HEADER TRANSCRIPTION ACTIVATOR 09-JAN-04 1UUR
TITLE STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS
TITLE 2 DNA-UNBOUND FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STATA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 235-707;
COMPND 5 SYNONYM: STAT PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_COMMON: SLIME MOLD;
SOURCE 4 ORGANISM_TAXID: 44689;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TKB1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PPROEXHTB
KEYWDS TRANSCRIPTION ACTIVATOR, DICTYOSTELIUM, STAT, SH2, SIGNAL
KEYWDS 2 TRANSDUCTION, TRANSDUCER, TRANSCRIPTION FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SOLER-LOPEZ,C.PETOSA,M.FUKUZAWA,R.RAVELLI,J.G.WILLIAMS,
AUTHOR 2 C.W.MULLER
REVDAT 3 16-JUN-09 1UUR 1 REMARK
REVDAT 2 24-FEB-09 1UUR 1 VERSN
REVDAT 1 26-MAR-04 1UUR 0
JRNL AUTH M.SOLER-LOPEZ,C.PETOSA,M.FUKUZAWA,R.RAVELLI,
JRNL AUTH 2 J.G.WILLIAMS,C.W.MULLER
JRNL TITL STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN
JRNL TITL 2 ITS DNA-UNBOUND FORM
JRNL REF MOL.CELL V. 13 791 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 15053873
JRNL DOI 10.1016/S1097-2765(04)00130-3
REMARK 2
REMARK 2 RESOLUTION. 2.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.7
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2420537
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 15971
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) : 0.21
REMARK 3 FREE R VALUE : 0.27
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 792
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.4
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2052
REMARK 3 BIN R VALUE (WORKING SET) : 0.380
REMARK 3 BIN FREE R VALUE : 0.397
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.7
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 123
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3621
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.8
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 30.28
REMARK 3 B22 (A**2) : -34.02
REMARK 3 B33 (A**2) : 3.74
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.65
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.49
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.65
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.5
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.5
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.13
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) : 5.61 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 8.31 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 9.32 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 12.37 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.319626
REMARK 3 BSOL : 41.7336
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 354-358 WERE MODELED AS
REMARK 3 POLYGLYCINE, RESIDUES 416-420 WERE OMITTED.
REMARK 4
REMARK 4 1UUR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-04.
REMARK 100 THE PDBE ID CODE IS EBI-14350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
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 : 15971
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.745
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 33.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.55000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.55000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.55000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 60.80000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.19 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLN A 235
REMARK 465 GLN A 236
REMARK 465 GLY A 237
REMARK 465 ASN A 238
REMARK 465 PRO A 239
REMARK 465 ASN A 240
REMARK 465 LEU A 241
REMARK 465 THR A 415
REMARK 465 ASN A 416
REMARK 465 LYS A 417
REMARK 465 ASN A 418
REMARK 465 ASN A 419
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 GLN A 354 CB CG CD OE1 NE2
REMARK 470 HIS A 355 CB CG ND1 CD2 CE1 NE2
REMARK 470 SER A 356 CB OG
REMARK 470 ALA A 357 CB
REMARK 470 PRO A 358 CB CG CD
REMARK 470 LYS A 359 CB CG CD CE NZ
REMARK 470 PRO A 414 CB CG CD
REMARK 470 PRO A 420 CB CG CD
REMARK 470 LEU A 678 CG CD1 CD2
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 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 SER A 243 33.43 71.14
REMARK 500 GLN A 245 -28.51 -35.61
REMARK 500 PRO A 246 -75.23 -75.55
REMARK 500 ILE A 247 -53.28 -28.93
REMARK 500 GLN A 269 -72.78 -66.35
REMARK 500 LEU A 272 5.05 -59.10
REMARK 500 THR A 279 143.28 179.33
REMARK 500 LEU A 280 149.30 176.50
REMARK 500 ASP A 281 -95.55 -94.84
REMARK 500 GLU A 282 -88.09 -46.55
REMARK 500 PRO A 320 -60.76 -24.69
REMARK 500 ILE A 350 -65.12 -105.01
REMARK 500 LYS A 359 -175.56 50.52
REMARK 500 VAL A 373 162.14 176.44
REMARK 500 ASN A 397 45.16 -102.53
REMARK 500 SER A 412 51.22 -97.43
REMARK 500 THR A 421 -158.79 -133.35
REMARK 500 MET A 426 52.99 72.71
REMARK 500 ASP A 463 173.08 -54.80
REMARK 500 GLU A 485 1.38 -60.34
REMARK 500 TRP A 488 -39.37 -37.25
REMARK 500 ARG A 530 75.03 -119.89
REMARK 500 TRP A 565 -62.35 -93.17
REMARK 500 HIS A 578 -8.62 73.86
REMARK 500 ARG A 594 -85.08 -37.39
REMARK 500 GLN A 602 107.48 -49.67
REMARK 500 ASN A 603 82.66 56.20
REMARK 500 ALA A 646 -44.75 -17.80
REMARK 500 SER A 659 -1.01 -58.74
REMARK 500 VAL A 662 -83.43 -104.11
REMARK 500 LYS A 679 93.67 -61.04
REMARK 500 LYS A 682 -38.13 -27.19
REMARK 500 ALA A 690 159.36 -49.20
REMARK 500 THR A 694 -94.34 -71.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 HIS A 413 10.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UUS RELATED DB: PDB
REMARK 900 STRUCTURE OF AN ACTIVATED DICTYOSTELIUM STAT IN ITS
REMARK 900 DNA-UNBOUND FORM
DBREF 1UUR A 235 707 UNP O00910 O00910 235 707
SEQRES 1 A 473 GLN GLN GLY ASN PRO ASN LEU SER SER PRO GLN PRO ILE
SEQRES 2 A 473 LEU ASP THR ILE TYR LYS LEU LEU SER GLU GLN GLU GLN
SEQRES 3 A 473 THR LEU VAL GLN MET ILE HIS GLU GLN SER LEU LEU LEU
SEQRES 4 A 473 ASN ARG LEU PRO PRO THR LEU ASP GLU ASN SER LEU ALA
SEQRES 5 A 473 PRO LEU LYS SER LEU SER GLN LYS GLN ILE THR LEU SER
SEQRES 6 A 473 GLY GLN MET ASN THR GLU MET SER ALA LEU ASP ALA THR
SEQRES 7 A 473 LYS LYS GLY MET ILE LEU GLU PRO THR ASP LEU ALA LYS
SEQRES 8 A 473 LEU PHE ALA LEU LYS GLN ASP LEU GLN ILE GLN PHE LYS
SEQRES 9 A 473 GLN LEU SER LEU LEU HIS ASN GLU ILE GLN SER ILE LEU
SEQRES 10 A 473 ASN PRO GLN HIS SER ALA PRO LYS PRO ASN VAL ALA LEU
SEQRES 11 A 473 VAL LEU LYS SER GLN PRO PHE PRO VAL VAL ILE SER LYS
SEQRES 12 A 473 GLY LYS GLN LEU GLY GLU ASN GLN LEU VAL VAL LEU VAL
SEQRES 13 A 473 LEU THR GLY ALA ARG SER ASN PHE HIS ILE ASN GLY PRO
SEQRES 14 A 473 VAL LYS ALA THR MET ILE CYS ASP SER HIS PRO THR ASN
SEQRES 15 A 473 LYS ASN ASN PRO THR THR PRO LEU GLU MET ASP SER GLN
SEQRES 16 A 473 PRO ILE TYR PRO ALA THR LEU THR ALA HIS PHE PRO LEU
SEQRES 17 A 473 LYS PHE LEU ALA GLY THR ARG LYS CYS SER VAL ASN LEU
SEQRES 18 A 473 LYS PHE GLY VAL ASN ILE ARG ASP LEU ASP ASN VAL THR
SEQRES 19 A 473 THR THR VAL GLU SER ASP ALA SER ASN PRO PHE VAL VAL
SEQRES 20 A 473 ILE THR ASN GLU CYS GLN TRP GLU GLY SER ALA GLY VAL
SEQRES 21 A 473 LEU LEU LYS LYS ASP ALA PHE ASP GLY GLN LEU GLU ILE
SEQRES 22 A 473 THR TRP ALA GLN PHE ILE ASN THR LEU GLN ARG HIS PHE
SEQRES 23 A 473 LEU ILE ALA THR LYS GLN ASP PRO VAL ARG PRO LYS ARG
SEQRES 24 A 473 PRO LEU SER SER TYR ASP LEU LYS TYR ILE GLN THR HIS
SEQRES 25 A 473 PHE PHE GLY ASN ARG SER ILE ILE HIS GLN GLN ASP PHE
SEQRES 26 A 473 ASP LYS PHE TRP VAL TRP PHE GLY LYS SER MET GLN THR
SEQRES 27 A 473 LEU ARG TYR GLN ARG HIS ILE SER THR LEU TRP GLN GLU
SEQRES 28 A 473 GLY ILE ILE TYR GLY TYR MET GLY ARG GLN GLU VAL ASN
SEQRES 29 A 473 ASP ALA LEU GLN ASN GLN ASP PRO GLY THR PHE ILE ILE
SEQRES 30 A 473 ARG PHE SER GLU ARG ASN PRO GLY GLN PHE GLY ILE ALA
SEQRES 31 A 473 TYR ILE GLY VAL GLU MET PRO ALA ARG ILE LYS HIS TYR
SEQRES 32 A 473 LEU VAL GLN PRO ASN ASP THR ALA ALA ALA LYS LYS THR
SEQRES 33 A 473 PHE PRO ASP PHE LEU SER GLU HIS SER GLN PHE VAL ASN
SEQRES 34 A 473 LEU LEU GLN TRP THR LYS ASP THR ASN GLY ALA PRO ARG
SEQRES 35 A 473 PHE LEU LYS LEU HIS LYS ASP THR ALA LEU GLY SER PHE
SEQRES 36 A 473 ALA PRO LYS ARG THR ALA PRO VAL PRO VAL GLY GLY PTR
SEQRES 37 A 473 GLU PRO LEU ASN SER
MODRES 1UUR PTR A 702 TYR PHOSPHOTYROSINE
HET PTR A 702 16
HETNAM PTR O-PHOSPHOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 HOH *40(H2 O1)
HELIX 1 1 PRO A 244 ARG A 275 1 32
HELIX 2 2 ASP A 281 MET A 316 1 36
HELIX 3 3 GLU A 319 ASN A 352 1 34
HELIX 4 4 GLN A 487 ASP A 502 1 16
HELIX 5 5 TRP A 509 THR A 524 1 16
HELIX 6 6 SER A 536 PHE A 547 1 12
HELIX 7 7 GLN A 556 GLN A 576 1 21
HELIX 8 8 HIS A 578 GLU A 585 1 8
HELIX 9 9 GLY A 593 ALA A 600 1 8
HELIX 10 10 GLN A 640 THR A 644 5 5
HELIX 11 11 THR A 650 SER A 656 1 7
HELIX 12 12 HIS A 681 LEU A 686 1 6
HELIX 13 13 GLY A 687 ALA A 690 5 4
SHEET 1 AA 3 ALA A 363 SER A 368 0
SHEET 2 AA 3 VAL A 387 LEU A 391 -1 O VAL A 387 N SER A 368
SHEET 3 AA 3 THR A 437 HIS A 439 -1 O ALA A 438 N VAL A 388
SHEET 1 AB 2 VAL A 374 SER A 376 0
SHEET 2 AB 2 VAL A 480 ILE A 482 1 O VAL A 480 N ILE A 375
SHEET 1 AC 4 SER A 428 GLN A 429 0
SHEET 2 AC 4 PHE A 398 ILE A 409 -1 O VAL A 404 N GLN A 429
SHEET 3 AC 4 ASN A 454 ASP A 463 -1 O ASN A 454 N ILE A 409
SHEET 4 AC 4 THR A 468 GLU A 472 -1 O THR A 469 N ILE A 461
SHEET 1 AD 2 LEU A 424 GLU A 425 0
SHEET 2 AD 2 LYS A 443 PHE A 444 -1 O LYS A 443 N GLU A 425
SHEET 1 AE 2 GLU A 506 THR A 508 0
SHEET 2 AE 2 ILE A 553 HIS A 555 -1 O ILE A 554 N ILE A 507
SHEET 1 AF 3 PHE A 609 PHE A 613 0
SHEET 2 AF 3 PHE A 621 ILE A 626 -1 O GLY A 622 N ARG A 612
SHEET 3 AF 3 ILE A 634 LEU A 638 -1 O LYS A 635 N TYR A 625
SHEET 1 AG 2 LEU A 665 LYS A 669 0
SHEET 2 AG 2 PRO A 675 LYS A 679 -1 O ARG A 676 N THR A 668
LINK C GLY A 701 N PTR A 702 1555 1555 1.33
LINK C PTR A 702 N GLU A 703 1555 1555 1.33
CISPEP 1 PHE A 371 PRO A 372 0 -1.57
CISPEP 2 MET A 630 PRO A 631 0 -0.41
CRYST1 121.600 144.000 67.100 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008224 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006944 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014903 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
