HEADER TRANSCRIPTION/ANTAGONIST 24-JAN-12 4DFW
TITLE OXIME-BASED POST SOLID-PHASE PEPTIDE DIVERSIFICATION: IDENTIFICATION
TITLE 2 OF HIGH AFFINITY POLO-LIKE KINASE 1 (PLK1) POLO-BOX DOMAIN BINDING
TITLE 3 PEPTIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE
COMPND 5 13, STPK13;
COMPND 6 EC: 2.7.11.21;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PEPTIDE;
COMPND 10 CHAIN: D;
COMPND 11 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: PLK, PLK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES
KEYWDS PHOSPHO BINDING DOMAIN, TRANSCRIPTION-ANTAGONIST COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.LIU,J.-E.PARK,W.-J.QIAN,D.LIM,M.GR BER,T.BERG,M.B.YAFFE,K.S.LEE,
AUTHOR 2 JR.BURKE,T.R.
REVDAT 1 28-MAR-12 4DFW 0
JRNL AUTH F.LIU,J.-E.PARK,W.-J.QIAN,D.LIM,A SCHAROW,T.BERG,M.B.YAFFE,
JRNL AUTH 2 K.S.LEE,T.R.BURKE
JRNL TITL OXIME-BASED POST SOLID-PHASE PEPTIDE DIVERSIFICATION:
JRNL TITL 2 IDENTIFICATION OF HIGH AFFINITY POLO-LIKE KINASE 1 (PLK1)
JRNL TITL 3 POLO-BOX DOMAIN BINDING PEPTIDES
JRNL REF CHEM.BIOL. 2012
JRNL REFN ISSN 1074-5521
JRNL PMID 22292814
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 3 NUMBER OF REFLECTIONS : 27011
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1352
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 13.8630 - 3.3231 0.93 2649 140 0.1686 0.1776
REMARK 3 2 3.3231 - 2.6436 0.96 2722 144 0.1346 0.1851
REMARK 3 3 2.6436 - 2.3112 0.95 2695 142 0.1370 0.1656
REMARK 3 4 2.3112 - 2.1007 0.94 2661 139 0.1275 0.1851
REMARK 3 5 2.1007 - 1.9505 0.92 2604 138 0.1333 0.1696
REMARK 3 6 1.9505 - 1.8358 0.91 2580 137 0.1401 0.2063
REMARK 3 7 1.8358 - 1.7440 0.89 2513 132 0.1445 0.2127
REMARK 3 8 1.7440 - 1.6683 0.88 2508 132 0.1472 0.2100
REMARK 3 9 1.6683 - 1.6041 0.87 2483 131 0.1461 0.2311
REMARK 3 10 1.6041 - 1.5500 0.79 2244 117 0.1516 0.2133
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.51
REMARK 3 B_SOL : 53.80
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : -0.000
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.20300
REMARK 3 B22 (A**2) : 0.65950
REMARK 3 B33 (A**2) : -0.40310
REMARK 3 B12 (A**2) : 0.66680
REMARK 3 B13 (A**2) : 0.12050
REMARK 3 B23 (A**2) : 1.66390
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3819
REMARK 3 ANGLE : 1.334 6899
REMARK 3 CHIRALITY : 0.100 285
REMARK 3 PLANARITY : 0.011 560
REMARK 3 DIHEDRAL : 17.014 1015
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4DFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070277.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.6000
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 31% (W/V) PEG 3350, 0.1 M BIS-TRIS PH
REMARK 280 5.5 AND 240 MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 1610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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 367
REMARK 465 GLU A 368
REMARK 465 VAL A 369
REMARK 465 VAL A 370
REMARK 465 ASP A 371
REMARK 465 CYS A 372
REMARK 465 SER A 467
REMARK 465 HIS A 468
REMARK 465 ARG A 594
REMARK 465 SER A 595
REMARK 465 ALA A 596
REMARK 465 SER A 597
REMARK 465 ASN A 598
REMARK 465 ARG A 599
REMARK 465 LEU A 600
REMARK 465 LYS A 601
REMARK 465 ALA A 602
REMARK 465 SER A 603
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 HOH A 944 O HOH A 1029 2.12
REMARK 500 O HOH A 907 O HOH A 1012 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1019 O HOH A 1023 1464 2.15
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 ARG A 579 NE - CZ - NH1 ANGL. DEV. = 3.8 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 ASP A 402 86.42 -151.03
REMARK 500 LYS A 420 -47.94 -133.10
REMARK 500 ASP A 449 -35.79 -134.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 483 20.0 L L OUTSIDE RANGE
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 CL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF PEPTIDE
DBREF 4DFW A 367 603 UNP P53350 PLK1_HUMAN 367 603
DBREF 4DFW D 1 7 PDB 4DFW 4DFW 1 7
SEQRES 1 A 237 GLY GLU VAL VAL ASP CYS HIS LEU SER ASP MET LEU GLN
SEQRES 2 A 237 GLN LEU HIS SER VAL ASN ALA SER LYS PRO SER GLU ARG
SEQRES 3 A 237 GLY LEU VAL ARG GLN GLU GLU ALA GLU ASP PRO ALA CYS
SEQRES 4 A 237 ILE PRO ILE PHE TRP VAL SER LYS TRP VAL ASP TYR SER
SEQRES 5 A 237 ASP LYS TYR GLY LEU GLY TYR GLN LEU CYS ASP ASN SER
SEQRES 6 A 237 VAL GLY VAL LEU PHE ASN ASP SER THR ARG LEU ILE LEU
SEQRES 7 A 237 TYR ASN ASP GLY ASP SER LEU GLN TYR ILE GLU ARG ASP
SEQRES 8 A 237 GLY THR GLU SER TYR LEU THR VAL SER SER HIS PRO ASN
SEQRES 9 A 237 SER LEU MET LYS LYS ILE THR LEU LEU LYS TYR PHE ARG
SEQRES 10 A 237 ASN TYR MET SER GLU HIS LEU LEU LYS ALA GLY ALA ASN
SEQRES 11 A 237 ILE THR PRO ARG GLU GLY ASP GLU LEU ALA ARG LEU PRO
SEQRES 12 A 237 TYR LEU ARG THR TRP PHE ARG THR ARG SER ALA ILE ILE
SEQRES 13 A 237 LEU HIS LEU SER ASN GLY SER VAL GLN ILE ASN PHE PHE
SEQRES 14 A 237 GLN ASP HIS THR LYS LEU ILE LEU CYS PRO LEU MET ALA
SEQRES 15 A 237 ALA VAL THR TYR ILE ASP GLU LYS ARG ASP PHE ARG THR
SEQRES 16 A 237 TYR ARG LEU SER LEU LEU GLU GLU TYR GLY CYS CYS LYS
SEQRES 17 A 237 GLU LEU ALA SER ARG LEU ARG TYR ALA ARG THR MET VAL
SEQRES 18 A 237 ASP LYS LEU LEU SER SER ARG SER ALA SER ASN ARG LEU
SEQRES 19 A 237 LYS ALA SER
SEQRES 1 D 7 ACE 0LF LEU HIS SER TPO NH2
MODRES 4DFW 0LF D 2 PRO (4R)-4-(4-PHENYLBUTOXY)-L-PROLINE
MODRES 4DFW TPO D 6 THR PHOSPHOTHREONINE
HET ACE D 1 6
HET 0LF D 2 37
HET TPO D 6 17
HET NH2 D 7 3
HET CL A 701 1
HET CL A 702 1
HETNAM ACE ACETYL GROUP
HETNAM 0LF (4R)-4-(4-PHENYLBUTOXY)-L-PROLINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM NH2 AMINO GROUP
HETNAM CL CHLORIDE ION
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 2 ACE C2 H4 O
FORMUL 2 0LF C15 H21 N O3
FORMUL 2 TPO C4 H10 N O6 P
FORMUL 2 NH2 H2 N
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *256(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 GLY A 433 N TYR A 425
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 THR A 551 N ILE A 542
SHEET 6 B 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
LINK C ACE D 1 N 0LF D 2 1555 1555 1.36
LINK C 0LF D 2 N LEU D 3 1555 1555 1.35
LINK C SER D 5 N TPO D 6 1555 1555 1.33
LINK C TPO D 6 N NH2 D 7 1555 1555 1.37
SITE 1 AC1 4 LYS A 388 PRO A 389 SER A 390 HOH A 824
SITE 1 AC2 4 ARG A 560 THR A 561 HOH A 876 HOH A1014
SITE 1 AC3 25 LYS A 413 TRP A 414 VAL A 415 ASP A 416
SITE 2 AC3 25 TYR A 421 THR A 459 TYR A 481 TYR A 485
SITE 3 AC3 25 LEU A 490 LEU A 491 ARG A 516 HIS A 538
SITE 4 AC3 25 LYS A 540 HOH A 802 HOH A 836 HOH A 843
SITE 5 AC3 25 HOH A 956 HOH A1040 HOH D 101 HOH D 102
SITE 6 AC3 25 HOH D 103 HOH D 104 HOH D 105 HOH D 107
SITE 7 AC3 25 HOH D 109
CRYST1 35.665 34.844 47.097 76.44 86.95 69.14 P 1 1
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 0.028039 -0.010685 0.001000 0.00000
SCALE2 0.000000 0.030712 -0.007291 0.00000
SCALE3 0.000000 0.000000 0.021854 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
