HEADER TRANSFERASE 17-DEC-10 3Q1I
TITLE POLO-LIKE KINASE I POLO-BOX DOMAIN IN COMPLEX WITH FMPPPMSPSM
TITLE 2 PHOSPHOPEPTIDE FROM TCERG1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: POLO-BOX DOMAIN, RESIDUES 371-594;
COMPND 5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE
COMPND 6 13, STPK13;
COMPND 7 EC: 2.7.11.21;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PEPTIDE FROM TRANSCRIPTION ELONGATION REGULATOR 1;
COMPND 11 CHAIN: E;
COMPND 12 SYNONYM: PEPTIDE FROM TCERG1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLK1, PLK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: SYNTHETIC PHOSPHOPEPTIDE
KEYWDS KINASE, PEPTIDE BINDING PROTEIN, PLK1, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.SLEDZ,M.HYVONEN,C.ABELL
REVDAT 2 01-NOV-23 3Q1I 1 REMARK SEQADV LINK
REVDAT 1 27-APR-11 3Q1I 0
JRNL AUTH P.SLEDZ,C.J.STUBBS,S.LANG,Y.Q.YANG,G.J.MCKENZIE,
JRNL AUTH 2 A.R.VENKITARAMAN,M.HYVONEN,C.ABELL
JRNL TITL FROM CRYSTAL PACKING TO MOLECULAR RECOGNITION: PREDICTION
JRNL TITL 2 AND DISCOVERY OF A BINDING SITE ON THE SURFACE OF POLO-LIKE
JRNL TITL 3 KINASE 1
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 50 4003 2011
JRNL REFN ISSN 1433-7851
JRNL PMID 21472932
JRNL DOI 10.1002/ANIE.201008019
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 37019
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1939
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2697
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1779
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -0.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.075
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.994
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1887 ; 0.005 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2559 ; 0.968 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 238 ; 5.312 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;31.649 ;23.049
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 320 ;12.727 ;15.047
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;15.781 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 286 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1397 ; 0.003 ; 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): 1142 ; 0.369 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1849 ; 0.744 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 745 ; 1.122 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 701 ; 1.846 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 390 A 580
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0950 -0.3230 14.4200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0103 T22: 0.0064
REMARK 3 T33: 0.0121 T12: 0.0077
REMARK 3 T13: -0.0087 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.6416 L22: 0.3004
REMARK 3 L33: 1.5407 L12: 0.3048
REMARK 3 L13: -0.6414 L23: -0.3046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0044 S12: -0.0039 S13: -0.0232
REMARK 3 S21: -0.0011 S22: -0.0116 S23: -0.0066
REMARK 3 S31: 0.0630 S32: 0.0578 S33: 0.0071
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: NULL
REMARK 4
REMARK 4 3Q1I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000063076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38959
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 56.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
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) : 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: MOLREP
REMARK 200 STARTING MODEL: 1UMW CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.1M MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.75000
REMARK 290 SMTRY3 2 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 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: 1070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 GLY A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 PHE A 8
REMARK 465 ASP A 371
REMARK 465 GLU A 501
REMARK 465 GLY A 502
REMARK 465 ASP A 503
REMARK 465 GLU A 504
REMARK 465 LEU A 505
REMARK 465 ALA A 506
REMARK 465 ARG A 507
REMARK 465 ACE E 98
REMARK 465 PHE E 99
REMARK 465 MET E 100
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 LYS A 388 CG CD CE NZ
REMARK 470 ARG A 456 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 470 CG OD1 ND2
REMARK 470 MET A 473 CG SD CE
REMARK 470 LYS A 474 CD CE NZ
REMARK 470 LYS A 480 CE NZ
REMARK 470 ARG A 512 CZ NH1 NH2
REMARK 470 LYS A 556 CG CD CE NZ
REMARK 470 LYS A 574 CG CD CE NZ
REMARK 470 GLU A 575 CG CD OE1 OE2
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 392 -135.24 -119.08
REMARK 500 LYS A 420 -45.77 -134.45
REMARK 500 ASP A 449 -43.96 -137.94
REMARK 500 HIS A 468 150.77 -46.31
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 1PE A 595
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 596
DBREF 3Q1I A 371 594 UNP P53350 PLK1_HUMAN 371 594
DBREF 3Q1I E 99 107 UNP O14776 TCRG1_HUMAN 99 107
SEQADV 3Q1I GLY A 1 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I PRO A 2 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I LEU A 3 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I GLY A 4 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I SER A 5 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I PRO A 6 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I GLU A 7 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I PHE A 8 UNP P53350 EXPRESSION TAG
SEQADV 3Q1I ACE E 98 UNP O14776 ACETYLATION
SEQADV 3Q1I NH2 E 108 UNP O14776 AMIDATION
SEQRES 1 A 232 GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER
SEQRES 2 A 232 ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS
SEQRES 3 A 232 PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU
SEQRES 4 A 232 ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP
SEQRES 5 A 232 VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU
SEQRES 6 A 232 CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR
SEQRES 7 A 232 ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR
SEQRES 8 A 232 ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER
SEQRES 9 A 232 SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU
SEQRES 10 A 232 LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS
SEQRES 11 A 232 ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU
SEQRES 12 A 232 ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG
SEQRES 13 A 232 SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN
SEQRES 14 A 232 ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS
SEQRES 15 A 232 PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG
SEQRES 16 A 232 ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR
SEQRES 17 A 232 GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA
SEQRES 18 A 232 ARG THR MET VAL ASP LYS LEU LEU SER SER ARG
SEQRES 1 E 11 ACE PHE MET PRO PRO PRO MET SER SEP MET NH2
MODRES 3Q1I SEP E 106 SER PHOSPHOSERINE
HET SEP E 106 10
HET NH2 E 108 1
HET 1PE A 595 16
HET PEG A 596 7
HET PG0 A 597 8
HETNAM SEP PHOSPHOSERINE
HETNAM NH2 AMINO GROUP
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETSYN SEP PHOSPHONOSERINE
HETSYN 1PE PEG400
HETSYN PG0 PEG 6000
FORMUL 2 SEP C3 H8 N O6 P
FORMUL 2 NH2 H2 N
FORMUL 3 1PE C10 H22 O6
FORMUL 4 PEG C4 H10 O3
FORMUL 5 PG0 C5 H12 O3
FORMUL 6 HOH *192(H2 O)
HELIX 1 1 HIS A 373 SER A 387 1 15
HELIX 2 2 ARG A 396 GLU A 401 5 6
HELIX 3 3 ASP A 402 ILE A 406 5 5
HELIX 4 4 PRO A 469 SER A 471 5 3
HELIX 5 5 LEU A 472 LEU A 490 1 19
HELIX 6 6 LEU A 564 GLY A 571 1 8
HELIX 7 7 CYS A 573 SER A 593 1 21
SHEET 1 A 6 VAL A 411 ASP A 416 0
SHEET 2 A 6 GLY A 422 LEU A 427 -1 O GLY A 424 N VAL A 415
SHEET 3 A 6 VAL A 432 PHE A 436 -1 O LEU A 435 N LEU A 423
SHEET 4 A 6 ARG A 441 LEU A 444 -1 O LEU A 444 N VAL A 432
SHEET 5 A 6 SER A 450 ILE A 454 -1 O ILE A 454 N ARG A 441
SHEET 6 A 6 GLU A 460 THR A 464 -1 O LEU A 463 N LEU A 451
SHEET 1 B 6 LEU A 511 ARG A 516 0
SHEET 2 B 6 ALA A 520 LEU A 525 -1 O ILE A 522 N PHE A 515
SHEET 3 B 6 VAL A 530 PHE A 534 -1 O GLN A 531 N LEU A 523
SHEET 4 B 6 LYS A 540 CYS A 544 -1 O LEU A 543 N VAL A 530
SHEET 5 B 6 ALA A 549 ILE A 553 -1 O ILE A 553 N LYS A 540
SHEET 6 B 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
LINK C SER E 105 N SEP E 106 1555 1555 1.33
LINK C SEP E 106 N MET E 107 1555 1555 1.33
LINK C MET E 107 N NH2 E 108 1555 1555 1.33
SITE 1 AC1 4 HOH A 93 HOH A 101 VAL A 415 TYR A 485
SITE 1 AC2 3 HOH A 147 THR A 477 LYS A 480
CRYST1 35.500 51.500 57.600 90.00 101.00 90.00 P 1 21 1 2
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 0.028169 0.000000 0.005476 0.00000
SCALE2 0.000000 0.019417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017686 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
