HEADER TRANSCRIPTION/DNA 20-DEC-11 3V79
TITLE STRUCTURE OF HUMAN NOTCH1 TRANSCRIPTION COMPLEX INCLUDING CSL, RAM,
TITLE 2 ANK, AND MAML-1 ON HES-1 PROMOTER DNA SEQUENCE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 3 CHAIN: K;
COMPND 4 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1,
COMPND 5 NOTCH 1 EXTRACELLULAR TRUNCATION, NOTCH 1 INTRACELLULAR DOMAIN, NICD;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: CBF-1, J KAPPA-RECOMBINATION SIGNAL-BINDING PROTEIN, RBP-J
COMPND 11 KAPPA, RBP-J, RBP-JK, RENAL CARCINOMA ANTIGEN NY-REN-30;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: MASTERMIND-LIKE PROTEIN 1;
COMPND 15 CHAIN: M;
COMPND 16 SYNONYM: MAM-1;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA 5'-
COMPND 20 D(*GP*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*AP*AP*A)-3';
COMPND 21 CHAIN: X;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 5;
COMPND 24 MOLECULE: DNA 5'-
COMPND 25 D(*TP*TP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*TP*AP*AP*C)-3';
COMPND 26 CHAIN: Y;
COMPND 27 ENGINEERED: YES;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: RAM;
COMPND 30 CHAIN: R;
COMPND 31 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: NOTCH1, TAN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: IGKJRB, IGKJRB1, RBPJ, RBPJK, RBPSUH;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: MAML1, KIAA0200;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 MOL_ID: 4;
SOURCE 23 SYNTHETIC: YES;
SOURCE 24 OTHER_DETAILS: SYNTHESIZED OLIGONUCLEOTIDES;
SOURCE 25 MOL_ID: 5;
SOURCE 26 SYNTHETIC: YES;
SOURCE 27 OTHER_DETAILS: SYNTHESIZED OLIGONUCLEOTIDES;
SOURCE 28 MOL_ID: 6;
SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-TREFOIL, ANKYRIN, TRANSCRIPTION ACTIVATION, DNA BINDING,
KEYWDS 2 TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NAM,P.SLIZ,S.BLACKLOW
REVDAT 3 21-MAR-12 3V79 1 JRNL
REVDAT 2 22-FEB-12 3V79 1 COMPND DBREF
REVDAT 1 15-FEB-12 3V79 0
JRNL AUTH S.H.CHOI,T.E.WALES,Y.NAM,D.J.O'DONOVAN,P.SLIZ,J.R.ENGEN,
JRNL AUTH 2 S.C.BLACKLOW
JRNL TITL CONFORMATIONAL LOCKING UPON COOPERATIVE ASSEMBLY OF NOTCH
JRNL TITL 2 TRANSCRIPTION COMPLEXES.
JRNL REF STRUCTURE V. 20 340 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22325781
JRNL DOI 10.1016/J.STR.2011.12.011
REMARK 2
REMARK 2 RESOLUTION. 3.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 40195
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : FROM PDB CODE 2F8X
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2049
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5689
REMARK 3 NUCLEIC ACID ATOMS : 732
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.46
REMARK 3 ESD FROM SIGMAA (A) : 0.87
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.54
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.85
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.003
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.63
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 9.144 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 14.186; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 12.798; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 18.289; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3V79 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB069683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792899
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40195
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 2F8X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 81.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 3350, 5% ETHYLENE GLYCOL, PH
REMARK 280 7.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 59.99350
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 59.99350
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 59.99350
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 59.99350
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 59.99350
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 59.99350
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 300 REMARK: INTRACELLULAR NOTCH, CSL, AND MAML CAN FORM A
REMARK 300 HETEROTRIMERIC COMPLEX ON DNA DUPLEX AS SHOWN IN THE ASYMMETRIC
REMARK 300 UNIT. IN SOME INSTANCES WHEN THE CSL BINDING SITES ARE LOCATED
REMARK 300 CLOSE TO EACH OTHER, A HETEROTRIMER MAY INTERACT WITH ANOTHER
REMARK 300 HETEROTRIMER.
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: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, C, M, R, X, Y
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 K 1872
REMARK 465 MET K 1873
REMARK 465 ASP K 1874
REMARK 465 VAL K 1875
REMARK 465 ASN K 1876
REMARK 465 VAL K 1877
REMARK 465 ARG K 1878
REMARK 465 GLY K 1879
REMARK 465 PRO K 1880
REMARK 465 ASP K 1881
REMARK 465 GLY K 1882
REMARK 465 PHE K 1883
REMARK 465 GLY K 1893
REMARK 465 GLY K 1894
REMARK 465 GLY K 1895
REMARK 465 LEU K 1896
REMARK 465 GLU K 1897
REMARK 465 THR K 1898
REMARK 465 GLY K 1899
REMARK 465 ASN K 1900
REMARK 465 SER K 1901
REMARK 465 GLU K 1902
REMARK 465 GLU K 1903
REMARK 465 GLU K 1904
REMARK 465 GLU K 1905
REMARK 465 ASP K 1906
REMARK 465 ALA K 1907
REMARK 465 PRO K 1908
REMARK 465 GLN K 1917
REMARK 465 GLY K 1918
REMARK 465 ALA K 1919
REMARK 465 ARG K 2121
REMARK 465 SER K 2122
REMARK 465 PRO K 2123
REMARK 465 GLN K 2124
REMARK 465 LEU K 2125
REMARK 465 HIS K 2126
REMARK 465 GLY K 2127
REMARK 465 MET C 8
REMARK 465 GLY C 9
REMARK 465 GLU C 10
REMARK 465 GLY C 435
REMARK 465 HIS C 436
REMARK 465 HIS C 437
REMARK 465 HIS C 438
REMARK 465 HIS C 439
REMARK 465 HIS C 440
REMARK 465 HIS C 441
REMARK 465 GLY M 12
REMARK 465 LEU M 13
REMARK 465 PRO M 14
REMARK 465 ARG M 15
REMARK 465 ALA M 71
REMARK 465 GLY M 72
REMARK 465 LYS M 73
REMARK 465 HIS M 74
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 K1921 -59.39 -152.15
REMARK 500 HIS K1922 53.50 -102.86
REMARK 500 ARG K1941 73.46 -102.79
REMARK 500 ALA K1951 24.99 -75.33
REMARK 500 SER K1952 87.40 51.03
REMARK 500 ASP K1959 -158.29 -83.87
REMARK 500 THR K1987 126.19 -38.70
REMARK 500 ASP K1990 34.18 -96.75
REMARK 500 MET K1993 -170.99 -68.15
REMARK 500 ARG K2005 -61.58 -93.29
REMARK 500 LEU K2006 20.12 -74.55
REMARK 500 ALA K2007 72.05 37.02
REMARK 500 MET K2011 -34.83 -30.81
REMARK 500 HIS K2019 73.94 60.97
REMARK 500 ASP K2021 109.46 -49.52
REMARK 500 ASN K2023 31.60 -93.42
REMARK 500 ASN K2051 39.05 -96.60
REMARK 500 ASN K2054 94.07 -51.61
REMARK 500 HIS K2084 40.82 -81.86
REMARK 500 PHE K2085 51.15 37.47
REMARK 500 ASP K2089 42.66 -106.96
REMARK 500 ASP K2092 -164.58 -70.87
REMARK 500 HIS K2107 62.32 -101.91
REMARK 500 HIS K2108 -37.59 -35.46
REMARK 500 LEU K2114 -4.90 -57.82
REMARK 500 ASN K2118 71.61 31.70
REMARK 500 LEU C 17 103.72 -52.21
REMARK 500 GLU C 28 -76.48 -73.47
REMARK 500 ARG C 29 46.86 77.37
REMARK 500 GLU C 49 -178.68 -58.61
REMARK 500 LYS C 50 79.62 -161.45
REMARK 500 PHE C 52 169.11 -48.57
REMARK 500 ARG C 75 5.59 -65.30
REMARK 500 ALA C 87 149.73 -170.13
REMARK 500 ASN C 93 49.06 -94.25
REMARK 500 ASP C 95 48.16 -84.69
REMARK 500 TYR C 108 -159.83 -149.53
REMARK 500 CYS C 109 129.34 169.53
REMARK 500 LYS C 112 24.85 -70.79
REMARK 500 THR C 113 11.96 -147.20
REMARK 500 LYS C 121 30.99 -75.56
REMARK 500 ASN C 135 44.01 -85.45
REMARK 500 SER C 136 18.82 48.68
REMARK 500 LYS C 152 137.10 172.55
REMARK 500 SER C 154 89.71 -55.92
REMARK 500 LEU C 160 30.44 -71.72
REMARK 500 ALA C 163 -151.87 -72.35
REMARK 500 ASP C 164 -32.83 69.22
REMARK 500 ARG C 180 25.75 41.98
REMARK 500 THR C 186 118.38 -17.11
REMARK 500
REMARK 500 THIS ENTRY HAS 85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3V79 K 1873 2127 UNP P46531 NOTC1_HUMAN 1872 2126
DBREF 3V79 C 9 435 UNP Q06330 SUH_HUMAN 23 449
DBREF 3V79 M 13 74 UNP Q92585 MAML1_HUMAN 13 74
DBREF 3V79 X 0 17 PDB 3V79 3V79 0 17
DBREF 3V79 Y 101 118 PDB 3V79 3V79 101 118
DBREF 3V79 R 936 954 PDB 3V79 3V79 936 954
SEQADV 3V79 GLY K 1872 UNP P46531 EXPRESSION TAG
SEQADV 3V79 MET C 8 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 HIS C 436 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 HIS C 437 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 HIS C 438 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 HIS C 439 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 HIS C 440 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 HIS C 441 UNP Q06330 EXPRESSION TAG
SEQADV 3V79 GLY M 12 UNP Q92585 EXPRESSION TAG
SEQRES 1 K 256 GLY MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR
SEQRES 2 K 256 PRO LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU
SEQRES 3 K 256 THR GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL
SEQRES 4 K 256 ILE SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN
SEQRES 5 K 256 GLN THR ASP ARG THR GLY GLU THR ALA LEU HIS LEU ALA
SEQRES 6 K 256 ALA ARG TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU
SEQRES 7 K 256 GLU ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY
SEQRES 8 K 256 ARG THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN
SEQRES 9 K 256 GLY VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP
SEQRES 10 K 256 LEU ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE
SEQRES 11 K 256 LEU ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP
SEQRES 12 K 256 LEU ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP
SEQRES 13 K 256 LEU GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN
SEQRES 14 K 256 ASN VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA
SEQRES 15 K 256 ASN LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU
SEQRES 16 K 256 PHE LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS
SEQRES 17 K 256 VAL LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP
SEQRES 18 K 256 HIS MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG
SEQRES 19 K 256 MET HIS HIS ASP ILE VAL ARG LEU LEU ASP GLU TYR ASN
SEQRES 20 K 256 LEU VAL ARG SER PRO GLN LEU HIS GLY
SEQRES 1 C 434 MET GLY GLU ARG PRO PRO PRO LYS ARG LEU THR ARG GLU
SEQRES 2 C 434 ALA MET ARG ASN TYR LEU LYS GLU ARG GLY ASP GLN THR
SEQRES 3 C 434 VAL LEU ILE LEU HIS ALA LYS VAL ALA GLN LYS SER TYR
SEQRES 4 C 434 GLY ASN GLU LYS ARG PHE PHE CYS PRO PRO PRO CYS VAL
SEQRES 5 C 434 TYR LEU MET GLY SER GLY TRP LYS LYS LYS LYS GLU GLN
SEQRES 6 C 434 MET GLU ARG ASP GLY CYS SER GLU GLN GLU SER GLN PRO
SEQRES 7 C 434 CYS ALA PHE ILE GLY ILE GLY ASN SER ASP GLN GLU MET
SEQRES 8 C 434 GLN GLN LEU ASN LEU GLU GLY LYS ASN TYR CYS THR ALA
SEQRES 9 C 434 LYS THR LEU TYR ILE SER ASP SER ASP LYS ARG LYS HIS
SEQRES 10 C 434 PHE MET LEU SER VAL LYS MET PHE TYR GLY ASN SER ASP
SEQRES 11 C 434 ASP ILE GLY VAL PHE LEU SER LYS ARG ILE LYS VAL ILE
SEQRES 12 C 434 SER LYS PRO SER LYS LYS LYS GLN SER LEU LYS ASN ALA
SEQRES 13 C 434 ASP LEU CYS ILE ALA SER GLY THR LYS VAL ALA LEU PHE
SEQRES 14 C 434 ASN ARG LEU ARG SER GLN THR VAL SER THR ARG TYR LEU
SEQRES 15 C 434 HIS VAL GLU GLY GLY ASN PHE HIS ALA SER SER GLN GLN
SEQRES 16 C 434 TRP GLY ALA PHE PHE ILE HIS LEU LEU ASP ASP ASP GLU
SEQRES 17 C 434 SER GLU GLY GLU GLU PHE THR VAL ARG ASP GLY TYR ILE
SEQRES 18 C 434 HIS TYR GLY GLN THR VAL LYS LEU VAL CYS SER VAL THR
SEQRES 19 C 434 GLY MET ALA LEU PRO ARG LEU ILE ILE ARG LYS VAL ASP
SEQRES 20 C 434 LYS GLN THR ALA LEU LEU ASP ALA ASP ASP PRO VAL SER
SEQRES 21 C 434 GLN LEU HIS LYS CYS ALA PHE TYR LEU LYS ASP THR GLU
SEQRES 22 C 434 ARG MET TYR LEU CYS LEU SER GLN GLU ARG ILE ILE GLN
SEQRES 23 C 434 PHE GLN ALA THR PRO CYS PRO LYS GLU PRO ASN LYS GLU
SEQRES 24 C 434 MET ILE ASN ASP GLY ALA SER TRP THR ILE ILE SER THR
SEQRES 25 C 434 ASP LYS ALA GLU TYR THR PHE TYR GLU GLY MET GLY PRO
SEQRES 26 C 434 VAL LEU ALA PRO VAL THR PRO VAL PRO VAL VAL GLU SER
SEQRES 27 C 434 LEU GLN LEU ASN GLY GLY GLY ASP VAL ALA MET LEU GLU
SEQRES 28 C 434 LEU THR GLY GLN ASN PHE THR PRO ASN LEU ARG VAL TRP
SEQRES 29 C 434 PHE GLY ASP VAL GLU ALA GLU THR MET TYR ARG CYS GLY
SEQRES 30 C 434 GLU SER MET LEU CYS VAL VAL PRO ASP ILE SER ALA PHE
SEQRES 31 C 434 ARG GLU GLY TRP ARG TRP VAL ARG GLN PRO VAL GLN VAL
SEQRES 32 C 434 PRO VAL THR LEU VAL ARG ASN ASP GLY ILE ILE TYR SER
SEQRES 33 C 434 THR SER LEU THR PHE THR TYR THR PRO GLU PRO GLY HIS
SEQRES 34 C 434 HIS HIS HIS HIS HIS
SEQRES 1 M 63 GLY LEU PRO ARG HIS SER ALA VAL MET GLU ARG LEU ARG
SEQRES 2 M 63 ARG ARG ILE GLU LEU CYS ARG ARG HIS HIS SER THR CYS
SEQRES 3 M 63 GLU ALA ARG TYR GLU ALA VAL SER PRO GLU ARG LEU GLU
SEQRES 4 M 63 LEU GLU ARG GLN HIS THR PHE ALA LEU HIS GLN ARG CYS
SEQRES 5 M 63 ILE GLN ALA LYS ALA LYS ARG ALA GLY LYS HIS
SEQRES 1 X 18 DG DT DT DA DC DT DG DT DG DG DG DA DA
SEQRES 2 X 18 DA DG DA DA DA
SEQRES 1 Y 18 DT DT DT DC DT DT DT DC DC DC DA DC DA
SEQRES 2 Y 18 DG DT DA DA DC
SEQRES 1 R 19 LYS ARG ARG ARG GLN HIS GLY GLN LEU TRP PHE PRO GLU
SEQRES 2 R 19 GLY PHE LYS VAL SER GLU
HELIX 1 1 ILE K 1911 TYR K 1916 1 6
HELIX 2 2 THR K 1931 TYR K 1939 1 9
HELIX 3 3 ARG K 1941 ALA K 1951 1 11
HELIX 4 4 THR K 1964 ALA K 1972 1 9
HELIX 5 5 ALA K 1974 ARG K 1983 1 10
HELIX 6 6 THR K 1998 LEU K 2006 1 9
HELIX 7 7 GLY K 2010 SER K 2018 1 9
HELIX 8 8 SER K 2031 VAL K 2039 1 9
HELIX 9 9 ASN K 2041 ASN K 2051 1 11
HELIX 10 10 THR K 2064 GLY K 2073 1 10
HELIX 11 11 SER K 2074 HIS K 2084 1 11
HELIX 12 12 LEU K 2097 MET K 2106 1 10
HELIX 13 13 HIS K 2107 TYR K 2117 1 11
HELIX 14 14 THR C 18 GLU C 28 1 11
HELIX 15 15 SER C 64 ARG C 75 1 12
HELIX 16 16 GLY C 351 VAL C 354 5 4
HELIX 17 17 ASP C 393 PHE C 397 5 5
HELIX 18 18 SER M 17 LYS M 69 1 53
HELIX 19 19 PHE R 950 GLU R 954 5 5
SHEET 1 A 2 GLN C 32 ALA C 39 0
SHEET 2 A 2 THR C 319 PHE C 326 -1 O ASP C 320 N HIS C 38
SHEET 1 B 3 VAL C 41 GLN C 43 0
SHEET 2 B 3 ILE C 147 ILE C 150 1 O ILE C 150 N ALA C 42
SHEET 3 B 3 HIS C 124 PHE C 125 -1 N PHE C 125 O ILE C 147
SHEET 1 C 4 GLN C 99 GLN C 100 0
SHEET 2 C 4 CYS C 86 ILE C 91 -1 N ILE C 89 O GLN C 99
SHEET 3 C 4 LEU C 127 PHE C 132 -1 O SER C 128 N GLY C 90
SHEET 4 C 4 ASP C 138 LEU C 143 -1 O PHE C 142 N VAL C 129
SHEET 1 D 5 LYS C 172 VAL C 173 0
SHEET 2 D 5 PHE C 206 LEU C 211 -1 O PHE C 206 N VAL C 173
SHEET 3 D 5 THR C 233 CYS C 238 -1 O THR C 233 N LEU C 211
SHEET 4 D 5 LEU C 248 ASP C 254 -1 O LEU C 248 N VAL C 234
SHEET 5 D 5 CYS C 272 TYR C 275 -1 O TYR C 275 N ILE C 249
SHEET 1 E 6 LYS C 172 VAL C 173 0
SHEET 2 E 6 PHE C 206 LEU C 211 -1 O PHE C 206 N VAL C 173
SHEET 3 E 6 THR C 233 CYS C 238 -1 O THR C 233 N LEU C 211
SHEET 4 E 6 LEU C 248 ASP C 254 -1 O LEU C 248 N VAL C 234
SHEET 5 E 6 THR C 257 LEU C 259 -1 O LEU C 259 N LYS C 252
SHEET 6 E 6 LYS C 305 MET C 307 -1 O GLU C 306 N ALA C 258
SHEET 1 F 2 PHE C 176 ASN C 177 0
SHEET 2 F 2 ARG C 187 TYR C 188 -1 O ARG C 187 N ASN C 177
SHEET 1 G 2 VAL C 191 GLU C 192 0
SHEET 2 G 2 ASN C 195 PHE C 196 -1 O ASN C 195 N GLU C 192
SHEET 1 H 2 MET C 243 ALA C 244 0
SHEET 2 H 2 GLN R 943 LEU R 944 1 O GLN R 943 N ALA C 244
SHEET 1 I 2 LEU C 284 LEU C 286 0
SHEET 2 I 2 ILE C 291 GLN C 293 -1 O ILE C 292 N CYS C 285
SHEET 1 J 4 VAL C 342 ASN C 349 0
SHEET 2 J 4 MET C 356 GLN C 362 -1 O MET C 356 N ASN C 349
SHEET 3 J 4 SER C 386 VAL C 390 -1 O MET C 387 N LEU C 359
SHEET 4 J 4 THR C 379 CYS C 383 -1 N MET C 380 O LEU C 388
SHEET 1 K 4 VAL C 375 ALA C 377 0
SHEET 2 K 4 LEU C 368 PHE C 372 -1 N PHE C 372 O VAL C 375
SHEET 3 K 4 THR C 413 ARG C 416 -1 O VAL C 415 N ARG C 369
SHEET 4 K 4 ILE C 421 SER C 423 -1 O TYR C 422 N LEU C 414
SHEET 1 L 2 VAL C 408 GLN C 409 0
SHEET 2 L 2 THR C 429 TYR C 430 -1 O TYR C 430 N VAL C 408
CISPEP 1 CYS C 54 PRO C 55 0 0.04
CISPEP 2 THR C 338 PRO C 339 0 -0.10
CRYST1 272.646 272.646 119.987 90.00 90.00 120.00 P 63 2 2 12
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 0.003668 0.002118 0.000000 0.00000
SCALE2 0.000000 0.004235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008334 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
