HEADER SIGNALING PROTEIN 03-DEC-03 1RPY
TITLE CRYSTAL STRUCTURE OF THE DIMERIC SH2 DOMAIN OF APS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADAPTOR PROTEIN APS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ADAPTER PROTEIN, SH2 DOMAIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HU,J.LIU,R.GHIRLANDO,A.R.SALTIEL,S.R.HUBBARD
REVDAT 2 24-FEB-09 1RPY 1 VERSN
REVDAT 1 23-DEC-03 1RPY 0
JRNL AUTH J.HU,J.LIU,R.GHIRLANDO,A.R.SALTIEL,S.R.HUBBARD
JRNL TITL STRUCTURAL BASIS FOR RECRUITMENT OF THE ADAPTOR
JRNL TITL 2 PROTEIN APS TO THE ACTIVATED INSULIN RECEPTOR.
JRNL REF MOL.CELL V. 12 1379 2003
JRNL REFN ISSN 1097-2765
JRNL PMID 14690593
JRNL DOI 10.1016/S1097-2765(03)00487-8
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 10288
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) : 0.228
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 542
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1360
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 30
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) : -5.40000
REMARK 3 B22 (A**2) : -5.40000
REMARK 3 B33 (A**2) : 10.80000
REMARK 3 B12 (A**2) : -2.40000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.70
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.700 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.700 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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: NULL
REMARK 4
REMARK 4 1RPY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-03.
REMARK 100 THE RCSB ID CODE IS RCSB020936.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 90.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
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 : 10560
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.19900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE/TRIS, PH 7.5, PH
REMARK 280 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 22.44333
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 44.88667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.88667
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 22.44333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 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 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 -22.44333
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 397
REMARK 465 SER A 398
REMARK 465 HIS A 399
REMARK 465 MET A 400
REMARK 465 GLU A 401
REMARK 465 LEU A 402
REMARK 465 SER A 462
REMARK 465 LEU A 463
REMARK 465 ASN A 464
REMARK 465 GLY A 465
REMARK 465 HIS A 489
REMARK 465 PRO A 490
REMARK 465 ILE A 491
REMARK 465 PRO A 492
REMARK 465 LEU A 493
REMARK 465 GLU A 494
REMARK 465 SER A 495
REMARK 465 GLY A 496
REMARK 465 GLY A 497
REMARK 465 SER A 498
REMARK 465 ALA A 499
REMARK 465 ASP A 500
REMARK 465 ILE A 501
REMARK 465 THR A 502
REMARK 465 LEU A 503
REMARK 465 ARG A 504
REMARK 465 SER A 505
REMARK 465 TYR A 506
REMARK 465 VAL A 507
REMARK 465 ARG A 508
REMARK 465 ALA A 509
REMARK 465 GLN A 510
REMARK 465 GLY B 397
REMARK 465 SER B 398
REMARK 465 HIS B 399
REMARK 465 MET B 400
REMARK 465 GLU B 401
REMARK 465 LEU B 402
REMARK 465 GLU B 403
REMARK 465 LEU B 463
REMARK 465 ASN B 464
REMARK 465 GLY B 465
REMARK 465 HIS B 466
REMARK 465 GLU B 494
REMARK 465 SER B 495
REMARK 465 GLY B 496
REMARK 465 GLY B 497
REMARK 465 SER B 498
REMARK 465 ALA B 499
REMARK 465 ASP B 500
REMARK 465 ILE B 501
REMARK 465 THR B 502
REMARK 465 LEU B 503
REMARK 465 ARG B 504
REMARK 465 SER B 505
REMARK 465 TYR B 506
REMARK 465 VAL B 507
REMARK 465 ARG B 508
REMARK 465 ALA B 509
REMARK 465 GLN B 510
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 460 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 466 CG ND1 CD2 CE1 NE2
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 LEU A 404 -65.12 -19.99
REMARK 500 THR B 488 -31.77 -147.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 101
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 102
DBREF 1RPY A 401 510 UNP Q9Z200 APS_RAT 401 510
DBREF 1RPY B 401 510 UNP Q9Z200 APS_RAT 401 510
SEQADV 1RPY GLY A 397 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY SER A 398 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY HIS A 399 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY MET A 400 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY MSE A 482 UNP Q9Z200 MET 482 MODIFIED RESIDUE
SEQADV 1RPY GLY B 397 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY SER B 398 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY HIS B 399 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY MET B 400 UNP Q9Z200 CLONING ARTIFACT
SEQADV 1RPY MSE B 482 UNP Q9Z200 MET 482 MODIFIED RESIDUE
SEQRES 1 A 114 GLY SER HIS MET GLU LEU GLU LEU SER ASP TYR PRO TRP
SEQRES 2 A 114 PHE HIS GLY THR LEU SER ARG VAL LYS ALA ALA GLN LEU
SEQRES 3 A 114 VAL LEU ALA GLY GLY PRO ARG SER HIS GLY LEU PHE VAL
SEQRES 4 A 114 ILE ARG GLN SER GLU THR ARG PRO GLY GLU CYS VAL LEU
SEQRES 5 A 114 THR PHE ASN PHE GLN GLY LYS ALA LYS HIS LEU ARG LEU
SEQRES 6 A 114 SER LEU ASN GLY HIS GLY GLN CYS HIS VAL GLN HIS LEU
SEQRES 7 A 114 TRP PHE GLN SER VAL PHE ASP MSE LEU ARG HIS PHE HIS
SEQRES 8 A 114 THR HIS PRO ILE PRO LEU GLU SER GLY GLY SER ALA ASP
SEQRES 9 A 114 ILE THR LEU ARG SER TYR VAL ARG ALA GLN
SEQRES 1 B 114 GLY SER HIS MET GLU LEU GLU LEU SER ASP TYR PRO TRP
SEQRES 2 B 114 PHE HIS GLY THR LEU SER ARG VAL LYS ALA ALA GLN LEU
SEQRES 3 B 114 VAL LEU ALA GLY GLY PRO ARG SER HIS GLY LEU PHE VAL
SEQRES 4 B 114 ILE ARG GLN SER GLU THR ARG PRO GLY GLU CYS VAL LEU
SEQRES 5 B 114 THR PHE ASN PHE GLN GLY LYS ALA LYS HIS LEU ARG LEU
SEQRES 6 B 114 SER LEU ASN GLY HIS GLY GLN CYS HIS VAL GLN HIS LEU
SEQRES 7 B 114 TRP PHE GLN SER VAL PHE ASP MSE LEU ARG HIS PHE HIS
SEQRES 8 B 114 THR HIS PRO ILE PRO LEU GLU SER GLY GLY SER ALA ASP
SEQRES 9 B 114 ILE THR LEU ARG SER TYR VAL ARG ALA GLN
MODRES 1RPY MSE A 482 MET SELENOMETHIONINE
MODRES 1RPY MSE B 482 MET SELENOMETHIONINE
HET MSE A 482 8
HET MSE B 482 8
HET SO4 B 101 5
HET SO4 A 102 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 2(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *30(H2 O)
HELIX 1 1 GLU A 403 TYR A 407 5 5
HELIX 2 2 SER A 415 ALA A 425 1 11
HELIX 3 3 GLY A 426 HIS A 431 5 6
HELIX 4 4 GLN A 468 HIS A 487 1 20
HELIX 5 5 SER B 415 ALA B 425 1 11
HELIX 6 6 GLY B 426 HIS B 431 5 6
HELIX 7 7 GLN B 468 HIS B 487 1 20
SHEET 1 A 3 PHE A 434 GLN A 438 0
SHEET 2 A 3 CYS A 446 PHE A 452 -1 O VAL A 447 N ARG A 437
SHEET 3 A 3 LYS A 455 ARG A 460 -1 O LEU A 459 N LEU A 448
SHEET 1 B 3 PHE B 434 GLN B 438 0
SHEET 2 B 3 CYS B 446 PHE B 452 -1 O VAL B 447 N ARG B 437
SHEET 3 B 3 LYS B 455 LEU B 461 -1 O LEU B 459 N LEU B 448
LINK C ASP A 481 N MSE A 482 1555 1555 1.33
LINK C MSE A 482 N LEU A 483 1555 1555 1.33
LINK C ASP B 481 N MSE B 482 1555 1555 1.33
LINK C MSE B 482 N LEU B 483 1555 1555 1.33
SITE 1 AC1 5 ARG B 416 ARG B 437 SER B 439 GLU B 440
SITE 2 AC1 5 THR B 441
SITE 1 AC2 6 HOH A 22 ARG A 416 ARG A 437 SER A 439
SITE 2 AC2 6 GLU A 440 THR A 441
CRYST1 78.378 78.378 67.330 90.00 90.00 120.00 P 31 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012759 0.007366 0.000000 0.00000
SCALE2 0.000000 0.014732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014852 0.00000
(ATOM LINES ARE NOT SHOWN.)
END