HEADER TRANSFERASE 04-MAY-10 3MVH
TITLE CRYSTAL STRUCTURE OF AKT-1-INHIBITOR COMPLEXES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: V-AKT MURINE THYMOMA VIRAL ONCOGENE HOMOLOG 1 (AKT1);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GSK3-BETA PEPTIDE;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: 10-RESIDUE PEPTIDE FROM GSK3-B (RESIDUES 3-12);
COMPND 12 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: AKT-1, AKT1;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES
KEYWDS KINASE INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PANDIT
REVDAT 4 06-OCT-21 3MVH 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3MVH 1 REMARK
REVDAT 2 30-MAR-11 3MVH 1 JRNL
REVDAT 1 02-JUN-10 3MVH 0
JRNL AUTH K.D.FREEMAN-COOK,C.AUTRY,G.BORZILLO,D.GORDON,
JRNL AUTH 2 E.BARBACCI-TOBIN,V.BERNARDO,D.BRIERE,T.CLARK,M.CORBETT,
JRNL AUTH 3 J.JAKUBCZAK,S.KAKAR,E.KNAUTH,B.LIPPA,M.J.LUZZIO,M.MANSOUR,
JRNL AUTH 4 G.MARTINELLI,M.MARX,K.NELSON,J.PANDIT,F.RAJAMOHAN,
JRNL AUTH 5 S.ROBINSON,C.SUBRAMANYAM,L.WEI,M.WYTHES,J.MORRIS
JRNL TITL DESIGN OF SELECTIVE, ATP-COMPETITIVE INHIBITORS OF AKT.
JRNL REF J.MED.CHEM. V. 53 4615 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 20481595
JRNL DOI 10.1021/JM1003842
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 27814
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1392
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1827
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.52000
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): 0.158
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.447
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2785 ; 0.028 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3760 ; 2.181 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 329 ; 7.085 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;35.292 ;23.529
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 501 ;14.666 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;20.618 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 390 ; 0.164 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2126 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1368 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1892 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 240 ; 0.175 ; 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): 29 ; 0.196 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.194 ; 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): 1703 ; 1.727 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2632 ; 2.275 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1292 ; 3.703 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1128 ; 5.216 ; 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 : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3MVH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARI-MAX OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27827
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 90.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.15500
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 27.63050
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: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 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 139
REMARK 465 ALA A 140
REMARK 465 MET A 141
REMARK 465 ASP A 142
REMARK 465 PRO A 143
REMARK 465 ARG A 144
REMARK 465 MET A 446
REMARK 465 ILE A 447
REMARK 465 THR A 448
REMARK 465 ILE A 449
REMARK 465 THR A 450
REMARK 465 PRO A 451
REMARK 465 PRO A 452
REMARK 465 ASP A 453
REMARK 465 GLN A 454
REMARK 465 ASP A 455
REMARK 465 ASP A 456
REMARK 465 SER A 457
REMARK 465 MET A 458
REMARK 465 GLU A 459
REMARK 465 CYS A 460
REMARK 465 VAL A 461
REMARK 465 ASP A 462
REMARK 465 SER A 463
REMARK 465 GLU A 464
REMARK 465 ARG A 465
REMARK 465 SER A 477
REMARK 465 SER A 478
REMARK 465 THR A 479
REMARK 465 ALA A 480
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 OE1 GLU B 10 O HOH B 1233 2.12
REMARK 500 O HOH A 1198 O HOH A 1211 2.12
REMARK 500 CB ASN A 204 O HOH A 1221 2.13
REMARK 500 OE2 GLU A 242 O HOH A 1220 2.15
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 VAL A 330 CB VAL A 330 CG2 0.130
REMARK 500 VAL A 337 CB VAL A 337 CG1 0.150
REMARK 500 TYR A 340 CE1 TYR A 340 CZ 0.080
REMARK 500 GLU A 397 CG GLU A 397 CD 0.096
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 328 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 367 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 LEU A 372 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP A 434 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 434 CB - CG - OD2 ANGL. DEV. = -6.0 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 LEU A 153 -69.40 -121.87
REMARK 500 THR A 160 -63.25 59.95
REMARK 500 THR A 219 -168.83 -115.52
REMARK 500 ARG A 243 -55.20 77.00
REMARK 500 ARG A 273 -15.19 75.58
REMARK 500 ASP A 292 89.81 77.18
REMARK 500 ASP A 302 -139.37 52.79
REMARK 500 ASP A 398 -124.32 52.35
REMARK 500 SER A 431 -36.77 -136.99
REMARK 500 GLU A 432 -39.58 107.88
REMARK 500 THR A 435 39.18 -99.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 1 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 314 OE2
REMARK 620 2 HIS A 354 NE2 94.7
REMARK 620 3 HOH A1034 O 91.7 93.8
REMARK 620 4 HOH A1057 O 90.4 88.4 176.7
REMARK 620 5 HOH A1210 O 172.8 91.9 85.1 92.5
REMARK 620 6 HOH B1045 O 93.2 169.3 93.2 84.2 80.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WFE A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CQU RELATED DB: PDB
REMARK 900 RELATED ID: 3CQW RELATED DB: PDB
REMARK 900 RELATED ID: 3MV5 RELATED DB: PDB
REMARK 900 RELATED ID: 3MVJ RELATED DB: PDB
DBREF 3MVH A 144 480 UNP B2RAM5 B2RAM5_HUMAN 144 480
DBREF 3MVH B 1 10 PDB 3MVH 3MVH 1 10
SEQADV 3MVH GLY A 139 UNP B2RAM5 EXPRESSION TAG
SEQADV 3MVH ALA A 140 UNP B2RAM5 EXPRESSION TAG
SEQADV 3MVH MET A 141 UNP B2RAM5 EXPRESSION TAG
SEQADV 3MVH ASP A 142 UNP B2RAM5 EXPRESSION TAG
SEQADV 3MVH PRO A 143 UNP B2RAM5 EXPRESSION TAG
SEQADV 3MVH ASP A 473 UNP B2RAM5 SER 473 ENGINEERED MUTATION
SEQRES 1 A 342 GLY ALA MET ASP PRO ARG VAL THR MET ASN GLU PHE GLU
SEQRES 2 A 342 TYR LEU LYS LEU LEU GLY LYS GLY THR PHE GLY LYS VAL
SEQRES 3 A 342 ILE LEU VAL LYS GLU LYS ALA THR GLY ARG TYR TYR ALA
SEQRES 4 A 342 MET LYS ILE LEU LYS LYS GLU VAL ILE VAL ALA LYS ASP
SEQRES 5 A 342 GLU VAL ALA HIS THR LEU THR GLU ASN ARG VAL LEU GLN
SEQRES 6 A 342 ASN SER ARG HIS PRO PHE LEU THR ALA LEU LYS TYR SER
SEQRES 7 A 342 PHE GLN THR HIS ASP ARG LEU CYS PHE VAL MET GLU TYR
SEQRES 8 A 342 ALA ASN GLY GLY GLU LEU PHE PHE HIS LEU SER ARG GLU
SEQRES 9 A 342 ARG VAL PHE SER GLU ASP ARG ALA ARG PHE TYR GLY ALA
SEQRES 10 A 342 GLU ILE VAL SER ALA LEU ASP TYR LEU HIS SER GLU LYS
SEQRES 11 A 342 ASN VAL VAL TYR ARG ASP LEU LYS LEU GLU ASN LEU MET
SEQRES 12 A 342 LEU ASP LYS ASP GLY HIS ILE LYS ILE THR ASP PHE GLY
SEQRES 13 A 342 LEU CYS LYS GLU GLY ILE LYS ASP GLY ALA THR MET LYS
SEQRES 14 A 342 TPO PHE CYS GLY THR PRO GLU TYR LEU ALA PRO GLU VAL
SEQRES 15 A 342 LEU GLU ASP ASN ASP TYR GLY ARG ALA VAL ASP TRP TRP
SEQRES 16 A 342 GLY LEU GLY VAL VAL MET TYR GLU MET MET CYS GLY ARG
SEQRES 17 A 342 LEU PRO PHE TYR ASN GLN ASP HIS GLU LYS LEU PHE GLU
SEQRES 18 A 342 LEU ILE LEU MET GLU GLU ILE ARG PHE PRO ARG THR LEU
SEQRES 19 A 342 GLY PRO GLU ALA LYS SER LEU LEU SER GLY LEU LEU LYS
SEQRES 20 A 342 LYS ASP PRO LYS GLN ARG LEU GLY GLY GLY SER GLU ASP
SEQRES 21 A 342 ALA LYS GLU ILE MET GLN HIS ARG PHE PHE ALA GLY ILE
SEQRES 22 A 342 VAL TRP GLN HIS VAL TYR GLU LYS LYS LEU SER PRO PRO
SEQRES 23 A 342 PHE LYS PRO GLN VAL THR SER GLU THR ASP THR ARG TYR
SEQRES 24 A 342 PHE ASP GLU GLU PHE THR ALA GLN MET ILE THR ILE THR
SEQRES 25 A 342 PRO PRO ASP GLN ASP ASP SER MET GLU CYS VAL ASP SER
SEQRES 26 A 342 GLU ARG ARG PRO HIS PHE PRO GLN PHE ASP TYR SER ALA
SEQRES 27 A 342 SER SER THR ALA
SEQRES 1 B 10 GLY ARG PRO ARG THR THR SER PHE ALA GLU
MODRES 3MVH TPO A 308 THR PHOSPHOTHREONINE
HET TPO A 308 11
HET MN A 1 1
HET WFE A 999 29
HETNAM TPO PHOSPHOTHREONINE
HETNAM MN MANGANESE (II) ION
HETNAM WFE N-{[(3S)-3-AMINO-1-(5-ETHYL-7H-PYRROLO[2,3-D]PYRIMIDIN-
HETNAM 2 WFE 4-YL)PYRROLIDIN-3-YL]METHYL}-2,4-DIFLUOROBENZAMIDE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 MN MN 2+
FORMUL 4 WFE C20 H22 F2 N6 O
FORMUL 5 HOH *247(H2 O)
HELIX 1 1 THR A 146 ASN A 148 5 3
HELIX 2 2 LYS A 183 LYS A 189 1 7
HELIX 3 3 GLU A 191 SER A 205 1 15
HELIX 4 4 GLU A 234 ARG A 243 1 10
HELIX 5 5 SER A 246 GLU A 267 1 22
HELIX 6 6 LYS A 276 GLU A 278 5 3
HELIX 7 7 THR A 312 LEU A 316 5 5
HELIX 8 8 ALA A 317 GLU A 322 1 6
HELIX 9 9 ALA A 329 GLY A 345 1 17
HELIX 10 10 ASP A 353 GLU A 364 1 12
HELIX 11 11 GLY A 373 LEU A 384 1 12
HELIX 12 12 ASP A 398 GLN A 404 1 7
HELIX 13 13 HIS A 405 ALA A 409 5 5
HELIX 14 14 VAL A 412 GLU A 418 1 7
HELIX 15 15 ASP A 439 GLN A 445 1 7
SHEET 1 A 6 PHE A 150 LYS A 158 0
SHEET 2 A 6 GLY A 162 GLU A 169 -1 O LYS A 168 N GLU A 151
SHEET 3 A 6 TYR A 175 LYS A 182 -1 O MET A 178 N ILE A 165
SHEET 4 A 6 ARG A 222 MET A 227 -1 O MET A 227 N ALA A 177
SHEET 5 A 6 LEU A 213 GLN A 218 -1 N TYR A 215 O VAL A 226
SHEET 6 A 6 TYR A 474 SER A 475 -1 O TYR A 474 N SER A 216
SHEET 1 B 2 LEU A 280 LEU A 282 0
SHEET 2 B 2 ILE A 288 ILE A 290 -1 O LYS A 289 N MET A 281
SHEET 1 C 2 PHE A 309 GLY A 311 0
SHEET 2 C 2 PHE B 8 GLU B 10 -1 O GLU B 10 N PHE A 309
LINK C LYS A 307 N TPO A 308 1555 1555 1.33
LINK C TPO A 308 N PHE A 309 1555 1555 1.34
LINK MN MN A 1 OE2 GLU A 314 1555 1555 2.29
LINK MN MN A 1 NE2 HIS A 354 1555 1555 2.37
LINK MN MN A 1 O HOH A1034 1555 1555 2.35
LINK MN MN A 1 O HOH A1057 1555 1555 2.38
LINK MN MN A 1 O HOH A1210 1555 1555 2.21
LINK MN MN A 1 O HOH B1045 1555 1555 2.27
SITE 1 AC1 6 GLU A 314 HIS A 354 HOH A1034 HOH A1057
SITE 2 AC1 6 HOH A1210 HOH B1045
SITE 1 AC2 18 LEU A 156 GLY A 157 LYS A 158 GLY A 162
SITE 2 AC2 18 VAL A 164 ALA A 177 LEU A 181 MET A 227
SITE 3 AC2 18 GLU A 228 TYR A 229 ALA A 230 GLU A 234
SITE 4 AC2 18 MET A 281 THR A 291 ASP A 292 PHE A 438
SITE 5 AC2 18 HOH A1058 HOH A1149
CRYST1 42.354 55.261 92.314 90.00 102.64 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 0.023611 0.000000 0.005294 0.00000
SCALE2 0.000000 0.018096 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END