HEADER TRANSFERASE 21-JUL-16 5KY8
TITLE MOUSE POFUT1 IN COMPLEX WITH O-GLUCOSYLATED MOUSE NOTCH1 EGF12 MUTANT
TITLE 2 (D464G) AND GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GDP-FUCOSE PROTEIN O-FUCOSYLTRANSFERASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PEPTIDE-O-FUCOSYLTRANSFERASE 1,O-FUCT-1;
COMPND 5 EC: 2.4.1.221;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: NOTCH 1,MOTCH A,MT14,P300;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: POFUT1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PB-T-PAF;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 GENE: NOTCH1, MOTCH;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LI,J.M.RINI
REVDAT 4 29-JUL-20 5KY8 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 28-JUN-17 5KY8 1 JRNL
REVDAT 2 31-MAY-17 5KY8 1 JRNL
REVDAT 1 17-MAY-17 5KY8 0
JRNL AUTH Z.LI,K.HAN,J.E.PAK,M.SATKUNARAJAH,D.ZHOU,J.M.RINI
JRNL TITL RECOGNITION OF EGF-LIKE DOMAINS BY THE NOTCH-MODIFYING
JRNL TITL 2 O-FUCOSYLTRANSFERASE POFUT1.
JRNL REF NAT. CHEM. BIOL. V. 13 757 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 28530709
JRNL DOI 10.1038/NCHEMBIO.2381
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 44211
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2225
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.4384 - 4.1568 0.97 2757 133 0.1630 0.1822
REMARK 3 2 4.1568 - 3.2997 0.98 2622 159 0.1580 0.1682
REMARK 3 3 3.2997 - 2.8826 0.98 2637 139 0.1837 0.2214
REMARK 3 4 2.8826 - 2.6191 0.99 2606 152 0.1922 0.2027
REMARK 3 5 2.6191 - 2.4314 0.99 2629 148 0.1927 0.2220
REMARK 3 6 2.4314 - 2.2880 0.99 2616 154 0.1986 0.2319
REMARK 3 7 2.2880 - 2.1735 1.00 2628 145 0.1990 0.2271
REMARK 3 8 2.1735 - 2.0788 1.00 2628 116 0.2069 0.2338
REMARK 3 9 2.0788 - 1.9988 1.00 2607 138 0.2160 0.2295
REMARK 3 10 1.9988 - 1.9298 1.00 2638 123 0.2294 0.2559
REMARK 3 11 1.9298 - 1.8695 1.00 2636 131 0.2389 0.2642
REMARK 3 12 1.8695 - 1.8161 1.00 2602 143 0.2526 0.2973
REMARK 3 13 1.8161 - 1.7682 1.00 2605 127 0.2734 0.3260
REMARK 3 14 1.7682 - 1.7251 1.00 2600 136 0.2867 0.2834
REMARK 3 15 1.7251 - 1.6859 1.00 2630 138 0.3128 0.3360
REMARK 3 16 1.6859 - 1.6500 0.99 2545 143 0.3360 0.3654
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.15
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3224
REMARK 3 ANGLE : 0.776 4402
REMARK 3 CHIRALITY : 0.046 471
REMARK 3 PLANARITY : 0.005 565
REMARK 3 DIHEDRAL : 15.714 1904
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9828 39.1978 22.5978
REMARK 3 T TENSOR
REMARK 3 T11: 0.2576 T22: 0.3462
REMARK 3 T33: 0.1943 T12: -0.0235
REMARK 3 T13: 0.0287 T23: -0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 1.4151 L22: 2.7063
REMARK 3 L33: 1.9433 L12: -0.1159
REMARK 3 L13: -0.2674 L23: 0.8173
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: -0.5020 S13: 0.0333
REMARK 3 S21: 0.2274 S22: -0.1409 S23: 0.2231
REMARK 3 S31: 0.0877 S32: 0.1171 S33: 0.1463
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 234 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4240 45.8454 18.7842
REMARK 3 T TENSOR
REMARK 3 T11: 0.2547 T22: 0.2634
REMARK 3 T33: 0.1685 T12: -0.0433
REMARK 3 T13: 0.0050 T23: -0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 2.2677 L22: 3.1062
REMARK 3 L33: 1.3670 L12: -0.2719
REMARK 3 L13: -0.4509 L23: 0.7816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0069 S12: -0.3124 S13: 0.2668
REMARK 3 S21: 0.0614 S22: 0.0050 S23: 0.0020
REMARK 3 S31: -0.2072 S32: 0.1447 S33: 0.0285
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 235 THROUGH 384 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7623 21.1268 3.8743
REMARK 3 T TENSOR
REMARK 3 T11: 0.1969 T22: 0.1643
REMARK 3 T33: 0.3097 T12: -0.0005
REMARK 3 T13: 0.0359 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 4.3843 L22: 3.2658
REMARK 3 L33: 2.3200 L12: -0.7265
REMARK 3 L13: -1.6673 L23: 1.2215
REMARK 3 S TENSOR
REMARK 3 S11: -0.2255 S12: 0.1538 S13: -0.7375
REMARK 3 S21: -0.0402 S22: -0.1005 S23: 0.1193
REMARK 3 S31: 0.0888 S32: 0.0052 S33: 0.0741
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 453 THROUGH 458 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7130 50.4926 5.6616
REMARK 3 T TENSOR
REMARK 3 T11: 0.5588 T22: 0.3704
REMARK 3 T33: 0.8051 T12: -0.1161
REMARK 3 T13: 0.1340 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 7.0643 L22: 1.2404
REMARK 3 L33: 6.4246 L12: 2.9135
REMARK 3 L13: -5.0543 L23: -2.4064
REMARK 3 S TENSOR
REMARK 3 S11: 0.3589 S12: -0.2625 S13: 0.7923
REMARK 3 S21: -1.1214 S22: -0.1862 S23: -1.7609
REMARK 3 S31: -1.2185 S32: 1.1264 S33: -0.1306
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 459 THROUGH 477 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2840 44.9278 1.7021
REMARK 3 T TENSOR
REMARK 3 T11: 0.5017 T22: 0.3321
REMARK 3 T33: 0.4858 T12: 0.0631
REMARK 3 T13: 0.0486 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 5.3417 L22: 1.9455
REMARK 3 L33: 5.5155 L12: -2.5545
REMARK 3 L13: -1.8716 L23: 0.6247
REMARK 3 S TENSOR
REMARK 3 S11: 0.5367 S12: 0.1690 S13: 0.9318
REMARK 3 S21: -0.8126 S22: -0.5386 S23: -0.2289
REMARK 3 S31: -0.6236 S32: 0.0320 S33: -0.0375
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 478 THROUGH 491 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8576 41.6919 -1.6326
REMARK 3 T TENSOR
REMARK 3 T11: 0.6126 T22: 0.6035
REMARK 3 T33: 0.5775 T12: 0.0618
REMARK 3 T13: -0.2836 T23: -0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 4.5726 L22: 2.7036
REMARK 3 L33: 7.1139 L12: -0.7536
REMARK 3 L13: -0.7659 L23: -1.9902
REMARK 3 S TENSOR
REMARK 3 S11: -0.4258 S12: 1.0144 S13: 0.4953
REMARK 3 S21: -1.3869 S22: 0.1007 S23: 1.5207
REMARK 3 S31: -0.4185 S32: -1.2459 S33: 0.2032
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5KY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-13
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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44218
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 1.12700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.330
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG2000 MME, 50 MM TRIS PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 25.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.41500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.41500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.95000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 GLY A 30
REMARK 465 ALA A 31
REMARK 465 PRO A 32
REMARK 465 ASP B 452
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 SER A 33 OG
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 LYS A 166 CG CD CE NZ
REMARK 470 GLU A 181 CG CD OE1 OE2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 LYS A 251 CG CD CE NZ
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 ASP A 259 CG OD1 OD2
REMARK 470 LYS A 293 CG CD CE NZ
REMARK 470 GLN A 326 CG CD OE1 NE2
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 ASP A 330 CG OD1 OD2
REMARK 470 LYS A 331 CG CD CE NZ
REMARK 470 ARG A 333 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 453 CG1 CG2
REMARK 470 GLN B 470 CG CD OE1 NE2
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 VAL A 273 HG1 THR A 279 1.57
REMARK 500 OD2 ASP A 141 H LYS A 143 1.58
REMARK 500 O HOH A 683 O HOH A 724 2.19
REMARK 500 ND2 ASN A 67 O5 NAG A 401 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS A 272 CA - CB - SG ANGL. DEV. = 6.8 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 ILE A 246 13.34 -141.39
REMARK 500 MET A 267 -116.82 46.68
REMARK 500 SER A 317 -118.75 -154.98
REMARK 500 ASP A 330 -3.18 93.96
REMARK 500 MET A 383 85.60 -154.01
REMARK 500 GLU B 473 -177.12 -176.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KXH RELATED DB: PDB
REMARK 900 RELATED ID: 5KXQ RELATED DB: PDB
REMARK 900 RELATED ID: 5KY0 RELATED DB: PDB
REMARK 900 RELATED ID: 5KY2 RELATED DB: PDB
REMARK 900 RELATED ID: 5KY3 RELATED DB: PDB
REMARK 900 RELATED ID: 5KY4 RELATED DB: PDB
REMARK 900 RELATED ID: 5KY5 RELATED DB: PDB
REMARK 900 RELATED ID: 5KY7 RELATED DB: PDB
REMARK 900 RELATED ID: 5KY9 RELATED DB: PDB
DBREF 5KY8 A 33 384 UNP Q91ZW2 OFUT1_MOUSE 33 384
DBREF 5KY8 B 452 491 UNP Q01705 NOTC1_MOUSE 452 491
SEQADV 5KY8 GLY A 30 UNP Q91ZW2 EXPRESSION TAG
SEQADV 5KY8 ALA A 31 UNP Q91ZW2 EXPRESSION TAG
SEQADV 5KY8 PRO A 32 UNP Q91ZW2 EXPRESSION TAG
SEQADV 5KY8 GLY B 464 UNP Q01705 ASP 464 ENGINEERED MUTATION
SEQRES 1 A 355 GLY ALA PRO SER TRP ASP LEU ALA GLY TYR LEU LEU TYR
SEQRES 2 A 355 CYS PRO CYS MET GLY ARG PHE GLY ASN GLN ALA ASP HIS
SEQRES 3 A 355 PHE LEU GLY SER LEU ALA PHE ALA LYS LEU LEU ASN ARG
SEQRES 4 A 355 THR LEU ALA VAL PRO PRO TRP ILE GLU TYR GLN HIS HIS
SEQRES 5 A 355 LYS PRO PRO PHE THR ASN LEU HIS VAL SER TYR GLN LYS
SEQRES 6 A 355 TYR PHE LYS LEU GLU PRO LEU GLN ALA TYR HIS ARG VAL
SEQRES 7 A 355 VAL SER LEU GLU ASP PHE MET GLU ASN LEU ALA PRO SER
SEQRES 8 A 355 HIS TRP PRO PRO GLU LYS ARG VAL ALA TYR CYS PHE GLU
SEQRES 9 A 355 VAL ALA ALA GLN ARG SER PRO ASP LYS LYS THR CYS PRO
SEQRES 10 A 355 MET LYS GLU GLY ASN PRO PHE GLY PRO PHE TRP ASP GLN
SEQRES 11 A 355 PHE HIS VAL SER PHE ASN LYS SER GLU LEU PHE THR GLY
SEQRES 12 A 355 ILE SER PHE SER ALA SER TYR LYS GLU GLN TRP THR GLN
SEQRES 13 A 355 ARG PHE PRO ALA LYS GLU HIS PRO VAL LEU ALA LEU PRO
SEQRES 14 A 355 GLY ALA PRO ALA GLN PHE PRO VAL LEU GLU GLU HIS ARG
SEQRES 15 A 355 GLU LEU GLN LYS TYR MET VAL TRP SER ASP GLU MET VAL
SEQRES 16 A 355 ARG THR GLY GLU ALA LEU ILE SER ALA HIS LEU VAL ARG
SEQRES 17 A 355 PRO TYR VAL GLY ILE HIS LEU ARG ILE GLY SER ASP TRP
SEQRES 18 A 355 LYS ASN ALA CYS ALA MET LEU LYS ASP GLY THR ALA GLY
SEQRES 19 A 355 SER HIS PHE MET ALA SER PRO GLN CYS VAL GLY TYR SER
SEQRES 20 A 355 ARG SER THR ALA THR PRO LEU THR MET THR MET CYS LEU
SEQRES 21 A 355 PRO ASP LEU LYS GLU ILE GLN ARG ALA VAL THR LEU TRP
SEQRES 22 A 355 VAL ARG ALA LEU ASN ALA ARG SER VAL TYR ILE ALA THR
SEQRES 23 A 355 ASP SER GLU SER TYR VAL SER GLU ILE GLN GLN LEU PHE
SEQRES 24 A 355 LYS ASP LYS VAL ARG VAL VAL SER LEU LYS PRO GLU VAL
SEQRES 25 A 355 ALA GLN ILE ASP LEU TYR ILE LEU GLY GLN ALA ASP HIS
SEQRES 26 A 355 PHE ILE GLY ASN CYS VAL SER SER PHE THR ALA PHE VAL
SEQRES 27 A 355 LYS ARG GLU ARG ASP LEU HIS GLY ARG GLN SER SER PHE
SEQRES 28 A 355 PHE GLY MET ASP
SEQRES 1 B 40 ASP VAL ASN GLU CYS ILE SER ASN PRO CYS GLN ASN GLY
SEQRES 2 B 40 ALA THR CYS LEU ASP GLN ILE GLY GLU PHE GLN CYS ILE
SEQRES 3 B 40 CYS MET PRO GLY TYR GLU GLY VAL TYR CYS GLU ILE ASN
SEQRES 4 B 40 THR
HET NAG A 401 28
HET GDP A 402 38
HET BGC B1001 21
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM BGC BETA-D-GLUCOPYRANOSE
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 GDP C10 H15 N5 O11 P2
FORMUL 5 BGC C6 H12 O6
FORMUL 6 HOH *271(H2 O)
HELIX 1 AA1 ARG A 48 ASN A 67 1 20
HELIX 2 AA2 SER A 91 PHE A 96 1 6
HELIX 3 AA3 LEU A 98 TYR A 104 5 7
HELIX 4 AA4 LEU A 110 LEU A 117 1 8
HELIX 5 AA5 LEU A 117 TRP A 122 1 6
HELIX 6 AA6 PRO A 123 LYS A 126 5 4
HELIX 7 AA7 GLU A 133 GLN A 137 1 5
HELIX 8 AA8 PRO A 152 GLN A 159 1 8
HELIX 9 AA9 SER A 176 SER A 178 5 3
HELIX 10 AB1 TYR A 179 PHE A 187 1 9
HELIX 11 AB2 LEU A 207 MET A 217 5 11
HELIX 12 AB3 SER A 220 LEU A 235 1 16
HELIX 13 AB4 GLY A 247 ASP A 259 1 13
HELIX 14 AB5 SER A 269 GLY A 274 1 6
HELIX 15 AB6 THR A 284 LEU A 289 1 6
HELIX 16 AB7 ASP A 291 ASN A 307 1 17
HELIX 17 AB8 TYR A 320 GLN A 326 1 7
HELIX 18 AB9 VAL A 341 GLN A 351 1 11
HELIX 19 AC1 SER A 361 HIS A 374 1 14
HELIX 20 AC2 ASN B 454 ASN B 459 5 6
SHEET 1 AA1 4 VAL A 107 SER A 109 0
SHEET 2 AA1 4 THR A 69 VAL A 72 1 N LEU A 70 O VAL A 108
SHEET 3 AA1 4 TYR A 39 TYR A 42 1 N LEU A 40 O ALA A 71
SHEET 4 AA1 4 VAL A 194 LEU A 197 1 O LEU A 195 N LEU A 41
SHEET 1 AA2 2 TRP A 75 GLU A 77 0
SHEET 2 AA2 2 LEU A 88 VAL A 90 -1 O LEU A 88 N GLU A 77
SHEET 1 AA3 2 VAL A 128 PHE A 132 0
SHEET 2 AA3 2 LYS A 166 PHE A 170 1 O GLU A 168 N ALA A 129
SHEET 1 AA4 5 ARG A 333 SER A 336 0
SHEET 2 AA4 5 SER A 310 THR A 315 1 N VAL A 311 O VAL A 335
SHEET 3 AA4 5 TYR A 239 LEU A 244 1 N LEU A 244 O ALA A 314
SHEET 4 AA4 5 HIS A 354 GLY A 357 1 O HIS A 354 N GLY A 241
SHEET 5 AA4 5 SER A 378 PHE A 380 1 O SER A 379 N PHE A 355
SHEET 1 AA5 2 THR B 466 ASP B 469 0
SHEET 2 AA5 2 PHE B 474 ILE B 477 -1 O ILE B 477 N THR B 466
SHEET 1 AA6 2 TYR B 482 GLU B 483 0
SHEET 2 AA6 2 ILE B 489 ASN B 490 -1 O ILE B 489 N GLU B 483
SSBOND 1 CYS A 43 CYS A 45 1555 1555 2.04
SSBOND 2 CYS A 131 CYS A 145 1555 1555 2.03
SSBOND 3 CYS A 254 CYS A 288 1555 1555 2.03
SSBOND 4 CYS A 272 CYS A 359 1555 1555 2.05
SSBOND 5 CYS B 456 CYS B 467 1555 1555 1.92
SSBOND 6 CYS B 461 CYS B 476 1555 1555 2.03
SSBOND 7 CYS B 478 CYS B 487 1555 1555 2.03
LINK ND2 ASN A 67 C1 NAG A 401 1555 1555 1.40
LINK OG SER B 458 C1 BGC B1001 1555 1555 1.48
CISPEP 1 PRO A 83 PRO A 84 0 4.02
CISPEP 2 ASN A 151 PRO A 152 0 4.99
CISPEP 3 PHE A 204 PRO A 205 0 -1.92
CISPEP 4 ARG A 237 PRO A 238 0 -2.00
CRYST1 51.540 65.900 106.830 90.00 90.00 90.00 P 21 21 21 4
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 0.019402 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009361 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
