HEADER TRANSFERASE 12-MAR-17 5NEV
TITLE CDK2/CYCLIN A IN COMPLEX WITH COMPOUND 73
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.11.22;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CYCLIN-A2;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: CYCLIN-A,CYCLIN A;
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: CDK2, CDKN2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CCNA2, CCN1, CCNA;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS CDK2 CYCLIN A, CDK2 SELECTIVE TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.COXON,E.ANSCOMBE,S.J.HARNOR,M.P.MARTIN,B.CARBAIN,I.R.HARDCASTLE,
AUTHOR 2 L.K.HARLOW,S.KOROLCHUK,C.J.MATHESON,M.E.M.NOBLE,D.R.NEWELL,D.TURNER,
AUTHOR 3 M.SIVAPRAKASAM,L.Z.WANG,C.WONG,B.T.GOLDING,R.J.GRIFFIN,G.CANO
REVDAT 2 17-JAN-24 5NEV 1 REMARK
REVDAT 1 29-MAR-17 5NEV 0
SPRSDE 29-MAR-17 5NEV 5LQE
JRNL AUTH C.R.COXON,E.ANSCOMBE,S.J.HARNOR,M.P.MARTIN,B.CARBAIN,
JRNL AUTH 2 B.T.GOLDING,I.R.HARDCASTLE,L.K.HARLOW,S.KOROLCHUK,
JRNL AUTH 3 C.J.MATHESON,D.R.NEWELL,M.E.NOBLE,M.SIVAPRAKASAM,
JRNL AUTH 4 S.J.TUDHOPE,D.M.TURNER,L.Z.WANG,S.R.WEDGE,C.WONG,
JRNL AUTH 5 R.J.GRIFFIN,J.A.ENDICOTT,C.CANO
JRNL TITL CYCLIN-DEPENDENT KINASE (CDK) INHIBITORS: STRUCTURE-ACTIVITY
JRNL TITL 2 RELATIONSHIPS AND INSIGHTS INTO THE CDK-2 SELECTIVITY OF
JRNL TITL 3 6-SUBSTITUTED 2-ARYLAMINOPURINES.
JRNL REF J. MED. CHEM. V. 60 1746 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28005359
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01254
REMARK 2
REMARK 2 RESOLUTION. 2.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 29173
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1544
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) : 2.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2135
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8886
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.42000
REMARK 3 B22 (A**2) : -1.63000
REMARK 3 B33 (A**2) : 2.05000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.438
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.423
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.790
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9182 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8677 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12471 ; 1.944 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20146 ; 1.341 ; 2.996
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1099 ; 7.086 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 392 ;41.246 ;23.929
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1604 ;18.442 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;19.116 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1400 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9915 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1831 ; 0.002 ; 0.020
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): 4412 ; 0.629 ; 1.295
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4413 ; 0.629 ; 1.295
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5505 ; 1.145 ; 1.942
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5506 ; 1.145 ; 1.941
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4770 ; 0.540 ; 1.318
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4771 ; 0.540 ; 1.318
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6967 ; 0.971 ; 1.960
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10177 ; 2.612 ;14.732
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10178 ; 2.612 ;14.731
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 0 294 C 0 294 18724 0.07 0.05
REMARK 3 2 B 175 429 D 175 429 17042 0.05 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
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 0 A 295
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7880 -25.7430 10.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0895 T22: 0.6300
REMARK 3 T33: 0.5459 T12: -0.0216
REMARK 3 T13: -0.0789 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 3.3951 L22: 3.2265
REMARK 3 L33: 3.1330 L12: -0.9791
REMARK 3 L13: -1.9045 L23: 0.1569
REMARK 3 S TENSOR
REMARK 3 S11: 0.0005 S12: -0.2596 S13: -0.2162
REMARK 3 S21: 0.4453 S22: 0.1164 S23: -0.2792
REMARK 3 S31: -0.2394 S32: 0.3684 S33: -0.1169
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 : B 175 B 429
REMARK 3 ORIGIN FOR THE GROUP (A): -20.9340 1.0790 -1.6270
REMARK 3 T TENSOR
REMARK 3 T11: 0.2698 T22: 0.5794
REMARK 3 T33: 0.5170 T12: 0.0270
REMARK 3 T13: 0.0526 T23: 0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 2.0566 L22: 3.4336
REMARK 3 L33: 3.4263 L12: 0.5627
REMARK 3 L13: 0.6793 L23: 0.6967
REMARK 3 S TENSOR
REMARK 3 S11: 0.0092 S12: 0.3425 S13: 0.3448
REMARK 3 S21: -0.2671 S22: 0.0338 S23: 0.0415
REMARK 3 S31: -0.5478 S32: 0.1251 S33: -0.0431
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 : C 0 C 296
REMARK 3 ORIGIN FOR THE GROUP (A): -47.2870 11.5220 33.4340
REMARK 3 T TENSOR
REMARK 3 T11: 0.8724 T22: 0.8632
REMARK 3 T33: 0.6329 T12: 0.0418
REMARK 3 T13: 0.0890 T23: -0.1852
REMARK 3 L TENSOR
REMARK 3 L11: 3.6817 L22: 3.6902
REMARK 3 L33: 2.0484 L12: -0.3566
REMARK 3 L13: -0.9654 L23: -0.6038
REMARK 3 S TENSOR
REMARK 3 S11: -0.3045 S12: -0.2918 S13: 0.0099
REMARK 3 S21: 0.3765 S22: 0.3084 S23: 0.3640
REMARK 3 S31: -0.2464 S32: -0.5584 S33: -0.0038
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 : D 175 D 429
REMARK 3 ORIGIN FOR THE GROUP (A): -42.6170 -21.3000 35.0160
REMARK 3 T TENSOR
REMARK 3 T11: 1.0515 T22: 0.7071
REMARK 3 T33: 0.8885 T12: -0.2259
REMARK 3 T13: 0.3752 T23: -0.1331
REMARK 3 L TENSOR
REMARK 3 L11: 4.4271 L22: 4.9015
REMARK 3 L33: 2.8193 L12: 0.0936
REMARK 3 L13: 0.0454 L23: -1.2030
REMARK 3 S TENSOR
REMARK 3 S11: -0.3472 S12: 0.0281 S13: -0.7376
REMARK 3 S21: 0.0670 S22: 0.2347 S23: 0.9383
REMARK 3 S31: 0.6908 S32: -0.6088 S33: 0.1125
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 : E 1 E 2
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8180 -3.7270 28.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.5701 T22: 1.3049
REMARK 3 T33: 1.0425 T12: 0.1349
REMARK 3 T13: -0.6622 T23: -0.7333
REMARK 3 L TENSOR
REMARK 3 L11: 0.8991 L22: 2.9625
REMARK 3 L33: 3.9754 L12: 1.6242
REMARK 3 L13: -1.8884 L23: -3.4266
REMARK 3 S TENSOR
REMARK 3 S11: 0.1871 S12: -0.0865 S13: -0.1610
REMARK 3 S21: 0.5235 S22: -0.4290 S23: -0.2315
REMARK 3 S31: -0.6189 S32: 0.2657 S33: 0.2419
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5NEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200003990.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.969
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30773
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.970
REMARK 200 RESOLUTION RANGE LOW (A) : 66.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 704.0
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1H1S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 5MG PER ML. 0.6 TO 0.8M
REMARK 280 KCL, 0.9 TO 1.2M (NH402SO4, AND 100MM HEPES (PH 7.0), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 36.76350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.61000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.02650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.61000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.76350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.02650
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 LEU A 296
REMARK 465 ARG A 297
REMARK 465 LEU A 298
REMARK 465 MET B 173
REMARK 465 GLU B 174
REMARK 465 LEU B 430
REMARK 465 ASN B 431
REMARK 465 LEU B 432
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 LEU C -2
REMARK 465 GLY C -1
REMARK 465 ARG C 297
REMARK 465 LEU C 298
REMARK 465 MET D 173
REMARK 465 GLU D 174
REMARK 465 LEU D 430
REMARK 465 ASN D 431
REMARK 465 LEU D 432
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 OH TYR A 15 OE1 GLU A 51 1.83
REMARK 500 O GLU C 40 N GLU C 42 1.99
REMARK 500 OH TYR C 15 OE1 GLU C 51 2.05
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 168 CE1 TYR A 168 CZ -0.087
REMARK 500 GLU A 257 CG GLU A 257 CD 0.115
REMARK 500 GLU B 374 CD GLU B 374 OE2 0.066
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 217 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 CYS B 327 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG B 378 CG - CD - NE ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG C 22 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 187 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG D 187 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LEU D 232 CA - CB - CG ANGL. DEV. = 14.0 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 TYR A 15 53.45 -150.36
REMARK 500 THR A 39 52.04 -59.45
REMARK 500 GLU A 40 -46.13 -166.05
REMARK 500 THR A 41 20.60 -55.27
REMARK 500 THR A 72 -158.33 -113.15
REMARK 500 ASP A 127 42.79 -158.09
REMARK 500 HIS A 161 -69.39 -90.88
REMARK 500 VAL A 163 -38.47 -133.01
REMARK 500 CYS A 177 152.19 -38.62
REMARK 500 SER A 181 -149.50 -142.29
REMARK 500 THR A 290 -155.51 -142.15
REMARK 500 PRO B 176 -25.03 -35.56
REMARK 500 LYS B 226 48.92 38.70
REMARK 500 PHE B 304 12.29 52.76
REMARK 500 VAL B 367 -68.39 -97.81
REMARK 500 TRP B 372 115.73 -34.85
REMARK 500 TYR C 15 46.62 -153.33
REMARK 500 THR C 39 -15.17 -30.15
REMARK 500 GLU C 40 -41.13 -141.48
REMARK 500 THR C 41 24.42 -41.87
REMARK 500 THR C 72 -164.77 -107.74
REMARK 500 ARG C 126 48.01 -92.19
REMARK 500 ASP C 127 46.00 -165.63
REMARK 500 ALA C 144 -12.19 -143.97
REMARK 500 HIS C 161 -69.59 -94.61
REMARK 500 VAL C 163 -51.50 -141.27
REMARK 500 CYS C 177 154.15 -43.63
REMARK 500 SER C 181 -151.50 -142.13
REMARK 500 ARG C 199 53.40 -90.83
REMARK 500 THR C 290 -158.06 -138.42
REMARK 500 PRO D 176 -27.96 -28.00
REMARK 500 CYS D 193 30.53 -91.70
REMARK 500 LYS D 226 48.05 38.80
REMARK 500 PHE D 304 11.61 53.70
REMARK 500 ALA D 307 59.47 -90.81
REMARK 500 VAL D 367 -68.99 -98.10
REMARK 500 TRP D 372 116.49 -37.95
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 GLY C 16 VAL C 17 -149.29
REMARK 500 HIS C 71 THR C 72 147.48
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 72L A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 72L C 301
DBREF 5NEV A 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 5NEV B 174 432 UNP P20248 CCNA2_HUMAN 174 432
DBREF 5NEV C 1 298 UNP P24941 CDK2_HUMAN 1 298
DBREF 5NEV D 174 432 UNP P20248 CCNA2_HUMAN 174 432
SEQADV 5NEV GLY A -4 UNP P24941 EXPRESSION TAG
SEQADV 5NEV PRO A -3 UNP P24941 EXPRESSION TAG
SEQADV 5NEV LEU A -2 UNP P24941 EXPRESSION TAG
SEQADV 5NEV GLY A -1 UNP P24941 EXPRESSION TAG
SEQADV 5NEV SER A 0 UNP P24941 EXPRESSION TAG
SEQADV 5NEV MET B 173 UNP P20248 INITIATING METHIONINE
SEQADV 5NEV GLY C -4 UNP P24941 EXPRESSION TAG
SEQADV 5NEV PRO C -3 UNP P24941 EXPRESSION TAG
SEQADV 5NEV LEU C -2 UNP P24941 EXPRESSION TAG
SEQADV 5NEV GLY C -1 UNP P24941 EXPRESSION TAG
SEQADV 5NEV SER C 0 UNP P24941 EXPRESSION TAG
SEQADV 5NEV MET D 173 UNP P20248 INITIATING METHIONINE
SEQRES 1 A 303 GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU
SEQRES 2 A 303 LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA
SEQRES 3 A 303 ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS
SEQRES 4 A 303 ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR
SEQRES 5 A 303 ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS
SEQRES 6 A 303 PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU
SEQRES 7 A 303 ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP
SEQRES 8 A 303 LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE
SEQRES 9 A 303 PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU
SEQRES 10 A 303 GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS
SEQRES 11 A 303 ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU
SEQRES 12 A 303 GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA
SEQRES 13 A 303 PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL
SEQRES 14 A 303 THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS
SEQRES 15 A 303 LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY
SEQRES 16 A 303 CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE
SEQRES 17 A 303 PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE
SEQRES 18 A 303 ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY
SEQRES 19 A 303 VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS
SEQRES 20 A 303 TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU
SEQRES 21 A 303 ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS
SEQRES 22 A 303 TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU
SEQRES 23 A 303 ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO
SEQRES 24 A 303 HIS LEU ARG LEU
SEQRES 1 B 260 MET GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR
SEQRES 2 B 260 LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY
SEQRES 3 B 260 TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG
SEQRES 4 B 260 ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU
SEQRES 5 B 260 TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN
SEQRES 6 B 260 TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG
SEQRES 7 B 260 GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU
SEQRES 8 B 260 ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA
SEQRES 9 B 260 GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS
SEQRES 10 B 260 GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU
SEQRES 11 B 260 THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU
SEQRES 12 B 260 THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS
SEQRES 13 B 260 VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU
SEQRES 14 B 260 ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL
SEQRES 15 B 260 ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL
SEQRES 16 B 260 THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR
SEQRES 17 B 260 GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP
SEQRES 18 B 260 LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN
SEQRES 19 B 260 GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS
SEQRES 20 B 260 GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
SEQRES 1 C 303 GLY PRO LEU GLY SER MET GLU ASN PHE GLN LYS VAL GLU
SEQRES 2 C 303 LYS ILE GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA
SEQRES 3 C 303 ARG ASN LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS
SEQRES 4 C 303 ILE ARG LEU ASP THR GLU THR GLU GLY VAL PRO SER THR
SEQRES 5 C 303 ALA ILE ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS
SEQRES 6 C 303 PRO ASN ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU
SEQRES 7 C 303 ASN LYS LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP
SEQRES 8 C 303 LEU LYS LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE
SEQRES 9 C 303 PRO LEU PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU
SEQRES 10 C 303 GLN GLY LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS
SEQRES 11 C 303 ARG ASP LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU
SEQRES 12 C 303 GLY ALA ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA
SEQRES 13 C 303 PHE GLY VAL PRO VAL ARG THR TYR TPO HIS GLU VAL VAL
SEQRES 14 C 303 THR LEU TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS
SEQRES 15 C 303 LYS TYR TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY
SEQRES 16 C 303 CYS ILE PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE
SEQRES 17 C 303 PRO GLY ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE
SEQRES 18 C 303 ARG THR LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY
SEQRES 19 C 303 VAL THR SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS
SEQRES 20 C 303 TRP ALA ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU
SEQRES 21 C 303 ASP GLU ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS
SEQRES 22 C 303 TYR ASP PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU
SEQRES 23 C 303 ALA HIS PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO
SEQRES 24 C 303 HIS LEU ARG LEU
SEQRES 1 D 260 MET GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR
SEQRES 2 D 260 LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY
SEQRES 3 D 260 TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG
SEQRES 4 D 260 ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU
SEQRES 5 D 260 TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN
SEQRES 6 D 260 TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG
SEQRES 7 D 260 GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU
SEQRES 8 D 260 ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA
SEQRES 9 D 260 GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS
SEQRES 10 D 260 GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU
SEQRES 11 D 260 THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU
SEQRES 12 D 260 THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS
SEQRES 13 D 260 VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU
SEQRES 14 D 260 ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL
SEQRES 15 D 260 ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL
SEQRES 16 D 260 THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR
SEQRES 17 D 260 GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP
SEQRES 18 D 260 LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN
SEQRES 19 D 260 GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS
SEQRES 20 D 260 GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU
MODRES 5NEV TPO A 160 THR MODIFIED RESIDUE
MODRES 5NEV TPO C 160 THR MODIFIED RESIDUE
HET TPO A 160 11
HET TPO C 160 11
HET 72L A 301 32
HET 72L C 301 32
HETNAM TPO PHOSPHOTHREONINE
HETNAM 72L 4-[[6-(3-PHENYLPHENYL)-7~{H}-PURIN-2-
HETNAM 2 72L YL]AMINO]BENZENESULFONAMIDE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 5 72L 2(C23 H18 N6 O2 S)
FORMUL 7 HOH *16(H2 O)
HELIX 1 AA1 PRO A 45 GLU A 57 1 13
HELIX 2 AA2 LEU A 87 SER A 94 1 8
HELIX 3 AA3 PRO A 100 HIS A 121 1 22
HELIX 4 AA4 LYS A 129 GLN A 131 5 3
HELIX 5 AA5 ASP A 145 ALA A 149 5 5
HELIX 6 AA6 THR A 165 ARG A 169 5 5
HELIX 7 AA7 ALA A 170 LEU A 175 1 6
HELIX 8 AA8 THR A 182 ARG A 199 1 18
HELIX 9 AA9 SER A 207 GLY A 220 1 14
HELIX 10 AB1 GLY A 229 MET A 233 5 5
HELIX 11 AB2 ASP A 247 VAL A 252 1 6
HELIX 12 AB3 ASP A 256 LEU A 267 1 12
HELIX 13 AB4 SER A 276 LEU A 281 1 6
HELIX 14 AB5 ALA A 282 GLN A 287 5 6
HELIX 15 AB6 TYR B 178 CYS B 193 1 16
HELIX 16 AB7 GLY B 198 GLN B 203 1 6
HELIX 17 AB8 THR B 207 TYR B 225 1 19
HELIX 18 AB9 GLN B 228 MET B 246 1 19
HELIX 19 AC1 LEU B 249 GLU B 269 1 21
HELIX 20 AC2 GLU B 274 THR B 282 1 9
HELIX 21 AC3 THR B 287 LEU B 302 1 16
HELIX 22 AC4 THR B 310 PHE B 319 1 10
HELIX 23 AC5 LEU B 320 GLN B 322 5 3
HELIX 24 AC6 ASN B 326 SER B 340 1 15
HELIX 25 AC7 ASP B 343 LEU B 348 1 6
HELIX 26 AC8 LEU B 351 VAL B 367 1 17
HELIX 27 AC9 PRO B 373 GLY B 381 1 9
HELIX 28 AD1 THR B 383 LYS B 400 1 18
HELIX 29 AD2 GLN B 407 TYR B 413 1 7
HELIX 30 AD3 LYS B 414 HIS B 419 5 6
HELIX 31 AD4 PRO C 45 GLU C 57 1 13
HELIX 32 AD5 LEU C 87 SER C 94 1 8
HELIX 33 AD6 PRO C 100 SER C 120 1 21
HELIX 34 AD7 LYS C 129 GLN C 131 5 3
HELIX 35 AD8 ASP C 145 ALA C 149 5 5
HELIX 36 AD9 THR C 165 ARG C 169 5 5
HELIX 37 AE1 ALA C 170 LEU C 175 1 6
HELIX 38 AE2 THR C 182 THR C 198 1 17
HELIX 39 AE3 SER C 207 GLY C 220 1 14
HELIX 40 AE4 GLY C 229 MET C 233 5 5
HELIX 41 AE5 ASP C 247 VAL C 252 1 6
HELIX 42 AE6 ASP C 256 LEU C 267 1 12
HELIX 43 AE7 SER C 276 LEU C 281 1 6
HELIX 44 AE8 ALA C 282 GLN C 287 5 6
HELIX 45 AE9 TYR D 178 CYS D 193 1 16
HELIX 46 AF1 GLY D 198 GLN D 203 1 6
HELIX 47 AF2 THR D 207 TYR D 225 1 19
HELIX 48 AF3 GLN D 228 MET D 246 1 19
HELIX 49 AF4 LEU D 249 GLU D 269 1 21
HELIX 50 AF5 GLU D 274 THR D 282 1 9
HELIX 51 AF6 THR D 287 LEU D 302 1 16
HELIX 52 AF7 THR D 310 PHE D 319 1 10
HELIX 53 AF8 LEU D 320 GLN D 322 5 3
HELIX 54 AF9 ASN D 326 SER D 340 1 15
HELIX 55 AG1 ASP D 343 LEU D 348 1 6
HELIX 56 AG2 LEU D 351 VAL D 367 1 17
HELIX 57 AG3 PRO D 373 GLY D 381 1 9
HELIX 58 AG4 THR D 383 LYS D 400 1 18
HELIX 59 AG5 GLN D 407 TYR D 413 1 7
HELIX 60 AG6 LYS D 414 HIS D 419 5 6
SHEET 1 AA1 5 PHE A 4 GLY A 13 0
SHEET 2 AA1 5 GLY A 16 ASN A 23 -1 O LYS A 20 N GLU A 8
SHEET 3 AA1 5 VAL A 29 ARG A 36 -1 O LYS A 34 N VAL A 17
SHEET 4 AA1 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 AA1 5 LEU A 66 HIS A 71 -1 N ILE A 70 O TYR A 77
SHEET 1 AA2 3 GLN A 85 ASP A 86 0
SHEET 2 AA2 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 AA2 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
SHEET 1 AA3 2 VAL A 123 LEU A 124 0
SHEET 2 AA3 2 ARG A 150 ALA A 151 -1 O ARG A 150 N LEU A 124
SHEET 1 AA4 5 PHE C 4 GLU C 12 0
SHEET 2 AA4 5 VAL C 17 ASN C 23 -1 O LYS C 20 N GLU C 8
SHEET 3 AA4 5 VAL C 29 ARG C 36 -1 O LYS C 34 N VAL C 17
SHEET 4 AA4 5 LYS C 75 GLU C 81 -1 O LEU C 76 N ILE C 35
SHEET 5 AA4 5 LEU C 66 HIS C 71 -1 N ILE C 70 O TYR C 77
SHEET 1 AA5 3 GLN C 85 ASP C 86 0
SHEET 2 AA5 3 LEU C 133 ILE C 135 -1 O ILE C 135 N GLN C 85
SHEET 3 AA5 3 ILE C 141 LEU C 143 -1 O LYS C 142 N LEU C 134
SHEET 1 AA6 2 VAL C 123 LEU C 124 0
SHEET 2 AA6 2 ARG C 150 ALA C 151 -1 O ARG C 150 N LEU C 124
LINK C TYR A 159 N TPO A 160 1555 1555 1.33
LINK C TPO A 160 N HIS A 161 1555 1555 1.35
LINK C TYR C 159 N TPO C 160 1555 1555 1.33
LINK C TPO C 160 N HIS C 161 1555 1555 1.33
CISPEP 1 VAL A 154 PRO A 155 0 -6.73
CISPEP 2 GLN B 323 PRO B 324 0 -7.76
CISPEP 3 ASP B 345 PRO B 346 0 11.60
CISPEP 4 VAL C 154 PRO C 155 0 -3.96
CISPEP 5 GLN D 323 PRO D 324 0 -6.27
CISPEP 6 ASP D 345 PRO D 346 0 10.31
SITE 1 AC1 15 GLY A 11 GLU A 12 ALA A 31 VAL A 64
SITE 2 AC1 15 PHE A 80 GLU A 81 PHE A 82 LEU A 83
SITE 3 AC1 15 HIS A 84 GLN A 85 ASP A 86 LYS A 89
SITE 4 AC1 15 GLN A 131 LEU A 134 ASP A 145
SITE 1 AC2 15 ILE C 10 GLY C 11 LYS C 33 VAL C 64
SITE 2 AC2 15 PHE C 80 GLU C 81 LEU C 83 HIS C 84
SITE 3 AC2 15 GLN C 85 ASP C 86 LYS C 89 GLN C 131
SITE 4 AC2 15 LEU C 134 ASP C 145 GLN D 403
CRYST1 73.527 132.053 149.220 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 0.013600 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007573 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
