HEADER TRANSFERASE 08-JUL-07 2V5Q
TITLE CRYSTAL STRUCTURE OF WILD-TYPE PLK-1 KINASE DOMAIN IN
TITLE 2 COMPLEX WITH A SELECTIVE DARPIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 33-345;
COMPND 5 SYNONYM: PLK-1, SERINE/THREONINE-PROTEIN KINASE 13, STPK13,
COMPND 6 POLO-LIKE KINASE 1, HUMAN POLO-LIKE KINASE 1;
COMPND 7 EC: 2.7.11.21;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: CONSTRUCT 4;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: DESIGN ANKYRIN REPEAT PROTEIN;
COMPND 12 CHAIN: C, D;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: VARIANT 3H10
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 9 ORGANISM_TAXID: 32644;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 OTHER_DETAILS: DESIGNED PROTEIN
KEYWDS DESIGN ANKYRIN REPEAT PROTEIN, TRANSFERASE COMPLEX, PHOSPHORYLATION,
KEYWDS 2 NUCLEOTIDE-BINDING, SERINE/THREONINE-PROTEIN KINASE, KINASE,
KEYWDS 3 NUCLEUS, TRANSFERASE, ATP-BINDING, SERINE/THREONINE PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.BANDEIRAS,R.C.HILLIG,P.M.MATIAS,U.EBERSPAECHER,J.FANGHAENEL,
AUTHOR 2 M.THOMAZ,S.MIRANDA,K.CRUSIUS,V.PUETTER,P.AMSTUTZ,
AUTHOR 3 M.GULOTTI-GEORGIEVA,H.K.BINZ,C.HOLZ,A.A.P.SCHMITZ,C.LANG,P.DONNER,
AUTHOR 4 U.EGNER,M.A.CARRONDO,B.MUELLER-TIEMANN
REVDAT 3 13-JUL-11 2V5Q 1 VERSN
REVDAT 2 24-FEB-09 2V5Q 1 VERSN
REVDAT 1 01-APR-08 2V5Q 0
JRNL AUTH T.M.BANDEIRAS,R.C.HILLIG,P.M.MATIAS,U.EBERSPAECHER,
JRNL AUTH 2 J.FANGHAENEL,M.THOMAZ,S.MIRANDA,K.CRUSIUS,V.PUETTER,
JRNL AUTH 3 P.AMSTUTZ,M.GULOTTI-GEORGIEVA,H.K.BINZ,C.HOLZ,A.A.P.SCHMITZ,
JRNL AUTH 4 C.LANG,P.DONNER,U.EGNER,M.A.CARRONDO,B.MUELLER-TIEMANN
JRNL TITL STRUCTURE PF WILD-TYPE PLK-1 KINASE DOMAIN IN COMPLEX WITH
JRNL TITL 2 A SELECTIVE DARPIN
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 64 339 2008
JRNL REFN ISSN 0907-4449
JRNL PMID 18391401
JRNL DOI 10.1107/S0907444907068217
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 49051
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2601
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3580
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6523
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 406
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 45.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.07000
REMARK 3 B22 (A**2) : -1.87000
REMARK 3 B33 (A**2) : 0.80000
REMARK 3 B12 (A**2) : 0.00000
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): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6697 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9072 ; 1.265 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 833 ; 5.952 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 298 ;35.477 ;23.490
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1188 ;15.116 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;18.875 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1036 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5019 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3169 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4572 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 453 ; 0.144 ; 0.200
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): 40 ; 0.207 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.162 ; 0.200
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): 4262 ; 1.615 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6691 ; 2.800 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2691 ; 5.214 ; 9.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2377 ; 7.068 ;12.000
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 : 6
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 45 A 131
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7900 29.1250 33.1390
REMARK 3 T TENSOR
REMARK 3 T11: -0.1241 T22: 0.0725
REMARK 3 T33: 0.1671 T12: 0.0763
REMARK 3 T13: -0.0216 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 5.6756 L22: 3.0215
REMARK 3 L33: 5.9214 L12: -2.2970
REMARK 3 L13: -3.5416 L23: -1.1850
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: -0.3611 S13: -0.1878
REMARK 3 S21: 0.4811 S22: 0.2548 S23: 0.9448
REMARK 3 S31: -0.4088 S32: -0.5455 S33: -0.2130
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 132 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0670 32.4140 28.8270
REMARK 3 T TENSOR
REMARK 3 T11: -0.2267 T22: -0.1560
REMARK 3 T33: -0.2206 T12: 0.0852
REMARK 3 T13: 0.0149 T23: -0.0615
REMARK 3 L TENSOR
REMARK 3 L11: 1.5273 L22: 3.1399
REMARK 3 L33: 2.1696 L12: 0.0644
REMARK 3 L13: 0.2201 L23: 0.1300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0387 S12: -0.1407 S13: 0.1577
REMARK 3 S21: -0.0875 S22: 0.0795 S23: -0.2592
REMARK 3 S31: -0.2076 S32: 0.0773 S33: -0.0407
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 45 B 131
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6530 -1.5770 10.7100
REMARK 3 T TENSOR
REMARK 3 T11: -0.1103 T22: 0.1953
REMARK 3 T33: 0.1191 T12: 0.1118
REMARK 3 T13: 0.0308 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 8.8270 L22: 9.4992
REMARK 3 L33: 1.4472 L12: -5.3070
REMARK 3 L13: -2.4114 L23: 1.1887
REMARK 3 S TENSOR
REMARK 3 S11: -0.1891 S12: -0.3782 S13: -0.7550
REMARK 3 S21: -0.0832 S22: 0.1317 S23: -0.5104
REMARK 3 S31: 0.3984 S32: 0.5704 S33: 0.0574
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 132 B 323
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4680 12.1320 2.1410
REMARK 3 T TENSOR
REMARK 3 T11: -0.1183 T22: -0.2196
REMARK 3 T33: -0.1976 T12: 0.0385
REMARK 3 T13: 0.1146 T23: -0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 2.4006 L22: 2.7190
REMARK 3 L33: 2.6390 L12: 0.6165
REMARK 3 L13: -0.3271 L23: -0.5671
REMARK 3 S TENSOR
REMARK 3 S11: -0.1086 S12: 0.1410 S13: -0.1117
REMARK 3 S21: -0.4210 S22: 0.1813 S23: -0.1760
REMARK 3 S31: -0.1658 S32: 0.0279 S33: -0.0726
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 13 C 141
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9580 -13.7140 17.7940
REMARK 3 T TENSOR
REMARK 3 T11: -0.1803 T22: -0.2275
REMARK 3 T33: -0.0968 T12: 0.0160
REMARK 3 T13: -0.0160 T23: 0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 2.7395 L22: 3.1828
REMARK 3 L33: 4.1490 L12: 0.7043
REMARK 3 L13: -0.2374 L23: 0.8409
REMARK 3 S TENSOR
REMARK 3 S11: 0.0557 S12: 0.0616 S13: -0.3610
REMARK 3 S21: 0.0332 S22: -0.1063 S23: 0.0727
REMARK 3 S31: 0.1993 S32: -0.2828 S33: 0.0506
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 14 D 141
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4910 7.3110 50.3620
REMARK 3 T TENSOR
REMARK 3 T11: 0.1269 T22: -0.0324
REMARK 3 T33: -0.1541 T12: 0.0837
REMARK 3 T13: -0.1111 T23: 0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 1.4394 L22: 7.0708
REMARK 3 L33: 3.8178 L12: 0.2042
REMARK 3 L13: 0.2423 L23: 1.4234
REMARK 3 S TENSOR
REMARK 3 S11: 0.1239 S12: -0.4054 S13: -0.1728
REMARK 3 S21: 1.2007 S22: 0.1309 S23: -0.4975
REMARK 3 S31: 0.4983 S32: 0.0303 S33: -0.2547
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2V5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUL-07.
REMARK 100 THE PDBE ID CODE IS EBI-33146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.037
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51702
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 96.20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.70
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) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.40
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 1.3
REMARK 200 STARTING MODEL: PLK-1 - HOMOLOGY MODEL FROM PDB ENTRY 1OL5
REMARK 200 DARPIN 3H10 - PDB ENTRY 1MJ0 TRUNCATED AFTER RESIDUE 141
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.0, 8% PEG
REMARK 280 5000 MME, 0.01 M EDTA SODIUM SALT AT 303 K.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 31.16450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.41200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.61250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.41200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.16450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.61250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.7 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 31
REMARK 465 SER A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 34
REMARK 465 PRO A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 LYS A 38
REMARK 465 ARG A 324
REMARK 465 PHE A 325
REMARK 465 SER A 326
REMARK 465 ILE A 327
REMARK 465 ALA A 328
REMARK 465 PRO A 329
REMARK 465 SER A 330
REMARK 465 SER A 331
REMARK 465 LEU A 332
REMARK 465 ASP A 333
REMARK 465 PRO A 334
REMARK 465 SER A 335
REMARK 465 ASN A 336
REMARK 465 ARG A 337
REMARK 465 LYS A 338
REMARK 465 PRO A 339
REMARK 465 LEU A 340
REMARK 465 THR A 341
REMARK 465 VAL A 342
REMARK 465 LEU A 343
REMARK 465 ASN A 344
REMARK 465 LYS A 345
REMARK 465 GLY B 31
REMARK 465 SER B 32
REMARK 465 ALA B 33
REMARK 465 ALA B 34
REMARK 465 PRO B 35
REMARK 465 PRO B 36
REMARK 465 ALA B 37
REMARK 465 LYS B 38
REMARK 465 ARG B 324
REMARK 465 PHE B 325
REMARK 465 SER B 326
REMARK 465 ILE B 327
REMARK 465 ALA B 328
REMARK 465 PRO B 329
REMARK 465 SER B 330
REMARK 465 SER B 331
REMARK 465 LEU B 332
REMARK 465 ASP B 333
REMARK 465 PRO B 334
REMARK 465 SER B 335
REMARK 465 ASN B 336
REMARK 465 ARG B 337
REMARK 465 LYS B 338
REMARK 465 PRO B 339
REMARK 465 LEU B 340
REMARK 465 THR B 341
REMARK 465 VAL B 342
REMARK 465 LEU B 343
REMARK 465 ASN B 344
REMARK 465 LYS B 345
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 GLY C 3
REMARK 465 SER C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 GLY C 11
REMARK 465 GLN C 142
REMARK 465 ASP C 143
REMARK 465 LYS C 144
REMARK 465 PHE C 145
REMARK 465 GLY C 146
REMARK 465 LYS C 147
REMARK 465 THR C 148
REMARK 465 ALA C 149
REMARK 465 PHE C 150
REMARK 465 ASP C 151
REMARK 465 ILE C 152
REMARK 465 SER C 153
REMARK 465 ILE C 154
REMARK 465 ASP C 155
REMARK 465 ASN C 156
REMARK 465 GLY C 157
REMARK 465 ASN C 158
REMARK 465 GLU C 159
REMARK 465 ASP C 160
REMARK 465 LEU C 161
REMARK 465 ALA C 162
REMARK 465 LYS C 163
REMARK 465 SER C 164
REMARK 465 CYS C 165
REMARK 465 ARG C 166
REMARK 465 ASN C 167
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 GLY D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 GLY D 11
REMARK 465 SER D 12
REMARK 465 GLN D 142
REMARK 465 ASP D 143
REMARK 465 LYS D 144
REMARK 465 PHE D 145
REMARK 465 GLY D 146
REMARK 465 LYS D 147
REMARK 465 THR D 148
REMARK 465 ALA D 149
REMARK 465 PHE D 150
REMARK 465 ASP D 151
REMARK 465 ILE D 152
REMARK 465 SER D 153
REMARK 465 ILE D 154
REMARK 465 ASP D 155
REMARK 465 ASN D 156
REMARK 465 GLY D 157
REMARK 465 ASN D 158
REMARK 465 GLU D 159
REMARK 465 ASP D 160
REMARK 465 LEU D 161
REMARK 465 ALA D 162
REMARK 465 LYS D 163
REMARK 465 SER D 164
REMARK 465 CYS D 165
REMARK 465 ARG D 166
REMARK 465 ASN D 167
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 95 NE CZ NH1 NH2
REMARK 470 ARG A 207 NH2
REMARK 470 LYS A 248 CE NZ
REMARK 470 LYS A 264 CD CE NZ
REMARK 470 LYS A 272 NZ
REMARK 470 ARG B 50 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 52 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 74 CG OD1 OD2
REMARK 470 LYS B 97 CE NZ
REMARK 470 LYS B 248 CD CE NZ
REMARK 470 LYS D 16 NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG D 31 CZ ARG D 31 NH1 0.189
REMARK 500 ARG D 31 CZ ARG D 31 NH2 0.079
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 144 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 144 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG D 31 NE - CZ - NH2 ANGL. DEV. = -9.4 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 ARG A 50 -4.64 79.04
REMARK 500 LYS A 91 -143.60 60.39
REMARK 500 PRO A 92 -87.64 -53.58
REMARK 500 ASP A 122 -167.48 -113.22
REMARK 500 ARG A 136 -137.13 59.96
REMARK 500 LYS A 146 -122.64 59.72
REMARK 500 ASP A 176 40.95 -154.36
REMARK 500 ASP A 194 75.17 62.93
REMARK 500 SER A 229 -152.37 -146.53
REMARK 500 THR A 320 -40.93 -135.56
REMARK 500 PRO B 41 153.99 -49.10
REMARK 500 ARG B 50 55.10 33.00
REMARK 500 ARG B 57 130.41 -38.27
REMARK 500 ASP B 122 -157.90 -116.41
REMARK 500 ARG B 136 -134.50 60.59
REMARK 500 LYS B 146 -130.29 50.59
REMARK 500 ASP B 176 38.34 -149.14
REMARK 500 ASP B 194 77.54 60.96
REMARK 500 PHE B 195 32.21 -92.83
REMARK 500 LYS B 209 -67.01 -136.92
REMARK 500 SER B 229 -153.04 -156.28
REMARK 500 THR B 320 -36.94 -130.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 91 PRO A 92 -124.78
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 LYS A 91 18.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q4K RELATED DB: PDB
REMARK 900 THE POLO-BOX DOMAIN OF PLK1 IN COMPLEX
REMARK 900 WITH A PHOSPHO-PEPTIDE
REMARK 900 RELATED ID: 1Q4O RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE POLO BOX DOMAIN OF
REMARK 900 HUMAN PLK1
REMARK 900 RELATED ID: 1UMW RELATED DB: PDB
REMARK 900 STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN
REMARK 900 /PHOSPHOPEPTIDE COMPLEX
DBREF 2V5Q A 31 32 PDB 2V5Q 2V5Q 31 32
DBREF 2V5Q A 33 345 UNP P53350 PLK1_HUMAN 33 345
DBREF 2V5Q B 31 32 PDB 2V5Q 2V5Q 31 32
DBREF 2V5Q B 33 345 UNP P53350 PLK1_HUMAN 33 345
DBREF 2V5Q C 1 167 PDB 2V5Q 2V5Q 1 167
DBREF 2V5Q D 1 167 PDB 2V5Q 2V5Q 1 167
SEQRES 1 A 315 GLY SER ALA ALA PRO PRO ALA LYS GLU ILE PRO GLU VAL
SEQRES 2 A 315 LEU VAL ASP PRO ARG SER ARG ARG ARG TYR VAL ARG GLY
SEQRES 3 A 315 ARG PHE LEU GLY LYS GLY GLY PHE ALA LYS CYS PHE GLU
SEQRES 4 A 315 ILE SER ASP ALA ASP THR LYS GLU VAL PHE ALA GLY LYS
SEQRES 5 A 315 ILE VAL PRO LYS SER LEU LEU LEU LYS PRO HIS GLN ARG
SEQRES 6 A 315 GLU LYS MET SER MET GLU ILE SER ILE HIS ARG SER LEU
SEQRES 7 A 315 ALA HIS GLN HIS VAL VAL GLY PHE HIS GLY PHE PHE GLU
SEQRES 8 A 315 ASP ASN ASP PHE VAL PHE VAL VAL LEU GLU LEU CYS ARG
SEQRES 9 A 315 ARG ARG SER LEU LEU GLU LEU HIS LYS ARG ARG LYS ALA
SEQRES 10 A 315 LEU THR GLU PRO GLU ALA ARG TYR TYR LEU ARG GLN ILE
SEQRES 11 A 315 VAL LEU GLY CYS GLN TYR LEU HIS ARG ASN ARG VAL ILE
SEQRES 12 A 315 HIS ARG ASP LEU LYS LEU GLY ASN LEU PHE LEU ASN GLU
SEQRES 13 A 315 ASP LEU GLU VAL LYS ILE GLY ASP PHE GLY LEU ALA THR
SEQRES 14 A 315 LYS VAL GLU TYR ASP GLY GLU ARG LYS LYS THR LEU CYS
SEQRES 15 A 315 GLY THR PRO ASN TYR ILE ALA PRO GLU VAL LEU SER LYS
SEQRES 16 A 315 LYS GLY HIS SER PHE GLU VAL ASP VAL TRP SER ILE GLY
SEQRES 17 A 315 CYS ILE MET TYR THR LEU LEU VAL GLY LYS PRO PRO PHE
SEQRES 18 A 315 GLU THR SER CYS LEU LYS GLU THR TYR LEU ARG ILE LYS
SEQRES 19 A 315 LYS ASN GLU TYR SER ILE PRO LYS HIS ILE ASN PRO VAL
SEQRES 20 A 315 ALA ALA SER LEU ILE GLN LYS MET LEU GLN THR ASP PRO
SEQRES 21 A 315 THR ALA ARG PRO THR ILE ASN GLU LEU LEU ASN ASP GLU
SEQRES 22 A 315 PHE PHE THR SER GLY TYR ILE PRO ALA ARG LEU PRO ILE
SEQRES 23 A 315 THR CYS LEU THR ILE PRO PRO ARG PHE SER ILE ALA PRO
SEQRES 24 A 315 SER SER LEU ASP PRO SER ASN ARG LYS PRO LEU THR VAL
SEQRES 25 A 315 LEU ASN LYS
SEQRES 1 B 315 GLY SER ALA ALA PRO PRO ALA LYS GLU ILE PRO GLU VAL
SEQRES 2 B 315 LEU VAL ASP PRO ARG SER ARG ARG ARG TYR VAL ARG GLY
SEQRES 3 B 315 ARG PHE LEU GLY LYS GLY GLY PHE ALA LYS CYS PHE GLU
SEQRES 4 B 315 ILE SER ASP ALA ASP THR LYS GLU VAL PHE ALA GLY LYS
SEQRES 5 B 315 ILE VAL PRO LYS SER LEU LEU LEU LYS PRO HIS GLN ARG
SEQRES 6 B 315 GLU LYS MET SER MET GLU ILE SER ILE HIS ARG SER LEU
SEQRES 7 B 315 ALA HIS GLN HIS VAL VAL GLY PHE HIS GLY PHE PHE GLU
SEQRES 8 B 315 ASP ASN ASP PHE VAL PHE VAL VAL LEU GLU LEU CYS ARG
SEQRES 9 B 315 ARG ARG SER LEU LEU GLU LEU HIS LYS ARG ARG LYS ALA
SEQRES 10 B 315 LEU THR GLU PRO GLU ALA ARG TYR TYR LEU ARG GLN ILE
SEQRES 11 B 315 VAL LEU GLY CYS GLN TYR LEU HIS ARG ASN ARG VAL ILE
SEQRES 12 B 315 HIS ARG ASP LEU LYS LEU GLY ASN LEU PHE LEU ASN GLU
SEQRES 13 B 315 ASP LEU GLU VAL LYS ILE GLY ASP PHE GLY LEU ALA THR
SEQRES 14 B 315 LYS VAL GLU TYR ASP GLY GLU ARG LYS LYS THR LEU CYS
SEQRES 15 B 315 GLY THR PRO ASN TYR ILE ALA PRO GLU VAL LEU SER LYS
SEQRES 16 B 315 LYS GLY HIS SER PHE GLU VAL ASP VAL TRP SER ILE GLY
SEQRES 17 B 315 CYS ILE MET TYR THR LEU LEU VAL GLY LYS PRO PRO PHE
SEQRES 18 B 315 GLU THR SER CYS LEU LYS GLU THR TYR LEU ARG ILE LYS
SEQRES 19 B 315 LYS ASN GLU TYR SER ILE PRO LYS HIS ILE ASN PRO VAL
SEQRES 20 B 315 ALA ALA SER LEU ILE GLN LYS MET LEU GLN THR ASP PRO
SEQRES 21 B 315 THR ALA ARG PRO THR ILE ASN GLU LEU LEU ASN ASP GLU
SEQRES 22 B 315 PHE PHE THR SER GLY TYR ILE PRO ALA ARG LEU PRO ILE
SEQRES 23 B 315 THR CYS LEU THR ILE PRO PRO ARG PHE SER ILE ALA PRO
SEQRES 24 B 315 SER SER LEU ASP PRO SER ASN ARG LYS PRO LEU THR VAL
SEQRES 25 B 315 LEU ASN LYS
SEQRES 1 C 167 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 C 167 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 C 167 ASP ASP GLU VAL ARG ILE LEU ILE ALA ASN GLY ALA ASP
SEQRES 4 C 167 VAL ASN ALA VAL ASP ASN THR GLY LEU THR PRO LEU HIS
SEQRES 5 C 167 LEU ALA ALA VAL SER GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 C 167 LEU LEU LYS HIS GLY ALA ASP VAL ASP ALA ALA ASP VAL
SEQRES 7 C 167 TYR GLY PHE THR PRO LEU HIS LEU ALA ALA MET THR GLY
SEQRES 8 C 167 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA
SEQRES 9 C 167 ASP VAL ASN ALA PHE ASP MET THR GLY SER THR PRO LEU
SEQRES 10 C 167 HIS LEU ALA ALA ASP GLU GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 C 167 VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 12 C 167 LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN
SEQRES 13 C 167 GLY ASN GLU ASP LEU ALA LYS SER CYS ARG ASN
SEQRES 1 D 167 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 D 167 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 D 167 ASP ASP GLU VAL ARG ILE LEU ILE ALA ASN GLY ALA ASP
SEQRES 4 D 167 VAL ASN ALA VAL ASP ASN THR GLY LEU THR PRO LEU HIS
SEQRES 5 D 167 LEU ALA ALA VAL SER GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 D 167 LEU LEU LYS HIS GLY ALA ASP VAL ASP ALA ALA ASP VAL
SEQRES 7 D 167 TYR GLY PHE THR PRO LEU HIS LEU ALA ALA MET THR GLY
SEQRES 8 D 167 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA
SEQRES 9 D 167 ASP VAL ASN ALA PHE ASP MET THR GLY SER THR PRO LEU
SEQRES 10 D 167 HIS LEU ALA ALA ASP GLU GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 D 167 VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 12 D 167 LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN
SEQRES 13 D 167 GLY ASN GLU ASP LEU ALA LYS SER CYS ARG ASN
FORMUL 5 HOH *406(H2 O)
HELIX 1 1 SER A 87 LEU A 89 5 3
HELIX 2 2 LYS A 91 SER A 107 1 17
HELIX 3 3 SER A 137 LYS A 146 1 10
HELIX 4 4 THR A 149 ASN A 170 1 22
HELIX 5 5 LYS A 178 GLY A 180 5 3
HELIX 6 6 ALA A 219 SER A 224 1 6
HELIX 7 7 PHE A 230 GLY A 247 1 18
HELIX 8 8 CYS A 255 ASN A 266 1 12
HELIX 9 9 ASN A 275 LEU A 286 1 12
HELIX 10 10 ASP A 289 ARG A 293 5 5
HELIX 11 11 THR A 295 ASN A 301 1 7
HELIX 12 12 ASP A 302 SER A 307 1 6
HELIX 13 13 PRO A 315 THR A 320 5 6
HELIX 14 14 SER B 87 LEU B 89 5 3
HELIX 15 15 LYS B 91 ARG B 106 1 16
HELIX 16 16 SER B 137 LYS B 146 1 10
HELIX 17 17 THR B 149 ASN B 170 1 22
HELIX 18 18 LYS B 178 GLY B 180 5 3
HELIX 19 19 ALA B 219 SER B 224 1 6
HELIX 20 20 PHE B 230 GLY B 247 1 18
HELIX 21 21 CYS B 255 ASN B 266 1 12
HELIX 22 22 ASN B 275 LEU B 286 1 12
HELIX 23 23 ASP B 289 ARG B 293 5 5
HELIX 24 24 THR B 295 ASN B 301 1 7
HELIX 25 25 ASP B 302 SER B 307 1 6
HELIX 26 26 PRO B 315 THR B 320 5 6
HELIX 27 27 SER C 12 GLY C 25 1 14
HELIX 28 28 GLN C 26 ASN C 36 1 11
HELIX 29 29 THR C 49 SER C 57 1 9
HELIX 30 30 HIS C 59 HIS C 69 1 11
HELIX 31 31 THR C 82 GLY C 91 1 10
HELIX 32 32 HIS C 92 TYR C 102 1 11
HELIX 33 33 THR C 115 GLU C 123 1 9
HELIX 34 34 HIS C 125 TYR C 135 1 11
HELIX 35 35 ASP D 13 GLY D 25 1 13
HELIX 36 36 GLN D 26 ASN D 36 1 11
HELIX 37 37 THR D 49 GLY D 58 1 10
HELIX 38 38 HIS D 59 HIS D 69 1 11
HELIX 39 39 THR D 82 GLY D 91 1 10
HELIX 40 40 HIS D 92 TYR D 102 1 11
HELIX 41 41 THR D 115 GLU D 123 1 9
HELIX 42 42 HIS D 125 TYR D 135 1 11
SHEET 1 AA 6 VAL A 43 VAL A 45 0
SHEET 2 AA 6 ARG A 52 GLY A 62 -1 O TYR A 53 N LEU A 44
SHEET 3 AA 6 ALA A 65 ASP A 72 -1 O ALA A 65 N GLY A 62
SHEET 4 AA 6 VAL A 78 PRO A 85 -1 O PHE A 79 N ILE A 70
SHEET 5 AA 6 PHE A 125 LEU A 130 -1 O VAL A 126 N VAL A 84
SHEET 6 AA 6 PHE A 116 GLU A 121 -1 N HIS A 117 O VAL A 129
SHEET 1 AB 2 VAL A 172 ILE A 173 0
SHEET 2 AB 2 THR A 199 LYS A 200 -1 O THR A 199 N ILE A 173
SHEET 1 AC 2 LEU A 182 LEU A 184 0
SHEET 2 AC 2 VAL A 190 ILE A 192 -1 O LYS A 191 N PHE A 183
SHEET 1 BA 6 VAL B 43 ASP B 46 0
SHEET 2 BA 6 ARG B 51 GLY B 62 -1 O ARG B 51 N ASP B 46
SHEET 3 BA 6 ALA B 65 ASP B 72 -1 O ALA B 65 N GLY B 62
SHEET 4 BA 6 VAL B 78 PRO B 85 -1 O PHE B 79 N ILE B 70
SHEET 5 BA 6 PHE B 125 LEU B 130 -1 O VAL B 126 N VAL B 84
SHEET 6 BA 6 PHE B 116 GLU B 121 -1 N HIS B 117 O VAL B 129
SHEET 1 BB 2 VAL B 172 ILE B 173 0
SHEET 2 BB 2 THR B 199 LYS B 200 -1 O THR B 199 N ILE B 173
SHEET 1 BC 2 LEU B 182 LEU B 184 0
SHEET 2 BC 2 VAL B 190 ILE B 192 -1 O LYS B 191 N PHE B 183
CRYST1 62.329 135.225 136.824 90.00 90.00 90.00 P 21 21 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 0.016044 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007309 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
