRES 36 A 583 MET PRO GLN TYR ILE LEU ARG GLU PHE LYS VAL THR ASP
SEQRES 37 A 583 ALA ARG ASP GLY GLN SER ARG THR VAL ARG GLN PHE GLN
SEQRES 38 A 583 PHE THR ASP TRP PRO GLU GLN GLY ALA PRO LYS SER GLY
SEQRES 39 A 583 GLU GLY PHE ILE ASP PHE ILE GLY GLN VAL HIS LYS THR
SEQRES 40 A 583 LYS GLU GLN PHE GLY GLN ASP GLY PRO ILE SER VAL HIS
SEQRES 41 A 583 CYS SER ALA GLY VAL GLY ARG THR GLY VAL PHE ILE THR
SEQRES 42 A 583 LEU SER ILE VAL LEU GLU ARG MET ARG TYR GLU GLY VAL
SEQRES 43 A 583 VAL ASP ILE PHE GLN THR VAL LYS VAL LEU ARG THR GLN
SEQRES 44 A 583 ARG PRO ALA MET VAL GLN THR GLU ASP GLU TYR GLN PHE
SEQRES 45 A 583 CYS PHE GLN ALA ALA LEU GLU TYR LEU GLY SER
FORMUL 2 HOH *89(H2 O)
HELIX 1 1 ASP A 1336 ILE A 1359 1 24
HELIX 2 2 TRP A 1367 LEU A 1372 1 6
HELIX 3 3 ASN A 1375 ASN A 1379 5 5
HELIX 4 4 TYR A 1387 HIS A 1389 5 3
HELIX 5 5 LEU A 1427 GLU A 1429 5 3
HELIX 6 6 THR A 1430 GLN A 1441 1 12
HELIX 7 7 PRO A 1523 CYS A 1536 1 14
HELIX 8 8 GLY A 1553 LYS A 1569 1 17
HELIX 9 9 ASP A 1575 SER A 1585 1 11
HELIX 10 10 THR A 1593 CYS A 1610 1 18
HELIX 11 11 SER A 1619 ALA A 1628 1 10
HELIX 12 12 THR A 1637 ARG A 1645 1 9
HELIX 13 13 THR A 1719 ASN A 1730 1 12
HELIX 14 14 GLY A 1812 PHE A 1829 1 18
HELIX 15 15 VAL A 1843 GLU A 1862 1 20
HELIX 16 16 ASP A 1866 THR A 1876 1 11
HELIX 17 17 THR A 1884 SER A 1901 1 18
SHEET 1 A 2 ILE A1332 PRO A1333 0
SHEET 2 A 2 THR A1573 VAL A1574 -1 O VAL A1574 N ILE A1332
SHEET 1 B 9 ARG A1391 ILE A1393 0
SHEET 2 B 9 TYR A1405 GLY A1413 -1 O ALA A1408 N VAL A1392
SHEET 3 B 9 ARG A1416 THR A1423 -1 O ARG A1416 N GLY A1413
SHEET 4 B 9 ILE A1544 HIS A1547 1 O VAL A1546 N ILE A1421
SHEET 5 B 9 THR A1445 MET A1448 1 N VAL A1447 O VAL A1545
SHEET 6 B 9 LYS A1503 PHE A1511 1 O PHE A1509 N VAL A1446
SHEET 7 B 9 PHE A1488 LYS A1497 -1 N LEU A1495 O ARG A1504
SHEET 8 B 9 ILE A1475 GLU A1484 -1 N GLN A1476 O HIS A1496
SHEET 9 B 9 THR A1469 TYR A1472 -1 N GLU A1470 O VAL A1477
SHEET 1 C 2 GLU A1453 GLU A1454 0
SHEET 2 C 2 ARG A1457 ILE A1458 -1 O ARG A1457 N GLU A1454
SHEET 1 D 2 VAL A1615 PRO A1616 0
SHEET 2 D 2 VAL A1864 VAL A1865 -1 O VAL A1865 N VAL A1615
SHEET 1 E 8 ALA A1697 ILE A1700 0
SHEET 2 E 8 TYR A1709 THR A1712 -1 O ALA A1711 N SER A1698
SHEET 3 E 8 ILE A1835 HIS A1838 1 O VAL A1837 N ILE A1710
SHEET 4 E 8 ILE A1734 MET A1737 1 N VAL A1736 O HIS A1838
SHEET 5 E 8 SER A1792 PHE A1800 1 O PHE A1798 N MET A1737
SHEET 6 E 8 TYR A1777 ASP A1786 -1 N ARG A1780 O GLN A1797
SHEET 7 E 8 PHE A1764 ASN A1773 -1 N TYR A1772 O LEU A1779
SHEET 8 E 8 ALA A1759 TYR A1761 -1 N TYR A1761 O PHE A1764
CRYST1 94.653 94.653 124.201 90.00 90.00 120.00 P 61 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 0.010565 0.006100 0.000000 0.00000
SCALE2 0.000000 0.012199 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008051 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
