HEADER SIGNALING PROTEIN 21-JUN-06 2HE0
TITLE CRYSTAL STRUCTURE OF A HUMAN NOTCH1 ANKYRIN DOMAIN MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOTCH1 PREPROPROTEIN VARIANT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ANKYRIN DOMAIN, RESIDUES 1873-2115;
COMPND 5 SYNONYM: HUMAN NOTCH ANKYRIN DOMAIN MUTANT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOTCH 1;
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: PET41A
KEYWDS NOTCH, ANKYRIN, SIGNALLING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.GUPTA,M.T.EHEBAUER,D.Y.CHIRGADZE,A.MARTINEZ ARIAS,T.L.BLUNDELL
REVDAT 4 30-AUG-23 2HE0 1 REMARK
REVDAT 3 20-OCT-21 2HE0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2HE0 1 VERSN
REVDAT 1 04-JUL-06 2HE0 0
JRNL AUTH D.GUPTA,M.T.EHEBAUER,D.Y.CHIRGADZE,A.MARTINEZ ARIAS,
JRNL AUTH 2 T.L.BLUNDELL
JRNL TITL CRYSTAL STRUCTURE OF A HUMAN NOTCH1 ANKYRIN DOMAIN MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 48.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 43201
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2297
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) : 3161
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2940
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 416
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.961
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3017 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4107 ; 1.491 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 398 ; 5.659 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;29.112 ;24.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 489 ;13.524 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;19.929 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 484 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2328 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1572 ; 0.232 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2105 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 319 ; 0.237 ; 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 ; 0.325 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 41 ; 0.338 ; 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): 2013 ; 3.341 ; 5.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3102 ; 3.973 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1103 ; 4.329 ; 5.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1001 ; 5.677 ; 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 2HE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9769
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45547
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : 0.48800
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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1YYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.55M SODIUM/POTASSIUM TARTRATE, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 72.47933
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 36.23967
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 54.35950
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 18.11983
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 90.59917
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 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 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 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 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 ARG A 69 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 52 CB CG CD OE1 NE2
REMARK 470 THR B 53 OG1 CG2
REMARK 470 ARG B 55 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 LYS B 178 CG CD CE NZ
REMARK 470 LYS B 207 CG CD CE NZ
REMARK 470 LEU B 244 CB CG CD1 CD2
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 O LEU A 140 O HOH A 698 1.58
REMARK 500 NE2 GLN A 103 O HOH A 640 1.68
REMARK 500 O MET B 185 O HOH B 351 1.71
REMARK 500 OD2 ASP A 237 O HOH A 662 1.72
REMARK 500 OE1 GLN A 103 O HOH A 641 1.73
REMARK 500 N ILE A 144 O HOH A 698 1.74
REMARK 500 OE1 GLN B 103 O HOH B 339 1.91
REMARK 500 O HOH A 731 O HOH A 749 2.04
REMARK 500 O HOH A 661 O HOH A 662 2.07
REMARK 500 CA THR B 192 O HOH B 351 2.11
REMARK 500 O HOH A 675 O HOH A 755 2.12
REMARK 500 O HOH A 639 O HOH A 733 2.12
REMARK 500 CD1 LEU B 196 O HOH B 416 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 752 O HOH B 359 2555 1.64
REMARK 500 CB ARG B 69 O HOH A 662 2454 2.19
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 HIS A 147 25.83 84.12
REMARK 500 ASP A 154 -166.37 -75.01
REMARK 500 ASP B 54 -153.98 -107.21
REMARK 500 HIS B 147 27.76 83.48
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 EDO A 510
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YYH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE WILD TYPE HUMAN NOTCH 1 ANKYRIN DOMAIN
DBREF 2HE0 A 1 243 UNP P46531 NOTC1_HUMAN 1873 2115
DBREF 2HE0 B 1 243 UNP P46531 NOTC1_HUMAN 1873 2115
SEQADV 2HE0 ALA A 58 UNP P46531 GLU 1930 ENGINEERED MUTATION
SEQADV 2HE0 ALA A 66 UNP P46531 ARG 1938 ENGINEERED MUTATION
SEQADV 2HE0 LEU A 244 UNP P46531 CLONING ARTIFACT
SEQADV 2HE0 GLU A 245 UNP P46531 CLONING ARTIFACT
SEQADV 2HE0 HIS A 246 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 247 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 248 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 249 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 250 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 251 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 252 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS A 253 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 ALA B 58 UNP P46531 GLU 1930 ENGINEERED MUTATION
SEQADV 2HE0 ALA B 66 UNP P46531 ARG 1938 ENGINEERED MUTATION
SEQADV 2HE0 LEU B 244 UNP P46531 CLONING ARTIFACT
SEQADV 2HE0 GLU B 245 UNP P46531 CLONING ARTIFACT
SEQADV 2HE0 HIS B 246 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS B 247 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS B 248 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS B 249 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS B 250 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS B 251 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 HIS B 252 UNP P46531 EXPRESSION TAG
SEQADV 2HE0 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 ALA THR ALA LEU HIS LEU ALA ALA
SEQRES 6 A 253 ALA 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 ALA THR ALA LEU HIS LEU ALA ALA
SEQRES 6 B 253 ALA 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
HET EDO A 510 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *416(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 ALA A 100 1 9
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 ALA B 100 1 9
HELIX 16 16 ALA B 102 ARG B 111 1 10
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
CISPEP 1 GLN B 52 THR B 53 0 5.29
SITE 1 AC1 7 ARG A 120 MET A 121 HIS A 122 GLY A 124
SITE 2 AC1 7 ASP A 155 HOH A 585 HOH A 747
CRYST1 96.982 96.982 108.719 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 0.010311 0.005953 0.000000 0.00000
SCALE2 0.000000 0.011906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
