HEADER TRANSCRIPTION REPRESSOR, CELL CYCLE 07-SEP-07 2R7G
TITLE STRUCTURE OF THE RETINOBLASTOMA PROTEIN POCKET DOMAIN IN COMPLEX WITH
TITLE 2 ADENOVIRUS E1A CR1 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOBLASTOMA-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: POCKET DOMAIN, DELETION OF RESIDUES 582-642;
COMPND 5 SYNONYM: PP110; P105-RB; RB;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EARLY E1A 32 KDA PROTEIN;
COMPND 9 CHAIN: B, D, E;
COMPND 10 FRAGMENT: CR1 DOMAIN;
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: RB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN ADENOVIRUS 5;
SOURCE 13 ORGANISM_TAXID: 28285;
SOURCE 14 STRAIN: TYPE 5;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PGEX4T-1
KEYWDS RETINOBLASTOMA PROTEIN, E1A, E2F DISPLACEMENT, TRANSCRIPTION
KEYWDS 2 REPRESSOR, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LIU,R.MARMORSTEIN
REVDAT 7 21-FEB-24 2R7G 1 REMARK
REVDAT 6 25-OCT-17 2R7G 1 REMARK
REVDAT 5 26-JUL-17 2R7G 1 SOURCE REMARK
REVDAT 4 13-JUL-11 2R7G 1 VERSN
REVDAT 3 24-FEB-09 2R7G 1 VERSN
REVDAT 2 20-NOV-07 2R7G 1 JRNL
REVDAT 1 02-OCT-07 2R7G 0
JRNL AUTH X.LIU,R.MARMORSTEIN
JRNL TITL STRUCTURE OF THE RETINOBLASTOMA PROTEIN BOUND TO ADENOVIRUS
JRNL TITL 2 E1A REVEALS THE MOLECULAR BASIS FOR VIRAL ONCOPROTEIN
JRNL TITL 3 INACTIVATION OF A TUMOR SUPPRESSOR
JRNL REF GENES DEV. V. 21 2711 2007
JRNL REFN ISSN 0890-9369
JRNL PMID 17974914
JRNL DOI 10.1101/GAD.1590607
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 115475
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11573
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) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3627
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 403
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5775
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 482
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.37000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.237
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5955 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8025 ; 1.256 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 699 ; 4.631 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 269 ;36.808 ;23.858
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1144 ;15.904 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;12.195 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 910 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4326 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3281 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4157 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 552 ; 0.115 ; 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): 53 ; 0.213 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.212 ; 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): 3646 ; 0.860 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5766 ; 1.405 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2594 ; 2.206 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2259 ; 3.332 ; 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 : 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 380 A 785
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1055 0.2593 0.6307
REMARK 3 T TENSOR
REMARK 3 T11: -0.0437 T22: -0.0448
REMARK 3 T33: -0.0399 T12: -0.0009
REMARK 3 T13: -0.0189 T23: 0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 0.8530 L22: 0.6726
REMARK 3 L33: 1.2205 L12: -0.0569
REMARK 3 L13: -0.0979 L23: 0.0403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0388 S12: 0.1643 S13: 0.0659
REMARK 3 S21: -0.2048 S22: -0.0212 S23: 0.0906
REMARK 3 S31: 0.0317 S32: -0.1991 S33: -0.0176
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 40 B 49
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6310 -5.2427 14.1492
REMARK 3 T TENSOR
REMARK 3 T11: -0.0571 T22: -0.0612
REMARK 3 T33: -0.0494 T12: -0.0373
REMARK 3 T13: -0.0242 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 7.8664 L22: 3.4987
REMARK 3 L33: 9.6675 L12: -3.2532
REMARK 3 L13: -0.4844 L23: -1.2412
REMARK 3 S TENSOR
REMARK 3 S11: 0.2488 S12: -0.0847 S13: 0.0306
REMARK 3 S21: -0.3015 S22: 0.0190 S23: 0.1953
REMARK 3 S31: 0.4032 S32: -0.4823 S33: -0.2678
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 380 C 785
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9239 -13.6436 32.4229
REMARK 3 T TENSOR
REMARK 3 T11: -0.0549 T22: -0.0291
REMARK 3 T33: -0.0414 T12: -0.0015
REMARK 3 T13: -0.0258 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 0.9331 L22: 0.8510
REMARK 3 L33: 1.1186 L12: -0.0566
REMARK 3 L13: -0.0979 L23: 0.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: -0.2900 S13: -0.1018
REMARK 3 S21: 0.1523 S22: 0.0133 S23: -0.0890
REMARK 3 S31: 0.1675 S32: 0.0427 S33: -0.0131
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 40 D 49
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7209 -21.4607 18.9919
REMARK 3 T TENSOR
REMARK 3 T11: -0.0344 T22: -0.0686
REMARK 3 T33: -0.0559 T12: -0.0408
REMARK 3 T13: -0.0084 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 5.7954 L22: 6.0318
REMARK 3 L33: 10.4035 L12: -4.4347
REMARK 3 L13: 0.8894 L23: 0.5912
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: -0.4209 S13: -0.1232
REMARK 3 S21: 0.0020 S22: 0.1471 S23: -0.0427
REMARK 3 S31: 0.5732 S32: -0.1259 S33: -0.2103
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 40 E 48
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1919 -13.0292 -30.0390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0003 T22: 0.0002
REMARK 3 T33: 0.0000 T12: 0.0001
REMARK 3 T13: -0.0003 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 11.7415 L22: 13.8033
REMARK 3 L33: 28.1912 L12: 5.5691
REMARK 3 L13: -3.0062 L23: -0.2428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0211 S12: 0.5892 S13: 0.0746
REMARK 3 S21: 0.5535 S22: 0.2573 S23: -0.4185
REMARK 3 S31: 0.9577 S32: 0.0877 S33: -0.2362
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 2R7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000044519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121240
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.671
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15MM MAGNESIUM ACETATE TETRAHYDRATE,
REMARK 280 50MM SODIUM CACODYLATE TRIHYDRATE, PH 6.0 AND 1.7M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7240 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 503
REMARK 465 GLN A 504
REMARK 465 ASN A 505
REMARK 465 LEU A 506
REMARK 465 ASP A 507
REMARK 465 SER A 508
REMARK 465 ARG A 579
REMARK 465 GLU A 580
REMARK 465 GLY A 581
REMARK 465 PRO A 786
REMARK 465 ARG A 787
REMARK 465 SER C 503
REMARK 465 GLN C 504
REMARK 465 ASN C 505
REMARK 465 LEU C 506
REMARK 465 ASP C 507
REMARK 465 SER C 508
REMARK 465 GLU C 580
REMARK 465 GLY C 581
REMARK 465 PRO C 786
REMARK 465 ARG C 787
REMARK 465 LEU E 49
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 GLN A 436 CG CD OE1 NE2
REMARK 470 GLU A 440 CG CD OE1 OE2
REMARK 470 GLN C 436 CG CD OE1 NE2
REMARK 470 GLU C 440 CG CD OE1 OE2
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 SER A 501 -95.15 -66.54
REMARK 500 SER A 560 -47.03 -154.58
REMARK 500 ILE A 744 -74.33 -95.68
REMARK 500 GLU A 746 -87.60 -119.84
REMARK 500 SER C 501 -86.78 -68.83
REMARK 500 SER C 560 -48.16 -157.69
REMARK 500 ASP C 718 -90.77 -52.81
REMARK 500 LEU C 719 85.37 47.63
REMARK 500 ILE C 744 -84.66 -101.33
REMARK 500 GLU C 746 -108.31 52.40
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 SO4 A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 901
DBREF 2R7G A 380 581 UNP P06400 RB_HUMAN 380 581
DBREF 2R7G A 643 787 UNP P06400 RB_HUMAN 643 787
DBREF 2R7G B 40 49 UNP P03255 E1A_ADE05 40 49
DBREF 2R7G C 380 581 UNP P06400 RB_HUMAN 380 581
DBREF 2R7G C 643 787 UNP P06400 RB_HUMAN 643 787
DBREF 2R7G D 40 49 UNP P03255 E1A_ADE05 40 49
DBREF 2R7G E 40 49 UNP P03255 E1A_ADE05 40 49
SEQRES 1 A 347 ASN THR ILE GLN GLN LEU MET MET ILE LEU ASN SER ALA
SEQRES 2 A 347 SER ASP GLN PRO SER GLU ASN LEU ILE SER TYR PHE ASN
SEQRES 3 A 347 ASN CYS THR VAL ASN PRO LYS GLU SER ILE LEU LYS ARG
SEQRES 4 A 347 VAL LYS ASP ILE GLY TYR ILE PHE LYS GLU LYS PHE ALA
SEQRES 5 A 347 LYS ALA VAL GLY GLN GLY CYS VAL GLU ILE GLY SER GLN
SEQRES 6 A 347 ARG TYR LYS LEU GLY VAL ARG LEU TYR TYR ARG VAL MET
SEQRES 7 A 347 GLU SER MET LEU LYS SER GLU GLU GLU ARG LEU SER ILE
SEQRES 8 A 347 GLN ASN PHE SER LYS LEU LEU ASN ASP ASN ILE PHE HIS
SEQRES 9 A 347 MET SER LEU LEU ALA CYS ALA LEU GLU VAL VAL MET ALA
SEQRES 10 A 347 THR TYR SER ARG SER THR SER GLN ASN LEU ASP SER GLY
SEQRES 11 A 347 THR ASP LEU SER PHE PRO TRP ILE LEU ASN VAL LEU ASN
SEQRES 12 A 347 LEU LYS ALA PHE ASP PHE TYR LYS VAL ILE GLU SER PHE
SEQRES 13 A 347 ILE LYS ALA GLU GLY ASN LEU THR ARG GLU MET ILE LYS
SEQRES 14 A 347 HIS LEU GLU ARG CYS GLU HIS ARG ILE MET GLU SER LEU
SEQRES 15 A 347 ALA TRP LEU SER ASP SER PRO LEU PHE ASP LEU ILE LYS
SEQRES 16 A 347 GLN SER LYS ASP ARG GLU GLY LYS SER THR SER LEU SER
SEQRES 17 A 347 LEU PHE TYR LYS LYS VAL TYR ARG LEU ALA TYR LEU ARG
SEQRES 18 A 347 LEU ASN THR LEU CYS GLU ARG LEU LEU SER GLU HIS PRO
SEQRES 19 A 347 GLU LEU GLU HIS ILE ILE TRP THR LEU PHE GLN HIS THR
SEQRES 20 A 347 LEU GLN ASN GLU TYR GLU LEU MET ARG ASP ARG HIS LEU
SEQRES 21 A 347 ASP GLN ILE MET MET CYS SER MET TYR GLY ILE CYS LYS
SEQRES 22 A 347 VAL LYS ASN ILE ASP LEU LYS PHE LYS ILE ILE VAL THR
SEQRES 23 A 347 ALA TYR LYS ASP LEU PRO HIS ALA VAL GLN GLU THR PHE
SEQRES 24 A 347 LYS ARG VAL LEU ILE LYS GLU GLU GLU TYR ASP SER ILE
SEQRES 25 A 347 ILE VAL PHE TYR ASN SER VAL PHE MET GLN ARG LEU LYS
SEQRES 26 A 347 THR ASN ILE LEU GLN TYR ALA SER THR ARG PRO PRO THR
SEQRES 27 A 347 LEU SER PRO ILE PRO HIS ILE PRO ARG
SEQRES 1 B 10 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU
SEQRES 1 C 347 ASN THR ILE GLN GLN LEU MET MET ILE LEU ASN SER ALA
SEQRES 2 C 347 SER ASP GLN PRO SER GLU ASN LEU ILE SER TYR PHE ASN
SEQRES 3 C 347 ASN CYS THR VAL ASN PRO LYS GLU SER ILE LEU LYS ARG
SEQRES 4 C 347 VAL LYS ASP ILE GLY TYR ILE PHE LYS GLU LYS PHE ALA
SEQRES 5 C 347 LYS ALA VAL GLY GLN GLY CYS VAL GLU ILE GLY SER GLN
SEQRES 6 C 347 ARG TYR LYS LEU GLY VAL ARG LEU TYR TYR ARG VAL MET
SEQRES 7 C 347 GLU SER MET LEU LYS SER GLU GLU GLU ARG LEU SER ILE
SEQRES 8 C 347 GLN ASN PHE SER LYS LEU LEU ASN ASP ASN ILE PHE HIS
SEQRES 9 C 347 MET SER LEU LEU ALA CYS ALA LEU GLU VAL VAL MET ALA
SEQRES 10 C 347 THR TYR SER ARG SER THR SER GLN ASN LEU ASP SER GLY
SEQRES 11 C 347 THR ASP LEU SER PHE PRO TRP ILE LEU ASN VAL LEU ASN
SEQRES 12 C 347 LEU LYS ALA PHE ASP PHE TYR LYS VAL ILE GLU SER PHE
SEQRES 13 C 347 ILE LYS ALA GLU GLY ASN LEU THR ARG GLU MET ILE LYS
SEQRES 14 C 347 HIS LEU GLU ARG CYS GLU HIS ARG ILE MET GLU SER LEU
SEQRES 15 C 347 ALA TRP LEU SER ASP SER PRO LEU PHE ASP LEU ILE LYS
SEQRES 16 C 347 GLN SER LYS ASP ARG GLU GLY LYS SER THR SER LEU SER
SEQRES 17 C 347 LEU PHE TYR LYS LYS VAL TYR ARG LEU ALA TYR LEU ARG
SEQRES 18 C 347 LEU ASN THR LEU CYS GLU ARG LEU LEU SER GLU HIS PRO
SEQRES 19 C 347 GLU LEU GLU HIS ILE ILE TRP THR LEU PHE GLN HIS THR
SEQRES 20 C 347 LEU GLN ASN GLU TYR GLU LEU MET ARG ASP ARG HIS LEU
SEQRES 21 C 347 ASP GLN ILE MET MET CYS SER MET TYR GLY ILE CYS LYS
SEQRES 22 C 347 VAL LYS ASN ILE ASP LEU LYS PHE LYS ILE ILE VAL THR
SEQRES 23 C 347 ALA TYR LYS ASP LEU PRO HIS ALA VAL GLN GLU THR PHE
SEQRES 24 C 347 LYS ARG VAL LEU ILE LYS GLU GLU GLU TYR ASP SER ILE
SEQRES 25 C 347 ILE VAL PHE TYR ASN SER VAL PHE MET GLN ARG LEU LYS
SEQRES 26 C 347 THR ASN ILE LEU GLN TYR ALA SER THR ARG PRO PRO THR
SEQRES 27 C 347 LEU SER PRO ILE PRO HIS ILE PRO ARG
SEQRES 1 D 10 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU
SEQRES 1 E 10 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU
HET SO4 A 902 5
HET SO4 C 901 5
HETNAM SO4 SULFATE ION
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 8 HOH *482(H2 O)
HELIX 1 1 THR A 381 ALA A 392 1 12
HELIX 2 2 SER A 397 ASN A 406 1 10
HELIX 3 3 PRO A 411 GLY A 435 1 25
HELIX 4 4 CYS A 438 SER A 469 1 32
HELIX 5 5 PHE A 473 ASN A 478 1 6
HELIX 6 6 ASP A 479 THR A 502 1 24
HELIX 7 7 PRO A 515 ASN A 522 1 8
HELIX 8 8 LYS A 524 LYS A 530 1 7
HELIX 9 9 VAL A 531 GLU A 539 1 9
HELIX 10 10 THR A 543 SER A 560 1 18
HELIX 11 11 LEU A 561 LEU A 564 5 4
HELIX 12 12 PRO A 568 ASP A 578 1 11
HELIX 13 13 SER A 644 LEU A 670 1 27
HELIX 14 14 GLU A 675 GLU A 691 1 17
HELIX 15 15 TYR A 692 ARG A 696 5 5
HELIX 16 16 HIS A 699 LYS A 715 1 17
HELIX 17 17 LYS A 720 LYS A 729 1 10
HELIX 18 18 GLN A 736 ARG A 741 1 6
HELIX 19 19 SER A 751 VAL A 759 1 9
HELIX 20 20 VAL A 759 TYR A 771 1 13
HELIX 21 21 THR B 42 TYR B 47 1 6
HELIX 22 22 THR C 381 ALA C 392 1 12
HELIX 23 23 SER C 397 ASN C 406 1 10
HELIX 24 24 PRO C 411 GLY C 435 1 25
HELIX 25 25 CYS C 438 SER C 469 1 32
HELIX 26 26 PHE C 473 ASN C 478 1 6
HELIX 27 27 ASP C 479 THR C 502 1 24
HELIX 28 28 PRO C 515 ASN C 522 1 8
HELIX 29 29 LYS C 524 LYS C 530 1 7
HELIX 30 30 VAL C 531 GLU C 539 1 9
HELIX 31 31 THR C 543 SER C 560 1 18
HELIX 32 32 LEU C 561 LEU C 564 5 4
HELIX 33 33 PRO C 568 ARG C 579 1 12
HELIX 34 34 SER C 644 LEU C 670 1 27
HELIX 35 35 GLU C 675 GLU C 691 1 17
HELIX 36 36 TYR C 692 ARG C 696 5 5
HELIX 37 37 HIS C 699 LYS C 715 1 17
HELIX 38 38 LYS C 720 LYS C 729 1 10
HELIX 39 39 GLN C 736 ARG C 741 1 6
HELIX 40 40 SER C 751 VAL C 759 1 9
HELIX 41 41 VAL C 759 GLN C 770 1 12
HELIX 42 42 TYR C 771 SER C 773 5 3
HELIX 43 43 THR D 42 TYR D 47 1 6
SHEET 1 A 2 VAL A 742 LEU A 743 0
SHEET 2 A 2 TYR A 749 ASP A 750 -1 O ASP A 750 N VAL A 742
SHEET 1 B 2 VAL C 742 LEU C 743 0
SHEET 2 B 2 TYR C 749 ASP C 750 -1 O ASP C 750 N VAL C 742
CISPEP 1 PHE A 514 PRO A 515 0 2.37
CISPEP 2 PHE C 514 PRO C 515 0 5.57
SITE 1 AC1 11 ASN A 406 CYS A 407 THR A 408 ASN A 472
SITE 2 AC1 11 PHE A 473 SER A 474 HOH A1001 HOH A1009
SITE 3 AC1 11 HOH A1087 LYS C 574 HOH C1076
SITE 1 AC2 11 LYS A 574 HOH A1060 ASN C 406 CYS C 407
SITE 2 AC2 11 THR C 408 ASN C 472 PHE C 473 SER C 474
SITE 3 AC2 11 HOH C1003 HOH C1011 HOH C1088
CRYST1 57.713 57.706 92.268 94.34 92.69 105.79 P 1 3
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 0.017327 0.004899 0.001271 0.00000
SCALE2 0.000000 0.018009 0.001664 0.00000
SCALE3 0.000000 0.000000 0.010896 0.00000
(ATOM LINES ARE NOT SHOWN.)
END