HEADER SIGNALING PROTEIN 25-MAR-10 3MB3
TITLE CRYSTAL STRUCTURE OF THE SECOND BROMODOMAIN OF PLECKSTRIN HOMOLOGY
TITLE 2 DOMAIN INTERACTING PROTEIN (PHIP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PH-INTERACTING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1302-1434;
COMPND 5 SYNONYM: PHIP, IRS-1 PH DOMAIN-BINDING PROTEIN, WD REPEAT-CONTAINING
COMPND 6 PROTEIN 11;
COMPND 7 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: PHIP, WDR11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS PHIP, PLECKSTRIN HOMOLOGY DOMAIN INTERACTING PROTEIN, DCAF14, NDRP,
KEYWDS 2 DDB1 AND CUL4 ASSOCIATED FACTOR 14, SGC, STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, BROMODOMAIN, PHOSPHOPROTEIN, WD REPEAT, SIGNALING
KEYWDS 4 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,S.PICAUD,T.KEATES,E.UGOCHUKWU,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 3 06-SEP-23 3MB3 1 REMARK SEQADV
REVDAT 2 11-APR-12 3MB3 1 JRNL VERSN
REVDAT 1 14-APR-10 3MB3 0
JRNL AUTH P.FILIPPAKOPOULOS,S.PICAUD,M.MANGOS,T.KEATES,J.P.LAMBERT,
JRNL AUTH 2 D.BARSYTE-LOVEJOY,I.FELLETAR,R.VOLKMER,S.MULLER,T.PAWSON,
JRNL AUTH 3 A.C.GINGRAS,C.H.ARROWSMITH,S.KNAPP
JRNL TITL HISTONE RECOGNITION AND LARGE-SCALE STRUCTURAL ANALYSIS OF
JRNL TITL 2 THE HUMAN BROMODOMAIN FAMILY.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 149 214 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22464331
JRNL DOI 10.1016/J.CELL.2012.02.013
REMARK 2
REMARK 2 RESOLUTION. 2.25 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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 17988
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 914
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1231
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.3750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 941
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.37000
REMARK 3 B22 (A**2) : 3.37000
REMARK 3 B33 (A**2) : -5.06000
REMARK 3 B12 (A**2) : 1.69000
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): 0.134
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.127
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.537
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 971 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 672 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1312 ; 1.573 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1629 ; 1.946 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 115 ; 5.861 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;29.072 ;24.167
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 173 ;15.678 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;13.709 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 142 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1066 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 198 ; 0.001 ; 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): 584 ; 4.490 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 226 ; 1.306 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 948 ; 6.428 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 387 ;11.001 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 364 ;14.065 ;11.000
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 : 3
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 1316 A 1350
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0280 48.6087 -0.5033
REMARK 3 T TENSOR
REMARK 3 T11: 0.1679 T22: 0.1067
REMARK 3 T33: 0.2025 T12: -0.0591
REMARK 3 T13: 0.0009 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 5.3359 L22: 3.0736
REMARK 3 L33: 7.5811 L12: 0.6182
REMARK 3 L13: 1.1776 L23: 0.0520
REMARK 3 S TENSOR
REMARK 3 S11: 0.1154 S12: 0.1014 S13: -0.8573
REMARK 3 S21: 0.0077 S22: 0.0624 S23: 0.4697
REMARK 3 S31: 0.5043 S32: -0.4725 S33: -0.1778
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 1351 A 1415
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5930 52.1035 2.0354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2054 T22: 0.0368
REMARK 3 T33: 0.0459 T12: -0.0158
REMARK 3 T13: -0.0119 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 5.7598 L22: 1.7049
REMARK 3 L33: 3.3627 L12: -2.6526
REMARK 3 L13: -1.1736 L23: 0.5896
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: -0.0133 S13: 0.1551
REMARK 3 S21: 0.0602 S22: -0.0249 S23: -0.1317
REMARK 3 S31: 0.0087 S32: 0.2690 S33: -0.0068
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 : A 1416 A 1431
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3376 65.6881 0.5259
REMARK 3 T TENSOR
REMARK 3 T11: 0.3777 T22: 0.4957
REMARK 3 T33: 0.2407 T12: 0.1243
REMARK 3 T13: 0.0401 T23: 0.2510
REMARK 3 L TENSOR
REMARK 3 L11: 12.6561 L22: 27.2923
REMARK 3 L33: 20.1553 L12: -14.1840
REMARK 3 L13: -8.5820 L23: 12.1527
REMARK 3 S TENSOR
REMARK 3 S11: -0.3808 S12: 1.4046 S13: 0.8955
REMARK 3 S21: 0.4266 S22: 0.5669 S23: 0.6056
REMARK 3 S31: -1.2340 S32: -1.3823 S33: -0.1860
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 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3MB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18012
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 39.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.45300
REMARK 200 R SYM FOR SHELL (I) : 0.53000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: ENSEMBLE OF 3HMH, 2NXB, 2OO1, 2OSS, 2OUO, 2RFJ,
REMARK 200 3DAI, 3D7C, 3DWY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG3350 4% GLYCEROL,0.1M ACETATE
REMARK 280 PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.37333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.74667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 50.74667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 25.37333
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 1300
REMARK 465 MET A 1301
REMARK 465 ASP A 1302
REMARK 465 HIS A 1303
REMARK 465 GLN A 1304
REMARK 465 PRO A 1305
REMARK 465 ARG A 1306
REMARK 465 ARG A 1307
REMARK 465 ARG A 1308
REMARK 465 LEU A 1309
REMARK 465 ARG A 1310
REMARK 465 ASN A 1311
REMARK 465 ARG A 1312
REMARK 465 ALA A 1313
REMARK 465 GLN A 1314
REMARK 465 SER A 1315
REMARK 465 HIS A 1432
REMARK 465 LYS A 1433
REMARK 465 ARG A 1434
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 TYR A1316 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A1323 CE NZ
REMARK 470 ARG A1430 CG CD NE CZ NH1 NH2
REMARK 470 PHE A1431 CG CD1 CD2 CE1 CE2 CZ
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 CYS A1382 CB CYS A1382 SG -0.108
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 CYS A1335 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
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 MB3 A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MB4 RELATED DB: PDB
DBREF 3MB3 A 1302 1434 UNP Q8WWQ0 PHIP_HUMAN 1302 1434
SEQADV 3MB3 SER A 1300 UNP Q8WWQ0 EXPRESSION TAG
SEQADV 3MB3 MET A 1301 UNP Q8WWQ0 EXPRESSION TAG
SEQRES 1 A 135 SER MET ASP HIS GLN PRO ARG ARG ARG LEU ARG ASN ARG
SEQRES 2 A 135 ALA GLN SER TYR ASP ILE GLN ALA TRP LYS LYS GLN CYS
SEQRES 3 A 135 GLU GLU LEU LEU ASN LEU ILE PHE GLN CYS GLU ASP SER
SEQRES 4 A 135 GLU PRO PHE ARG GLN PRO VAL ASP LEU LEU GLU TYR PRO
SEQRES 5 A 135 ASP TYR ARG ASP ILE ILE ASP THR PRO MET ASP PHE ALA
SEQRES 6 A 135 THR VAL ARG GLU THR LEU GLU ALA GLY ASN TYR GLU SER
SEQRES 7 A 135 PRO MET GLU LEU CYS LYS ASP VAL ARG LEU ILE PHE SER
SEQRES 8 A 135 ASN SER LYS ALA TYR THR PRO SER LYS ARG SER ARG ILE
SEQRES 9 A 135 TYR SER MET SER LEU ARG LEU SER ALA PHE PHE GLU GLU
SEQRES 10 A 135 HIS ILE SER SER VAL LEU SER ASP TYR LYS SER ALA LEU
SEQRES 11 A 135 ARG PHE HIS LYS ARG
HET MB3 A 1 7
HETNAM MB3 1-METHYLPYRROLIDIN-2-ONE
FORMUL 2 MB3 C5 H9 N O
FORMUL 3 HOH *85(H2 O)
HELIX 1 1 ALA A 1320 CYS A 1335 1 16
HELIX 2 2 GLU A 1336 ARG A 1342 5 7
HELIX 3 3 ASP A 1352 ILE A 1357 1 6
HELIX 4 4 ASP A 1362 ALA A 1372 1 11
HELIX 5 5 SER A 1377 THR A 1396 1 20
HELIX 6 6 SER A 1401 LEU A 1429 1 29
SITE 1 AC1 7 HOH A 41 HOH A 90 HOH A 151 HOH A 152
SITE 2 AC1 7 PRO A1340 VAL A1345 TYR A1350
CRYST1 92.090 92.090 76.120 90.00 90.00 120.00 P 31 2 1 6
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 0.010859 0.006269 0.000000 0.00000
SCALE2 0.000000 0.012539 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013137 0.00000
(ATOM LINES ARE NOT SHOWN.)
END