HEADER CELL CYCLE,TRANSCRIPTION 25-FEB-05 1YYH
TITLE CRYSTAL STRUCTURE OF THE HUMAN NOTCH 1 ANKYRIN DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOTCH 1, ANKYRIN DOMAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ANKYRIN DOMAIN;
COMPND 5 SYNONYM: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; HN1;
COMPND 6 TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;
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: NOTCH1, TAN1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET41
KEYWDS ANKYRIN REPEATS; NOTCH 1, CELL CYCLE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.T.EHEBAUER,D.Y.CHIRGADZE,P.HAYWARD,A.MARTINEZ-ARIAS,T.L.BLUNDELL
REVDAT 5 23-AUG-23 1YYH 1 SEQADV
REVDAT 4 18-JUL-18 1YYH 1 REMARK
REVDAT 3 24-FEB-09 1YYH 1 VERSN
REVDAT 2 13-DEC-05 1YYH 1 JRNL
REVDAT 1 16-AUG-05 1YYH 0
JRNL AUTH M.T.EHEBAUER,D.Y.CHIRGADZE,P.HAYWARD,A.MARTINEZ-ARIAS,
JRNL AUTH 2 T.L.BLUNDELL
JRNL TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN NOTCH 1
JRNL TITL 2 ANKYRIN DOMAIN
JRNL REF BIOCHEM.J. V. 392 13 2005
JRNL REFN ISSN 0264-6021
JRNL PMID 16011479
JRNL DOI 10.1042/BJ20050515
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 42631
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2261
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3138
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 181
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2918
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 537
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72000
REMARK 3 B22 (A**2) : 0.72000
REMARK 3 B33 (A**2) : -1.08000
REMARK 3 B12 (A**2) : 0.36000
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): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.271
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2984 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4054 ; 1.425 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 380 ; 5.367 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 155 ;29.899 ;24.194
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 499 ;12.908 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;14.885 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 479 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2292 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1520 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2091 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 358 ; 0.197 ; 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): 40 ; 0.120 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.195 ; 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): 1974 ; 2.888 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3040 ; 3.487 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1112 ; 4.011 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1014 ; 5.779 ; 7.500
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 : 1.20
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 1YYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : DARESBURY
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44926
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 83.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.38500
REMARK 200 R SYM FOR SHELL (I) : 0.38500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1OT8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM HYDROGEN PHOSPHATE, SODIUM
REMARK 280 CHLORIDE, IMIDAZOLE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 72.66400
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 36.33200
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 54.49800
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 18.16600
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 90.83000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 1
REMARK 465 ASP A 2
REMARK 465 VAL A 3
REMARK 465 ASN A 4
REMARK 465 VAL A 5
REMARK 465 ARG A 6
REMARK 465 GLY A 7
REMARK 465 PRO A 8
REMARK 465 ASP A 9
REMARK 465 GLY A 10
REMARK 465 PHE A 11
REMARK 465 THR A 12
REMARK 465 PRO A 13
REMARK 465 LEU A 14
REMARK 465 MET A 15
REMARK 465 ILE A 16
REMARK 465 ALA A 17
REMARK 465 SER A 18
REMARK 465 CYS A 19
REMARK 465 SER A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 LEU A 24
REMARK 465 GLU A 25
REMARK 465 THR A 26
REMARK 465 GLY A 27
REMARK 465 ASN A 28
REMARK 465 SER A 29
REMARK 465 GLU A 30
REMARK 465 GLU A 31
REMARK 465 GLU A 32
REMARK 465 GLU A 33
REMARK 465 ASP A 34
REMARK 465 ALA A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 VAL A 38
REMARK 465 ILE A 39
REMARK 465 SER A 40
REMARK 465 ASP A 41
REMARK 465 PHE A 42
REMARK 465 ILE A 43
REMARK 465 TYR A 44
REMARK 465 GLN A 45
REMARK 465 GLY A 46
REMARK 465 ALA A 47
REMARK 465 SER A 48
REMARK 465 LEU A 49
REMARK 465 HIS A 50
REMARK 465 ASN A 51
REMARK 465 GLU A 245
REMARK 465 HIS A 246
REMARK 465 HIS A 247
REMARK 465 HIS A 248
REMARK 465 HIS A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 VAL B 3
REMARK 465 ASN B 4
REMARK 465 VAL B 5
REMARK 465 ARG B 6
REMARK 465 GLY B 7
REMARK 465 PRO B 8
REMARK 465 ASP B 9
REMARK 465 GLY B 10
REMARK 465 PHE B 11
REMARK 465 THR B 12
REMARK 465 PRO B 13
REMARK 465 LEU B 14
REMARK 465 MET B 15
REMARK 465 ILE B 16
REMARK 465 ALA B 17
REMARK 465 SER B 18
REMARK 465 CYS B 19
REMARK 465 SER B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 LEU B 24
REMARK 465 GLU B 25
REMARK 465 THR B 26
REMARK 465 GLY B 27
REMARK 465 ASN B 28
REMARK 465 SER B 29
REMARK 465 GLU B 30
REMARK 465 GLU B 31
REMARK 465 GLU B 32
REMARK 465 GLU B 33
REMARK 465 ASP B 34
REMARK 465 ALA B 35
REMARK 465 PRO B 36
REMARK 465 ALA B 37
REMARK 465 VAL B 38
REMARK 465 ILE B 39
REMARK 465 SER B 40
REMARK 465 ASP B 41
REMARK 465 PHE B 42
REMARK 465 ILE B 43
REMARK 465 TYR B 44
REMARK 465 GLN B 45
REMARK 465 GLY B 46
REMARK 465 ALA B 47
REMARK 465 SER B 48
REMARK 465 LEU B 49
REMARK 465 HIS B 50
REMARK 465 ASN B 51
REMARK 465 GLN B 52
REMARK 465 THR B 53
REMARK 465 ASP B 54
REMARK 465 LEU B 244
REMARK 465 GLU B 245
REMARK 465 HIS B 246
REMARK 465 HIS B 247
REMARK 465 HIS B 248
REMARK 465 HIS B 249
REMARK 465 HIS B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
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 52 CG CD OE1 NE2
REMARK 470 THR A 53 OG1 CG2
REMARK 470 ARG A 55 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 55 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 178 CG CD CE NZ
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 NE2 GLN B 103 O HOH B 482 1.47
REMARK 500 NH2 ARG B 75 O HOH B 464 2.02
REMARK 500 O HOH B 289 O HOH B 476 2.03
REMARK 500 O HOH A 435 O HOH A 535 2.05
REMARK 500 OE1 GLN A 103 O HOH A 450 2.08
REMARK 500 NH1 ARG B 75 O HOH B 463 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 381 O HOH B 504 2654 2.11
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 ASP B 237 CB - CG - OD1 ANGL. DEV. = 6.2 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 ASP A 54 -157.98 -90.41
REMARK 500 ASP A 87 -169.90 -77.19
REMARK 500 HIS A 147 25.34 80.84
REMARK 500 HIS B 147 24.21 83.69
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YYH A 1 243 UNP P46531 NOTC1_HUMAN 1873 2115
DBREF 1YYH B 1 243 UNP P46531 NOTC1_HUMAN 1873 2115
SEQADV 1YYH LEU A 244 UNP P46531 EXPRESSION TAG
SEQADV 1YYH GLU A 245 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 246 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 247 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 248 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 249 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 250 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 251 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 252 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS A 253 UNP P46531 EXPRESSION TAG
SEQADV 1YYH LEU B 244 UNP P46531 EXPRESSION TAG
SEQADV 1YYH GLU B 245 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 246 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 247 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 248 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 249 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 250 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 251 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 252 UNP P46531 EXPRESSION TAG
SEQADV 1YYH HIS B 253 UNP P46531 EXPRESSION TAG
SEQRES 1 A 253 MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR PRO
SEQRES 2 A 253 LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU THR
SEQRES 3 A 253 GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL ILE
SEQRES 4 A 253 SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN GLN
SEQRES 5 A 253 THR ASP ARG THR GLY GLU THR ALA LEU HIS LEU ALA ALA
SEQRES 6 A 253 ARG TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU GLU
SEQRES 7 A 253 ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY ARG
SEQRES 8 A 253 THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN GLY
SEQRES 9 A 253 VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP LEU
SEQRES 10 A 253 ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE LEU
SEQRES 11 A 253 ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP LEU
SEQRES 12 A 253 ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP LEU
SEQRES 13 A 253 GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN ASN
SEQRES 14 A 253 VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA ASN
SEQRES 15 A 253 LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU PHE
SEQRES 16 A 253 LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS VAL
SEQRES 17 A 253 LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP HIS
SEQRES 18 A 253 MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG MET
SEQRES 19 A 253 HIS HIS ASP ILE VAL ARG LEU LEU ASP LEU GLU HIS HIS
SEQRES 20 A 253 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 253 MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR PRO
SEQRES 2 B 253 LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU THR
SEQRES 3 B 253 GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL ILE
SEQRES 4 B 253 SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN GLN
SEQRES 5 B 253 THR ASP ARG THR GLY GLU THR ALA LEU HIS LEU ALA ALA
SEQRES 6 B 253 ARG TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU GLU
SEQRES 7 B 253 ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY ARG
SEQRES 8 B 253 THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN GLY
SEQRES 9 B 253 VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP LEU
SEQRES 10 B 253 ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE LEU
SEQRES 11 B 253 ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP LEU
SEQRES 12 B 253 ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP LEU
SEQRES 13 B 253 GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN ASN
SEQRES 14 B 253 VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA ASN
SEQRES 15 B 253 LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU PHE
SEQRES 16 B 253 LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS VAL
SEQRES 17 B 253 LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP HIS
SEQRES 18 B 253 MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG MET
SEQRES 19 B 253 HIS HIS ASP ILE VAL ARG LEU LEU ASP LEU GLU HIS HIS
SEQRES 20 B 253 HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *537(H2 O)
HELIX 1 1 THR A 59 TYR A 67 1 9
HELIX 2 2 ARG A 69 ALA A 79 1 11
HELIX 3 3 THR A 92 ASP A 101 1 10
HELIX 4 4 ALA A 102 ASN A 112 1 11
HELIX 5 5 THR A 126 ALA A 135 1 10
HELIX 6 6 GLY A 138 SER A 146 1 9
HELIX 7 7 SER A 159 ASN A 168 1 10
HELIX 8 8 ASN A 169 ASN A 179 1 11
HELIX 9 9 THR A 192 GLY A 201 1 10
HELIX 10 10 SER A 202 HIS A 212 1 11
HELIX 11 11 LEU A 225 ARG A 233 1 9
HELIX 12 12 HIS A 235 LEU A 244 1 10
HELIX 13 13 THR B 59 TYR B 67 1 9
HELIX 14 14 ARG B 69 ALA B 79 1 11
HELIX 15 15 THR B 92 ASP B 101 1 10
HELIX 16 16 ALA B 102 ASN B 112 1 11
HELIX 17 17 THR B 126 ALA B 135 1 10
HELIX 18 18 GLY B 138 SER B 146 1 9
HELIX 19 19 SER B 159 ASN B 168 1 10
HELIX 20 20 ASN B 169 ASN B 179 1 11
HELIX 21 21 THR B 192 GLY B 201 1 10
HELIX 22 22 SER B 202 HIS B 212 1 11
HELIX 23 23 LEU B 225 ARG B 233 1 9
HELIX 24 24 HIS B 235 ASP B 243 1 9
CRYST1 96.840 96.840 108.996 90.00 90.00 120.00 P 65 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 0.010326 0.005962 0.000000 0.00000
SCALE2 0.000000 0.011924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009175 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
