HEADER RNA BINDING PROTEIN 18-JUL-09 3ICQ
TITLE KARYOPHERIN NUCLEAR STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXPORTIN-T;
COMPND 3 CHAIN: T, U;
COMPND 4 SYNONYM: TRNA EXPORTIN, EXPORTIN(TRNA), KARYOPHERIN-BETA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GTP-BINDING NUCLEAR PROTEIN GSP1/CNR1;
COMPND 8 CHAIN: B, C;
COMPND 9 FRAGMENT: RAN, UNP RESIDUES 9-179;
COMPND 10 SYNONYM: GTPASE RAN HOMOLOG, GENETIC SUPPRESSOR OF PRP20-1,
COMPND 11 CHROMOSOME STABILITY PROTEIN 17;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: RNA (62-MER);
COMPND 16 CHAIN: D, E;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 4896;
SOURCE 5 GENE: LOS1, SPBP8B7.09C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: CNR1, CST17, GSP1, L8003.19, YLR293C;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: DL-41;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTB;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: NUCLEOTIDE SYNTHESIS
KEYWDS KARYOPHERIN, EXPORTIN, HEAT REPEAT, TRNA, GTPASE, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.G.COOK,N.FUKUHARA,M.JINEK,E.CONTI
REVDAT 4 01-NOV-23 3ICQ 1 REMARK
REVDAT 3 10-NOV-21 3ICQ 1 REMARK DBREF SEQADV LINK
REVDAT 2 15-SEP-09 3ICQ 1 JRNL
REVDAT 1 25-AUG-09 3ICQ 0
JRNL AUTH A.G.COOK,N.FUKUHARA,M.JINEK,E.CONTI
JRNL TITL STRUCTURES OF THE TRNA EXPORT FACTOR IN THE NUCLEAR AND
JRNL TITL 2 CYTOSOLIC STATES
JRNL REF NATURE V. 461 60 2009
JRNL REFN ISSN 0028-0836
JRNL PMID 19680239
JRNL DOI 10.1038/NATURE08394
REMARK 2
REMARK 2 RESOLUTION. 3.20 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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 57375
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 SET) : 0.243
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2914
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 : 16422
REMARK 3 NUCLEIC ACID ATOMS : 2633
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.15100
REMARK 3 B22 (A**2) : -0.58600
REMARK 3 B33 (A**2) : -6.56400
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.407
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 50.59
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : GTP.PARAM
REMARK 3 PARAMETER FILE 5 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ICQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054247.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.070
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57452
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 72.174
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : 0.14900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : 0.65000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.3
REMARK 200 STARTING MODEL: PDB ENTRY 3IBV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS, PH5.5, 20% PEG3350,
REMARK 280 180MM SODIUM ACETATE AT 18 DEGREES, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 71.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 71.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 71.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 71.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, B, D
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, C, 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 GLY T -1
REMARK 465 PRO T 0
REMARK 465 MET T 1
REMARK 465 GLN T 283
REMARK 465 GLU T 284
REMARK 465 GLN T 285
REMARK 465 GLN T 569
REMARK 465 VAL T 570
REMARK 465 GLY T 685
REMARK 465 SER T 686
REMARK 465 GLY T 851
REMARK 465 GLU T 852
REMARK 465 PRO T 897
REMARK 465 ASN T 898
REMARK 465 PHE T 899
REMARK 465 ASN T 900
REMARK 465 THR T 901
REMARK 465 ARG T 902
REMARK 465 ASP T 903
REMARK 465 GLY T 904
REMARK 465 LYS T 923
REMARK 465 LEU T 924
REMARK 465 GLY T 925
REMARK 465 ASP T 926
REMARK 465 ILE T 927
REMARK 465 TYR T 928
REMARK 465 LYS T 929
REMARK 465 ASP T 958
REMARK 465 GLY T 976
REMARK 465 ASN T 977
REMARK 465 VAL T 978
REMARK 465 GLU B 9
REMARK 465 VAL B 10
REMARK 465 PHE B 178
REMARK 465 VAL B 179
REMARK 465 C D 37
REMARK 465 U D 38
REMARK 465 U D 39
REMARK 465 C D 40
REMARK 465 G D 41
REMARK 465 GLY U -1
REMARK 465 PRO U 0
REMARK 465 MET U 1
REMARK 465 ASP U 15
REMARK 465 PRO U 16
REMARK 465 SER U 17
REMARK 465 VAL U 18
REMARK 465 GLN U 283
REMARK 465 GLU U 284
REMARK 465 GLN U 285
REMARK 465 GLY U 851
REMARK 465 GLU U 852
REMARK 465 ASP U 874
REMARK 465 GLY U 875
REMARK 465 ILE U 876
REMARK 465 ALA U 877
REMARK 465 PHE U 899
REMARK 465 ASN U 900
REMARK 465 THR U 901
REMARK 465 ARG U 902
REMARK 465 ASP U 903
REMARK 465 GLY U 904
REMARK 465 GLY U 925
REMARK 465 ASP U 926
REMARK 465 ILE U 927
REMARK 465 ASN U 941
REMARK 465 PHE U 942
REMARK 465 PRO U 943
REMARK 465 ASP U 944
REMARK 465 VAL U 945
REMARK 465 MET U 946
REMARK 465 ALA U 947
REMARK 465 ASN U 956
REMARK 465 LEU U 957
REMARK 465 GLY U 976
REMARK 465 ASN U 977
REMARK 465 VAL U 978
REMARK 465 GLU C 9
REMARK 465 VAL C 10
REMARK 465 THR C 56
REMARK 465 ASN C 57
REMARK 465 PHE C 58
REMARK 465 GLY C 59
REMARK 465 PHE C 178
REMARK 465 VAL C 179
REMARK 465 U E 38
REMARK 465 U E 39
REMARK 465 C E 40
REMARK 465 G E 41
REMARK 465 G E 42
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 T 2 OG
REMARK 470 GLN T 4 CG CD OE1 NE2
REMARK 470 GLU T 11 CG CD OE1 OE2
REMARK 470 LEU T 14 CG CD1 CD2
REMARK 470 SER T 17 OG
REMARK 470 ILE T 21 CG1 CG2 CD1
REMARK 470 LYS T 23 CG CD CE NZ
REMARK 470 GLN T 24 CG CD OE1 NE2
REMARK 470 GLN T 25 CG CD OE1 NE2
REMARK 470 LYS T 41 CG CD CE NZ
REMARK 470 ILE T 42 CG1 CG2 CD1
REMARK 470 GLU T 45 CG CD OE1 OE2
REMARK 470 GLU T 49 CG CD OE1 OE2
REMARK 470 LYS T 50 CG CD CE NZ
REMARK 470 THR T 51 OG1 CG2
REMARK 470 LYS T 52 CG CD CE NZ
REMARK 470 ILE T 60 CG1 CG2 CD1
REMARK 470 GLU T 67 CG CD OE1 OE2
REMARK 470 GLU T 71 CG CD OE1 OE2
REMARK 470 GLU T 75 CG CD OE1 OE2
REMARK 470 LEU T 78 CG CD1 CD2
REMARK 470 LEU T 79 CG CD1 CD2
REMARK 470 LYS T 93 CD CE NZ
REMARK 470 SER T 96 OG
REMARK 470 PHE T 97 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU T 142 CG CD OE1 OE2
REMARK 470 ASP T 160 CG OD1 OD2
REMARK 470 VAL T 163 CG1 CG2
REMARK 470 LEU T 164 CG CD1 CD2
REMARK 470 LYS T 165 CG CD CE NZ
REMARK 470 ASP T 167 CG OD1 OD2
REMARK 470 GLN T 169 CG CD OE1 NE2
REMARK 470 GLN T 171 CG CD OE1 NE2
REMARK 470 LYS T 172 CG CD CE NZ
REMARK 470 GLU T 230 CG CD OE1 OE2
REMARK 470 LYS T 262 CG CD CE NZ
REMARK 470 LEU T 264 CG CD1 CD2
REMARK 470 SER T 280 OG
REMARK 470 LYS T 281 CD CE NZ
REMARK 470 SER T 282 OG
REMARK 470 SER T 286 OG
REMARK 470 THR T 287 OG1 CG2
REMARK 470 GLU T 319 CG CD OE1 OE2
REMARK 470 LEU T 320 CG CD1 CD2
REMARK 470 LYS T 321 CG CD CE NZ
REMARK 470 GLU T 322 CG CD OE1 OE2
REMARK 470 SER T 325 OG
REMARK 470 GLU T 345 CG CD OE1 OE2
REMARK 470 LYS T 363 CG CD CE NZ
REMARK 470 GLU T 364 CG CD OE1 OE2
REMARK 470 SER T 367 OG
REMARK 470 LYS T 368 CG CD CE NZ
REMARK 470 LEU T 370 CG CD1 CD2
REMARK 470 SER T 373 OG
REMARK 470 ASP T 402 CG OD1 OD2
REMARK 470 GLU T 411 CG CD OE1 OE2
REMARK 470 ARG T 473 CG CD NE CZ NH1 NH2
REMARK 470 GLU T 481 CG CD OE1 OE2
REMARK 470 LYS T 484 CG CD CE NZ
REMARK 470 GLN T 500 CG CD OE1 NE2
REMARK 470 ARG T 503 CG CD NE CZ NH1 NH2
REMARK 470 LEU T 534 CG CD1 CD2
REMARK 470 GLU T 536 CG CD OE1 OE2
REMARK 470 GLU T 549 CG CD OE1 OE2
REMARK 470 ARG T 550 CG CD NE CZ NH1 NH2
REMARK 470 LYS T 567 CG CD CE NZ
REMARK 470 LYS T 568 CG CD CE NZ
REMARK 470 VAL T 571 CG1 CG2
REMARK 470 ASN T 572 CG OD1 ND2
REMARK 470 TYR T 573 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER T 576 OG
REMARK 470 ARG T 607 CG CD NE CZ NH1 NH2
REMARK 470 SER T 627 OG
REMARK 470 ASN T 629 CG OD1 ND2
REMARK 470 THR T 631 OG1 CG2
REMARK 470 GLU T 633 CG CD OE1 OE2
REMARK 470 LEU T 637 CG CD1 CD2
REMARK 470 TYR T 638 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP T 640 CG OD1 OD2
REMARK 470 LYS T 649 CG CD CE NZ
REMARK 470 ARG T 684 CG CD NE CZ NH1 NH2
REMARK 470 GLU T 687 CG CD OE1 OE2
REMARK 470 GLU T 688 CG CD OE1 OE2
REMARK 470 VAL T 689 CG1 CG2
REMARK 470 LYS T 697 CG CD CE NZ
REMARK 470 LEU T 704 CG CD1 CD2
REMARK 470 PHE T 711 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS T 737 CG CD CE NZ
REMARK 470 GLN T 740 CG CD OE1 NE2
REMARK 470 SER T 748 OG
REMARK 470 MET T 751 CG SD CE
REMARK 470 ASP T 756 CG OD1 OD2
REMARK 470 LYS T 769 CG CD CE NZ
REMARK 470 GLU T 774 CG CD OE1 OE2
REMARK 470 ARG T 778 CG CD NE CZ NH1 NH2
REMARK 470 LYS T 803 CG CD CE NZ
REMARK 470 ASN T 805 CG OD1 ND2
REMARK 470 ASP T 806 CG OD1 OD2
REMARK 470 LYS T 809 CG CD CE NZ
REMARK 470 GLN T 817 CG CD OE1 NE2
REMARK 470 LEU T 818 CG CD1 CD2
REMARK 470 LYS T 821 CG CD CE NZ
REMARK 470 ILE T 826 CG1 CG2 CD1
REMARK 470 LEU T 827 CG CD1 CD2
REMARK 470 THR T 829 OG1 CG2
REMARK 470 GLU T 830 CG CD OE1 OE2
REMARK 470 GLN T 833 CG CD OE1 NE2
REMARK 470 SER T 842 OG
REMARK 470 VAL T 850 CG1 CG2
REMARK 470 PRO T 853 CG CD
REMARK 470 THR T 855 OG1 CG2
REMARK 470 SER T 859 OG
REMARK 470 LYS T 865 CD CE NZ
REMARK 470 LEU T 869 CG CD1 CD2
REMARK 470 LYS T 873 CG CD CE NZ
REMARK 470 ASP T 874 CG OD1 OD2
REMARK 470 ILE T 876 CG1 CG2 CD1
REMARK 470 GLU T 880 CG CD OE1 OE2
REMARK 470 SER T 885 OG
REMARK 470 ASN T 896 CG OD1 ND2
REMARK 470 GLN T 905 CG CD OE1 NE2
REMARK 470 SER T 906 OG
REMARK 470 LEU T 907 CG CD1 CD2
REMARK 470 VAL T 908 CG1 CG2
REMARK 470 VAL T 909 CG1 CG2
REMARK 470 LEU T 910 CG CD1 CD2
REMARK 470 GLN T 917 CG CD OE1 NE2
REMARK 470 LYS T 918 CG CD CE NZ
REMARK 470 SER T 930 OG
REMARK 470 TYR T 931 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU T 932 CG CD1 CD2
REMARK 470 TYR T 936 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE T 937 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL T 940 CG1 CG2
REMARK 470 PHE T 942 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP T 944 CG OD1 OD2
REMARK 470 GLN T 952 CG CD OE1 NE2
REMARK 470 LEU T 954 CG CD1 CD2
REMARK 470 ASN T 956 CG OD1 ND2
REMARK 470 SER T 959 OG
REMARK 470 ARG T 960 CG CD NE CZ NH1 NH2
REMARK 470 SER T 961 OG
REMARK 470 LYS T 963 CG CD CE NZ
REMARK 470 GLN T 964 CG CD OE1 NE2
REMARK 470 GLN T 967 CG CD OE1 NE2
REMARK 470 LYS T 968 CG CD CE NZ
REMARK 470 SER T 975 OG
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 LEU B 33 CG CD1 CD2
REMARK 470 GLU B 36 CG CD OE1 OE2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 LYS B 40 CG CD CE NZ
REMARK 470 THR B 56 OG1 CG2
REMARK 470 ASN B 57 CG OD1 ND2
REMARK 470 PHE B 58 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 GLU B 72 CG CD OE1 OE2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 ARG B 97 NH1 NH2
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 470 LYS B 136 CG CD CE NZ
REMARK 470 ARG B 142 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 175 CG CD OE1 NE2
REMARK 470 LEU B 176 CG CD1 CD2
REMARK 470 U D 17 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U D 17 C6
REMARK 470 SER U 2 OG
REMARK 470 VAL U 6 CG1 CG2
REMARK 470 GLU U 7 CG CD OE1 OE2
REMARK 470 VAL U 10 CG1 CG2
REMARK 470 GLU U 11 CG CD OE1 OE2
REMARK 470 LEU U 14 CG CD1 CD2
REMARK 470 ILE U 21 CG1 CG2 CD1
REMARK 470 ILE U 22 CG1 CG2 CD1
REMARK 470 LYS U 23 CG CD CE NZ
REMARK 470 GLN U 24 CG CD OE1 NE2
REMARK 470 GLN U 25 CG CD OE1 NE2
REMARK 470 THR U 27 OG1 CG2
REMARK 470 ASP U 28 CG OD1 OD2
REMARK 470 SER U 32 OG
REMARK 470 ARG U 34 CG CD NE CZ NH1 NH2
REMARK 470 SER U 35 OG
REMARK 470 SER U 36 OG
REMARK 470 SER U 37 OG
REMARK 470 THR U 38 OG1 CG2
REMARK 470 LYS U 41 CG CD CE NZ
REMARK 470 ILE U 42 CG1 CG2 CD1
REMARK 470 HIS U 44 CG ND1 CD2 CE1 NE2
REMARK 470 GLU U 45 CG CD OE1 OE2
REMARK 470 ILE U 46 CG1 CG2 CD1
REMARK 470 PHE U 47 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER U 48 OG
REMARK 470 LYS U 50 CG CD CE NZ
REMARK 470 THR U 51 OG1 CG2
REMARK 470 LYS U 52 CG CD CE NZ
REMARK 470 TYR U 53 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PRO U 55 CG CD
REMARK 470 GLU U 67 CG CD OE1 OE2
REMARK 470 LYS U 68 CG CD CE NZ
REMARK 470 GLU U 71 CG CD OE1 OE2
REMARK 470 ASN U 74 CG OD1 ND2
REMARK 470 GLU U 75 CG CD OE1 OE2
REMARK 470 LEU U 78 CG CD1 CD2
REMARK 470 LEU U 79 CG CD1 CD2
REMARK 470 GLU U 94 CG CD OE1 OE2
REMARK 470 SER U 96 OG
REMARK 470 PHE U 97 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU U 142 CG CD OE1 OE2
REMARK 470 ASP U 160 CG OD1 OD2
REMARK 470 VAL U 163 CG1 CG2
REMARK 470 LYS U 165 CG CD CE NZ
REMARK 470 ASP U 167 CG OD1 OD2
REMARK 470 GLN U 171 CG CD OE1 NE2
REMARK 470 LYS U 172 CG CD CE NZ
REMARK 470 LYS U 203 CD CE NZ
REMARK 470 GLU U 230 CG CD OE1 OE2
REMARK 470 LYS U 262 CG CD CE NZ
REMARK 470 LEU U 277 CG CD1 CD2
REMARK 470 SER U 280 OG
REMARK 470 LYS U 281 CG CD CE NZ
REMARK 470 SER U 282 OG
REMARK 470 SER U 286 OG
REMARK 470 THR U 287 OG1 CG2
REMARK 470 ASN U 290 CG OD1 ND2
REMARK 470 SER U 314 OG
REMARK 470 GLU U 315 CG CD OE1 OE2
REMARK 470 LEU U 316 CG CD1 CD2
REMARK 470 GLU U 319 CG CD OE1 OE2
REMARK 470 LEU U 320 CG CD1 CD2
REMARK 470 LYS U 321 CG CD CE NZ
REMARK 470 GLU U 322 CG CD OE1 OE2
REMARK 470 ASN U 323 CG OD1 ND2
REMARK 470 TYR U 329 OH
REMARK 470 ARG U 337 CG CD NE CZ NH1 NH2
REMARK 470 GLU U 345 CG CD OE1 OE2
REMARK 470 LYS U 363 CG CD CE NZ
REMARK 470 SER U 366 OG
REMARK 470 SER U 367 OG
REMARK 470 LYS U 368 CG CD CE NZ
REMARK 470 GLU U 369 CG CD OE1 OE2
REMARK 470 LEU U 370 CG CD1 CD2
REMARK 470 ASP U 392 CG OD1 OD2
REMARK 470 GLU U 393 CG CD OE1 OE2
REMARK 470 SER U 394 OG
REMARK 470 GLN U 395 CG CD OE1 NE2
REMARK 470 GLU U 396 CG CD OE1 OE2
REMARK 470 ASP U 402 CG OD1 OD2
REMARK 470 GLU U 405 CG CD OE1 OE2
REMARK 470 GLU U 406 CG CD OE1 OE2
REMARK 470 GLU U 411 CG CD OE1 OE2
REMARK 470 LYS U 414 CG CD CE NZ
REMARK 470 LYS U 415 CD CE NZ
REMARK 470 GLU U 452 CG CD OE1 OE2
REMARK 470 ASN U 453 CG OD1 ND2
REMARK 470 ARG U 473 CG CD NE CZ NH1 NH2
REMARK 470 GLU U 481 CG CD OE1 OE2
REMARK 470 LYS U 484 CG CD CE NZ
REMARK 470 GLN U 500 CG CD OE1 NE2
REMARK 470 ARG U 503 CG CD NE CZ NH1 NH2
REMARK 470 GLU U 536 CG CD OE1 OE2
REMARK 470 ARG U 542 CG CD NE CZ NH1 NH2
REMARK 470 GLU U 549 CG CD OE1 OE2
REMARK 470 LYS U 567 CG CD CE NZ
REMARK 470 LYS U 568 CG CD CE NZ
REMARK 470 GLN U 569 CG CD OE1 NE2
REMARK 470 VAL U 570 CG1 CG2
REMARK 470 VAL U 571 CG1 CG2
REMARK 470 ASN U 572 CG OD1 ND2
REMARK 470 GLU U 575 CG CD OE1 OE2
REMARK 470 ARG U 607 CG CD NE CZ NH1 NH2
REMARK 470 ASN U 608 CG OD1 ND2
REMARK 470 SER U 627 OG
REMARK 470 ASN U 629 CG OD1 ND2
REMARK 470 LEU U 637 CG CD1 CD2
REMARK 470 SER U 656 OG
REMARK 470 ASP U 657 CG OD1 OD2
REMARK 470 SER U 659 OG
REMARK 470 ARG U 684 CG CD NE CZ NH1 NH2
REMARK 470 SER U 686 OG
REMARK 470 GLU U 687 CG CD OE1 OE2
REMARK 470 GLU U 688 CG CD OE1 OE2
REMARK 470 LYS U 697 CG CD CE NZ
REMARK 470 ASP U 700 CG OD1 OD2
REMARK 470 GLU U 701 CG CD OE1 OE2
REMARK 470 LEU U 704 CG CD1 CD2
REMARK 470 LYS U 737 CG CD CE NZ
REMARK 470 GLN U 740 CG CD OE1 NE2
REMARK 470 LYS U 769 CG CD CE NZ
REMARK 470 GLN U 796 CG CD OE1 NE2
REMARK 470 LYS U 809 CG CD CE NZ
REMARK 470 SER U 813 OG
REMARK 470 LEU U 816 CG CD1 CD2
REMARK 470 GLN U 817 CG CD OE1 NE2
REMARK 470 LYS U 821 CG CD CE NZ
REMARK 470 GLU U 830 CG CD OE1 OE2
REMARK 470 GLU U 831 CG CD OE1 OE2
REMARK 470 ASN U 832 CG OD1 ND2
REMARK 470 GLN U 833 CG CD OE1 NE2
REMARK 470 ASP U 837 CG OD1 OD2
REMARK 470 LEU U 844 CG CD1 CD2
REMARK 470 HIS U 845 CG ND1 CD2 CE1 NE2
REMARK 470 VAL U 850 CG1 CG2
REMARK 470 PRO U 853 CG CD
REMARK 470 THR U 855 OG1 CG2
REMARK 470 LYS U 857 CG CD CE NZ
REMARK 470 LYS U 873 CG CD CE NZ
REMARK 470 GLU U 880 CG CD OE1 OE2
REMARK 470 ASN U 881 CG OD1 ND2
REMARK 470 LEU U 884 CG CD1 CD2
REMARK 470 SER U 885 OG
REMARK 470 CYS U 890 SG
REMARK 470 PHE U 891 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN U 896 CG OD1 ND2
REMARK 470 ASN U 898 CG OD1 ND2
REMARK 470 GLN U 905 CG CD OE1 NE2
REMARK 470 SER U 906 OG
REMARK 470 LEU U 907 CG CD1 CD2
REMARK 470 VAL U 908 CG1 CG2
REMARK 470 LEU U 910 CG CD1 CD2
REMARK 470 LYS U 918 CG CD CE NZ
REMARK 470 LEU U 921 CG CD1 CD2
REMARK 470 GLU U 922 CG CD OE1 OE2
REMARK 470 LYS U 923 CG CD CE NZ
REMARK 470 LEU U 924 CG CD1 CD2
REMARK 470 TYR U 928 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS U 929 CG CD CE NZ
REMARK 470 SER U 930 OG
REMARK 470 TYR U 931 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU U 932 CG CD1 CD2
REMARK 470 VAL U 933 CG1 CG2
REMARK 470 THR U 934 OG1 CG2
REMARK 470 VAL U 935 CG1 CG2
REMARK 470 TYR U 936 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE U 937 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO U 938 CG CD
REMARK 470 THR U 939 OG1 CG2
REMARK 470 VAL U 940 CG1 CG2
REMARK 470 SER U 948 OG
REMARK 470 GLU U 949 CG CD OE1 OE2
REMARK 470 TYR U 950 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU U 951 CG CD1 CD2
REMARK 470 GLN U 952 CG CD OE1 NE2
REMARK 470 LEU U 954 CG CD1 CD2
REMARK 470 SER U 955 OG
REMARK 470 ASP U 958 CG OD1 OD2
REMARK 470 SER U 959 OG
REMARK 470 ARG U 960 CG CD NE CZ NH1 NH2
REMARK 470 SER U 961 OG
REMARK 470 PHE U 962 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS U 963 CG CD CE NZ
REMARK 470 GLN U 964 CG CD OE1 NE2
REMARK 470 GLN U 967 CG CD OE1 NE2
REMARK 470 LYS U 968 CG CD CE NZ
REMARK 470 LEU U 973 CG CD1 CD2
REMARK 470 LYS U 974 CG CD CE NZ
REMARK 470 SER U 975 OG
REMARK 470 LYS C 30 CG CD CE NZ
REMARK 470 ARG C 31 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 33 CG CD1 CD2
REMARK 470 GLU C 36 CG CD OE1 OE2
REMARK 470 LYS C 39 CG CD CE NZ
REMARK 470 LYS C 40 CG CD CE NZ
REMARK 470 PHE C 54 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 60 CG CD OE1 OE2
REMARK 470 ILE C 61 CG1 CG2 CD1
REMARK 470 LYS C 62 CG CD CE NZ
REMARK 470 GLU C 72 CG CD OE1 OE2
REMARK 470 LYS C 73 CG CD CE NZ
REMARK 470 ARG C 97 NH1 NH2
REMARK 470 GLU C 115 CG CD OE1 OE2
REMARK 470 LYS C 132 CG CD CE NZ
REMARK 470 LYS C 134 CG CD CE NZ
REMARK 470 LYS C 136 CG CD CE NZ
REMARK 470 ARG C 142 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 143 CG CD CE NZ
REMARK 470 LYS C 154 CG CD CE NZ
REMARK 470 LYS C 169 CG CD CE NZ
REMARK 470 GLN C 175 CG CD OE1 NE2
REMARK 470 LEU C 176 CG CD1 CD2
REMARK 470 U E 17 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U E 17 C6
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 O2 C E 27 N2 G E 43 1.91
REMARK 500 CB LEU U 95 CZ PHE U 143 2.07
REMARK 500 O LEU T 907 N GLY T 911 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 97 NE ARG B 97 CZ 0.158
REMARK 500 G D 1 P G D 1 OP3 -0.080
REMARK 500 ARG C 97 NE ARG C 97 CZ 0.162
REMARK 500 G E 1 P G E 1 OP3 -0.083
REMARK 500 G E 43 C6 G E 43 O6 0.100
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 PRO T 507 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG B 97 CD - NE - CZ ANGL. DEV. = -15.0 DEGREES
REMARK 500 ARG C 97 CD - NE - CZ ANGL. DEV. = -12.8 DEGREES
REMARK 500 G E 43 C6 - N1 - C2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 G E 43 N1 - C2 - N3 ANGL. DEV. = 5.4 DEGREES
REMARK 500 G E 43 C5 - C6 - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 G E 43 N1 - C2 - N2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 G E 43 N3 - C2 - N2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 G E 43 C5 - C6 - O6 ANGL. DEV. = -5.0 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 T 99 39.48 -98.72
REMARK 500 GLU T 100 -159.80 -88.69
REMARK 500 GLN T 169 -38.12 -39.03
REMARK 500 ASN T 223 108.04 -53.45
REMARK 500 VAL T 228 38.11 -99.19
REMARK 500 ASN T 274 56.84 31.41
REMARK 500 THR T 287 74.13 -108.08
REMARK 500 SER T 314 -86.66 -45.69
REMARK 500 GLU T 393 22.85 -76.64
REMARK 500 LEU T 416 -18.97 -49.36
REMARK 500 ASP T 427 87.11 -165.70
REMARK 500 PRO T 475 -1.90 -57.29
REMARK 500 GLU T 481 -7.24 -58.44
REMARK 500 VAL T 501 -55.92 -9.20
REMARK 500 PRO T 541 13.03 -69.09
REMARK 500 THR T 631 154.13 -45.10
REMARK 500 SER T 656 -169.59 -75.60
REMARK 500 ASP T 657 98.32 -59.20
REMARK 500 LEU T 658 -19.73 -48.84
REMARK 500 ASP T 750 -154.30 -128.60
REMARK 500 LYS T 769 -71.96 -73.28
REMARK 500 GLU T 830 -22.85 -33.12
REMARK 500 LEU T 849 -76.12 -51.65
REMARK 500 LYS T 873 -4.27 -53.40
REMARK 500 ASP T 874 88.76 -61.55
REMARK 500 PRO T 894 15.44 -57.96
REMARK 500 VAL B 126 0.75 -64.24
REMARK 500 LYS B 129 -70.08 -47.67
REMARK 500 LEU B 176 107.38 -56.60
REMARK 500 GLU U 49 88.31 -60.46
REMARK 500 LEU U 78 -19.23 -46.95
REMARK 500 ASP U 160 104.29 -59.31
REMARK 500 ASN U 223 109.68 -47.65
REMARK 500 LEU U 270 8.91 -66.61
REMARK 500 ASN U 274 63.30 -104.34
REMARK 500 ASP U 341 128.89 -35.08
REMARK 500 ALA U 349 -7.65 -58.76
REMARK 500 SER U 367 73.40 -157.59
REMARK 500 ASP U 427 88.26 -155.36
REMARK 500 VAL U 482 -52.22 -126.69
REMARK 500 LYS U 484 19.06 59.36
REMARK 500 GLN U 500 31.35 -93.50
REMARK 500 LYS U 568 27.29 -79.20
REMARK 500 SER U 609 -168.17 -118.21
REMARK 500 LEU U 654 11.79 -69.84
REMARK 500 SER U 686 -13.64 84.43
REMARK 500 PRO U 894 18.04 -67.00
REMARK 500 ASP C 20 158.09 -42.33
REMARK 500 ASN C 116 69.78 35.14
REMARK 500 LYS C 125 48.26 71.17
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 2 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 26 OG1
REMARK 620 2 THR B 44 OG1 76.6
REMARK 620 3 ASP B 67 OD1 101.1 127.3
REMARK 620 4 GTP B 250 O1G 132.1 112.1 107.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 5 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 26 OG1
REMARK 620 2 THR C 44 OG1 62.6
REMARK 620 3 GTP C 250 O1G 148.7 148.6
REMARK 620 4 GTP C 250 O2B 82.3 89.2 96.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP B 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IBV RELATED DB: PDB
REMARK 900 KARYOPHERIN CYTOSOLIC STATE
DBREF 3ICQ T 1 978 UNP O94258 XPOT_SCHPO 1 978
DBREF 3ICQ B 9 179 UNP P32835 GSP1_YEAST 9 179
DBREF 3ICQ D 1 76 PDB 3ICQ 3ICQ 1 76
DBREF 3ICQ U 1 978 UNP O94258 XPOT_SCHPO 1 978
DBREF 3ICQ C 9 179 UNP P32835 GSP1_YEAST 9 179
DBREF 3ICQ E 1 76 PDB 3ICQ 3ICQ 1 76
SEQADV 3ICQ GLY T -1 UNP O94258 EXPRESSION TAG
SEQADV 3ICQ PRO T 0 UNP O94258 EXPRESSION TAG
SEQADV 3ICQ LEU B 71 UNP P32835 GLN 71 ENGINEERED MUTATION
SEQADV 3ICQ GLY U -1 UNP O94258 EXPRESSION TAG
SEQADV 3ICQ PRO U 0 UNP O94258 EXPRESSION TAG
SEQADV 3ICQ LEU C 71 UNP P32835 GLN 71 ENGINEERED MUTATION
SEQRES 1 T 980 GLY PRO MET SER ALA GLN ASP VAL GLU ASN ALA VAL GLU
SEQRES 2 T 980 ALA ALA LEU ASP PRO SER VAL GLY PRO ILE ILE LYS GLN
SEQRES 3 T 980 GLN ALA THR ASP PHE ILE GLY SER LEU ARG SER SER SER
SEQRES 4 T 980 THR GLY TRP LYS ILE CYS HIS GLU ILE PHE SER GLU LYS
SEQRES 5 T 980 THR LYS TYR LYS PRO SER THR ARG LEU ILE CYS LEU GLN
SEQRES 6 T 980 THR LEU SER GLU LYS VAL ARG GLU TRP ASN ASN GLU SER
SEQRES 7 T 980 ASN LEU LEU GLU LEU GLN MET ILE ARG ASP SER VAL TRP
SEQRES 8 T 980 SER TYR ILE LYS GLU LEU SER PHE LEU ASP GLU PRO ALA
SEQRES 9 T 980 TYR ILE SER ASN ALA VAL GLN HIS LEU LEU THR LEU LEU
SEQRES 10 T 980 PHE LEU GLN LEU TYR PRO SER ASN TRP ASN ASP PHE PHE
SEQRES 11 T 980 ALA SER LEU GLN GLY VAL ILE ALA ALA SER SER GLN SER
SEQRES 12 T 980 GLU PHE SER ASN PHE TYR LEU LYS VAL LEU LEU SER ILE
SEQRES 13 T 980 GLY ASP GLU ILE ALA ASP SER LEU VAL LEU LYS THR ASP
SEQRES 14 T 980 VAL GLN ILE GLN LYS ASP ASN LEU VAL LYS ASP ALA ILE
SEQRES 15 T 980 ARG ALA ASN ASP MET SER ASP ILE VAL SER PHE VAL TYR
SEQRES 16 T 980 GLU MET MET LEU ALA TYR SER ASN ALA LYS ASN TYR GLY
SEQRES 17 T 980 THR VAL GLY LEU CYS LEU GLN VAL TYR ALA GLN TRP VAL
SEQRES 18 T 980 SER TRP ILE ASN ILE ASN LEU ILE VAL ASN GLU PRO CYS
SEQRES 19 T 980 MET ASN LEU LEU TYR SER PHE LEU GLN ILE GLU GLU LEU
SEQRES 20 T 980 ARG CYS ALA ALA CYS GLU THR MET THR GLU ILE VAL ASN
SEQRES 21 T 980 LYS LYS MET LYS PRO LEU GLU LYS LEU ASN LEU LEU ASN
SEQRES 22 T 980 ILE LEU ASN LEU ASN LEU PHE PHE SER LYS SER GLN GLU
SEQRES 23 T 980 GLN SER THR ASP PRO ASN PHE ASP GLU HIS VAL ALA LYS
SEQRES 24 T 980 LEU ILE ASN ALA GLN GLY VAL GLU LEU VAL ALA ILE LYS
SEQRES 25 T 980 SER ASP PRO SER GLU LEU SER PRO GLU LEU LYS GLU ASN
SEQRES 26 T 980 CYS SER PHE GLN LEU TYR ASN LEU PHE PRO TYR LEU ILE
SEQRES 27 T 980 ARG TYR LEU SER ASP ASP TYR ASP GLU THR SER THR ALA
SEQRES 28 T 980 VAL PHE PRO PHE LEU SER ASP LEU LEU VAL SER LEU ARG
SEQRES 29 T 980 LYS GLU SER SER SER LYS GLU LEU SER ALA SER LEU LYS
SEQRES 30 T 980 GLU PHE LEU LYS SER LEU LEU GLU ALA ILE ILE LYS LYS
SEQRES 31 T 980 MET LYS TYR ASP GLU SER GLN GLU TRP ASP ASP ASP PRO
SEQRES 32 T 980 ASP SER GLU GLU GLU ALA GLU PHE GLN GLU MET ARG LYS
SEQRES 33 T 980 LYS LEU LYS ILE PHE GLN ASP THR ILE ASN SER ILE ASP
SEQRES 34 T 980 SER SER LEU PHE SER SER TYR MET TYR SER ALA ILE THR
SEQRES 35 T 980 SER SER LEU SER THR ALA ALA THR LEU SER PRO GLU ASN
SEQRES 36 T 980 SER TRP GLN LEU ILE GLU PHE ALA LEU TYR GLU THR TYR
SEQRES 37 T 980 ILE PHE GLY GLU GLY LEU ARG GLY PRO ASP ALA PHE PHE
SEQRES 38 T 980 ASN GLU VAL ASP LYS SER PRO THR VAL LEU SER GLN ILE
SEQRES 39 T 980 LEU ALA LEU VAL THR THR SER GLN VAL CYS ARG HIS PRO
SEQRES 40 T 980 HIS PRO LEU VAL GLN LEU LEU TYR MET GLU ILE LEU VAL
SEQRES 41 T 980 ARG TYR ALA SER PHE PHE ASP TYR GLU SER ALA ALA ILE
SEQRES 42 T 980 PRO ALA LEU ILE GLU TYR PHE VAL GLY PRO ARG GLY ILE
SEQRES 43 T 980 HIS ASN THR ASN GLU ARG VAL ARG PRO ARG ALA TRP TYR
SEQRES 44 T 980 LEU PHE TYR ARG PHE VAL LYS SER ILE LYS LYS GLN VAL
SEQRES 45 T 980 VAL ASN TYR THR GLU SER SER LEU ALA MET LEU GLY ASP
SEQRES 46 T 980 LEU LEU ASN ILE SER VAL SER PRO VAL THR ASP MET ASP
SEQRES 47 T 980 ALA PRO VAL PRO THR LEU ASN SER SER ILE ARG ASN SER
SEQRES 48 T 980 ASP PHE ASN SER GLN LEU TYR LEU PHE GLU THR VAL GLY
SEQRES 49 T 980 VAL LEU ILE SER SER GLY ASN LEU THR PRO GLU GLU GLN
SEQRES 50 T 980 ALA LEU TYR CYS ASP SER LEU ILE ASN ALA LEU ILE GLY
SEQRES 51 T 980 LYS ALA ASN ALA ALA LEU SER SER ASP LEU SER ALA LEU
SEQRES 52 T 980 GLU ASN ILE ILE SER VAL TYR CYS SER LEU MET ALA ILE
SEQRES 53 T 980 GLY ASN PHE ALA LYS GLY PHE PRO ALA ARG GLY SER GLU
SEQRES 54 T 980 GLU VAL ALA TRP LEU ALA SER PHE ASN LYS ALA SER ASP
SEQRES 55 T 980 GLU ILE PHE LEU ILE LEU ASP ARG MET GLY PHE ASN GLU
SEQRES 56 T 980 ASP ILE ARG GLY ALA VAL ARG PHE THR SER GLY ARG ILE
SEQRES 57 T 980 ILE ASN VAL VAL GLY PRO ASP MET LEU PRO LYS VAL PRO
SEQRES 58 T 980 GLN LEU ILE SER ILE LEU LEU ASN SER ILE ASP MET ASN
SEQRES 59 T 980 GLU LEU VAL ASP VAL LEU SER PHE ILE SER GLN LEU ILE
SEQRES 60 T 980 HIS ILE TYR LYS ASP ASN MET MET GLU ILE THR ASN ARG
SEQRES 61 T 980 MET LEU PRO THR LEU LEU MET ARG ILE PHE SER SER LEU
SEQRES 62 T 980 SER ALA ALA PRO GLN GLY THR ASP ASP ALA VAL LYS GLN
SEQRES 63 T 980 ASN ASP LEU ARG LYS SER TYR ILE SER PHE ILE LEU GLN
SEQRES 64 T 980 LEU LEU ASN LYS GLY PHE GLY SER ILE LEU PHE THR GLU
SEQRES 65 T 980 GLU ASN GLN VAL TYR PHE ASP PRO LEU ILE ASN SER ILE
SEQRES 66 T 980 LEU HIS PHE ALA ASN LEU VAL GLY GLU PRO ALA THR GLN
SEQRES 67 T 980 LYS SER SER ILE ALA LEU VAL SER LYS MET VAL SER LEU
SEQRES 68 T 980 TRP GLY GLY LYS ASP GLY ILE ALA GLY PHE GLU ASN PHE
SEQRES 69 T 980 THR LEU SER LEU THR PRO LEU CYS PHE GLU MET PRO VAL
SEQRES 70 T 980 ASN PRO ASN PHE ASN THR ARG ASP GLY GLN SER LEU VAL
SEQRES 71 T 980 VAL LEU GLY GLU LEU ALA GLY LEU GLN LYS ILE ILE LEU
SEQRES 72 T 980 GLU LYS LEU GLY ASP ILE TYR LYS SER TYR LEU VAL THR
SEQRES 73 T 980 VAL TYR PHE PRO THR VAL ASN PHE PRO ASP VAL MET ALA
SEQRES 74 T 980 SER GLU TYR LEU GLN ALA LEU SER ASN LEU ASP SER ARG
SEQRES 75 T 980 SER PHE LYS GLN PHE PHE GLN LYS PHE ILE GLN ALA LEU
SEQRES 76 T 980 LYS SER GLY ASN VAL
SEQRES 1 B 171 GLU VAL PRO THR PHE LYS LEU VAL LEU VAL GLY ASP GLY
SEQRES 2 B 171 GLY THR GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR
SEQRES 3 B 171 GLY GLU PHE GLU LYS LYS TYR ILE ALA THR ILE GLY VAL
SEQRES 4 B 171 GLU VAL HIS PRO LEU SER PHE TYR THR ASN PHE GLY GLU
SEQRES 5 B 171 ILE LYS PHE ASP VAL TRP ASP THR ALA GLY LEU GLU LYS
SEQRES 6 B 171 PHE GLY GLY LEU ARG ASP GLY TYR TYR ILE ASN ALA GLN
SEQRES 7 B 171 CYS ALA ILE ILE MET PHE ASP VAL THR SER ARG ILE THR
SEQRES 8 B 171 TYR LYS ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG
SEQRES 9 B 171 VAL CYS GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS
SEQRES 10 B 171 VAL ASP VAL LYS GLU ARG LYS VAL LYS ALA LYS THR ILE
SEQRES 11 B 171 THR PHE HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE
SEQRES 12 B 171 SER ALA LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU
SEQRES 13 B 171 TRP LEU ALA ARG LYS LEU ALA GLY ASN PRO GLN LEU GLU
SEQRES 14 B 171 PHE VAL
SEQRES 1 D 67 G C G G A U U U A A C U C
SEQRES 2 D 67 A G U U G G G A G A G C G
SEQRES 3 D 67 C C U U C G G G A G G U C
SEQRES 4 D 67 C U G U G U U C G A U C C
SEQRES 5 D 67 A C A G A A U U C G C A C
SEQRES 6 D 67 C A
SEQRES 1 U 980 GLY PRO MET SER ALA GLN ASP VAL GLU ASN ALA VAL GLU
SEQRES 2 U 980 ALA ALA LEU ASP PRO SER VAL GLY PRO ILE ILE LYS GLN
SEQRES 3 U 980 GLN ALA THR ASP PHE ILE GLY SER LEU ARG SER SER SER
SEQRES 4 U 980 THR GLY TRP LYS ILE CYS HIS GLU ILE PHE SER GLU LYS
SEQRES 5 U 980 THR LYS TYR LYS PRO SER THR ARG LEU ILE CYS LEU GLN
SEQRES 6 U 980 THR LEU SER GLU LYS VAL ARG GLU TRP ASN ASN GLU SER
SEQRES 7 U 980 ASN LEU LEU GLU LEU GLN MET ILE ARG ASP SER VAL TRP
SEQRES 8 U 980 SER TYR ILE LYS GLU LEU SER PHE LEU ASP GLU PRO ALA
SEQRES 9 U 980 TYR ILE SER ASN ALA VAL GLN HIS LEU LEU THR LEU LEU
SEQRES 10 U 980 PHE LEU GLN LEU TYR PRO SER ASN TRP ASN ASP PHE PHE
SEQRES 11 U 980 ALA SER LEU GLN GLY VAL ILE ALA ALA SER SER GLN SER
SEQRES 12 U 980 GLU PHE SER ASN PHE TYR LEU LYS VAL LEU LEU SER ILE
SEQRES 13 U 980 GLY ASP GLU ILE ALA ASP SER LEU VAL LEU LYS THR ASP
SEQRES 14 U 980 VAL GLN ILE GLN LYS ASP ASN LEU VAL LYS ASP ALA ILE
SEQRES 15 U 980 ARG ALA ASN ASP MET SER ASP ILE VAL SER PHE VAL TYR
SEQRES 16 U 980 GLU MET MET LEU ALA TYR SER ASN ALA LYS ASN TYR GLY
SEQRES 17 U 980 THR VAL GLY LEU CYS LEU GLN VAL TYR ALA GLN TRP VAL
SEQRES 18 U 980 SER TRP ILE ASN ILE ASN LEU ILE VAL ASN GLU PRO CYS
SEQRES 19 U 980 MET ASN LEU LEU TYR SER PHE LEU GLN ILE GLU GLU LEU
SEQRES 20 U 980 ARG CYS ALA ALA CYS GLU THR MET THR GLU ILE VAL ASN
SEQRES 21 U 980 LYS LYS MET LYS PRO LEU GLU LYS LEU ASN LEU LEU ASN
SEQRES 22 U 980 ILE LEU ASN LEU ASN LEU PHE PHE SER LYS SER GLN GLU
SEQRES 23 U 980 GLN SER THR ASP PRO ASN PHE ASP GLU HIS VAL ALA LYS
SEQRES 24 U 980 LEU ILE ASN ALA GLN GLY VAL GLU LEU VAL ALA ILE LYS
SEQRES 25 U 980 SER ASP PRO SER GLU LEU SER PRO GLU LEU LYS GLU ASN
SEQRES 26 U 980 CYS SER PHE GLN LEU TYR ASN LEU PHE PRO TYR LEU ILE
SEQRES 27 U 980 ARG TYR LEU SER ASP ASP TYR ASP GLU THR SER THR ALA
SEQRES 28 U 980 VAL PHE PRO PHE LEU SER ASP LEU LEU VAL SER LEU ARG
SEQRES 29 U 980 LYS GLU SER SER SER LYS GLU LEU SER ALA SER LEU LYS
SEQRES 30 U 980 GLU PHE LEU LYS SER LEU LEU GLU ALA ILE ILE LYS LYS
SEQRES 31 U 980 MET LYS TYR ASP GLU SER GLN GLU TRP ASP ASP ASP PRO
SEQRES 32 U 980 ASP SER GLU GLU GLU ALA GLU PHE GLN GLU MET ARG LYS
SEQRES 33 U 980 LYS LEU LYS ILE PHE GLN ASP THR ILE ASN SER ILE ASP
SEQRES 34 U 980 SER SER LEU PHE SER SER TYR MET TYR SER ALA ILE THR
SEQRES 35 U 980 SER SER LEU SER THR ALA ALA THR LEU SER PRO GLU ASN
SEQRES 36 U 980 SER TRP GLN LEU ILE GLU PHE ALA LEU TYR GLU THR TYR
SEQRES 37 U 980 ILE PHE GLY GLU GLY LEU ARG GLY PRO ASP ALA PHE PHE
SEQRES 38 U 980 ASN GLU VAL ASP LYS SER PRO THR VAL LEU SER GLN ILE
SEQRES 39 U 980 LEU ALA LEU VAL THR THR SER GLN VAL CYS ARG HIS PRO
SEQRES 40 U 980 HIS PRO LEU VAL GLN LEU LEU TYR MET GLU ILE LEU VAL
SEQRES 41 U 980 ARG TYR ALA SER PHE PHE ASP TYR GLU SER ALA ALA ILE
SEQRES 42 U 980 PRO ALA LEU ILE GLU TYR PHE VAL GLY PRO ARG GLY ILE
SEQRES 43 U 980 HIS ASN THR ASN GLU ARG VAL ARG PRO ARG ALA TRP TYR
SEQRES 44 U 980 LEU PHE TYR ARG PHE VAL LYS SER ILE LYS LYS GLN VAL
SEQRES 45 U 980 VAL ASN TYR THR GLU SER SER LEU ALA MET LEU GLY ASP
SEQRES 46 U 980 LEU LEU ASN ILE SER VAL SER PRO VAL THR ASP MET ASP
SEQRES 47 U 980 ALA PRO VAL PRO THR LEU ASN SER SER ILE ARG ASN SER
SEQRES 48 U 980 ASP PHE ASN SER GLN LEU TYR LEU PHE GLU THR VAL GLY
SEQRES 49 U 980 VAL LEU ILE SER SER GLY ASN LEU THR PRO GLU GLU GLN
SEQRES 50 U 980 ALA LEU TYR CYS ASP SER LEU ILE ASN ALA LEU ILE GLY
SEQRES 51 U 980 LYS ALA ASN ALA ALA LEU SER SER ASP LEU SER ALA LEU
SEQRES 52 U 980 GLU ASN ILE ILE SER VAL TYR CYS SER LEU MET ALA ILE
SEQRES 53 U 980 GLY ASN PHE ALA LYS GLY PHE PRO ALA ARG GLY SER GLU
SEQRES 54 U 980 GLU VAL ALA TRP LEU ALA SER PHE ASN LYS ALA SER ASP
SEQRES 55 U 980 GLU ILE PHE LEU ILE LEU ASP ARG MET GLY PHE ASN GLU
SEQRES 56 U 980 ASP ILE ARG GLY ALA VAL ARG PHE THR SER GLY ARG ILE
SEQRES 57 U 980 ILE ASN VAL VAL GLY PRO ASP MET LEU PRO LYS VAL PRO
SEQRES 58 U 980 GLN LEU ILE SER ILE LEU LEU ASN SER ILE ASP MET ASN
SEQRES 59 U 980 GLU LEU VAL ASP VAL LEU SER PHE ILE SER GLN LEU ILE
SEQRES 60 U 980 HIS ILE TYR LYS ASP ASN MET MET GLU ILE THR ASN ARG
SEQRES 61 U 980 MET LEU PRO THR LEU LEU MET ARG ILE PHE SER SER LEU
SEQRES 62 U 980 SER ALA ALA PRO GLN GLY THR ASP ASP ALA VAL LYS GLN
SEQRES 63 U 980 ASN ASP LEU ARG LYS SER TYR ILE SER PHE ILE LEU GLN
SEQRES 64 U 980 LEU LEU ASN LYS GLY PHE GLY SER ILE LEU PHE THR GLU
SEQRES 65 U 980 GLU ASN GLN VAL TYR PHE ASP PRO LEU ILE ASN SER ILE
SEQRES 66 U 980 LEU HIS PHE ALA ASN LEU VAL GLY GLU PRO ALA THR GLN
SEQRES 67 U 980 LYS SER SER ILE ALA LEU VAL SER LYS MET VAL SER LEU
SEQRES 68 U 980 TRP GLY GLY LYS ASP GLY ILE ALA GLY PHE GLU ASN PHE
SEQRES 69 U 980 THR LEU SER LEU THR PRO LEU CYS PHE GLU MET PRO VAL
SEQRES 70 U 980 ASN PRO ASN PHE ASN THR ARG ASP GLY GLN SER LEU VAL
SEQRES 71 U 980 VAL LEU GLY GLU LEU ALA GLY LEU GLN LYS ILE ILE LEU
SEQRES 72 U 980 GLU LYS LEU GLY ASP ILE TYR LYS SER TYR LEU VAL THR
SEQRES 73 U 980 VAL TYR PHE PRO THR VAL ASN PHE PRO ASP VAL MET ALA
SEQRES 74 U 980 SER GLU TYR LEU GLN ALA LEU SER ASN LEU ASP SER ARG
SEQRES 75 U 980 SER PHE LYS GLN PHE PHE GLN LYS PHE ILE GLN ALA LEU
SEQRES 76 U 980 LYS SER GLY ASN VAL
SEQRES 1 C 171 GLU VAL PRO THR PHE LYS LEU VAL LEU VAL GLY ASP GLY
SEQRES 2 C 171 GLY THR GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR
SEQRES 3 C 171 GLY GLU PHE GLU LYS LYS TYR ILE ALA THR ILE GLY VAL
SEQRES 4 C 171 GLU VAL HIS PRO LEU SER PHE TYR THR ASN PHE GLY GLU
SEQRES 5 C 171 ILE LYS PHE ASP VAL TRP ASP THR ALA GLY LEU GLU LYS
SEQRES 6 C 171 PHE GLY GLY LEU ARG ASP GLY TYR TYR ILE ASN ALA GLN
SEQRES 7 C 171 CYS ALA ILE ILE MET PHE ASP VAL THR SER ARG ILE THR
SEQRES 8 C 171 TYR LYS ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG
SEQRES 9 C 171 VAL CYS GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS
SEQRES 10 C 171 VAL ASP VAL LYS GLU ARG LYS VAL LYS ALA LYS THR ILE
SEQRES 11 C 171 THR PHE HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE
SEQRES 12 C 171 SER ALA LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU
SEQRES 13 C 171 TRP LEU ALA ARG LYS LEU ALA GLY ASN PRO GLN LEU GLU
SEQRES 14 C 171 PHE VAL
SEQRES 1 E 67 G C G G A U U U A A C U C
SEQRES 2 E 67 A G U U G G G A G A G C G
SEQRES 3 E 67 C C U U C G G G A G G U C
SEQRES 4 E 67 C U G U G U U C G A U C C
SEQRES 5 E 67 A C A G A A U U C G C A C
SEQRES 6 E 67 C A
HET GTP B 250 32
HET MG B 2 1
HET GTP C 250 32
HET MG C 5 1
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 7 GTP 2(C10 H16 N5 O14 P3)
FORMUL 8 MG 2(MG 2+)
FORMUL 11 HOH *4(H2 O)
HELIX 1 1 SER T 2 LEU T 14 1 13
HELIX 2 2 GLY T 19 SER T 36 1 18
HELIX 3 3 TRP T 40 GLU T 49 1 10
HELIX 4 4 LYS T 54 GLU T 71 1 18
HELIX 5 5 ASN T 73 LEU T 95 1 23
HELIX 6 6 PRO T 101 TYR T 120 1 20
HELIX 7 7 ASP T 126 SER T 138 1 13
HELIX 8 8 GLN T 140 ASP T 160 1 21
HELIX 9 9 THR T 166 ASN T 183 1 18
HELIX 10 10 ASP T 184 ALA T 202 1 19
HELIX 11 11 ASN T 204 SER T 220 1 17
HELIX 12 12 ASN T 223 VAL T 228 1 6
HELIX 13 13 ASN T 229 LEU T 240 1 12
HELIX 14 14 ILE T 242 LYS T 259 1 18
HELIX 15 15 LYS T 262 LEU T 273 1 12
HELIX 16 16 LEU T 275 SER T 282 1 8
HELIX 17 17 ASP T 288 LYS T 310 1 23
HELIX 18 18 SER T 317 SER T 340 1 24
HELIX 19 19 TYR T 343 ALA T 349 1 7
HELIX 20 20 VAL T 350 SER T 365 1 16
HELIX 21 21 SER T 371 LYS T 390 1 20
HELIX 22 22 SER T 403 ASP T 427 1 25
HELIX 23 23 ASP T 427 THR T 448 1 22
HELIX 24 24 LEU T 449 ASN T 453 5 5
HELIX 25 25 SER T 454 GLY T 469 1 16
HELIX 26 26 THR T 487 SER T 499 1 13
HELIX 27 27 GLN T 500 HIS T 504 5 5
HELIX 28 28 HIS T 506 TYR T 520 1 15
HELIX 29 29 ALA T 521 TYR T 526 5 6
HELIX 30 30 GLU T 527 ALA T 529 5 3
HELIX 31 31 ALA T 530 GLY T 540 1 11
HELIX 32 32 ARG T 550 ILE T 566 1 17
HELIX 33 33 TYR T 573 ASN T 586 1 14
HELIX 34 34 THR T 601 ASN T 608 1 8
HELIX 35 35 ASP T 610 ILE T 625 1 16
HELIX 36 36 THR T 631 SER T 656 1 26
HELIX 37 37 ALA T 660 ALA T 678 1 19
HELIX 38 38 LYS T 679 PHE T 681 5 3
HELIX 39 39 ALA T 690 GLY T 710 1 21
HELIX 40 40 ASN T 712 GLY T 731 1 20
HELIX 41 41 PRO T 732 PRO T 736 5 5
HELIX 42 42 LYS T 737 SER T 748 1 12
HELIX 43 43 GLU T 753 TYR T 768 1 16
HELIX 44 44 LYS T 769 ASN T 771 5 3
HELIX 45 45 MET T 772 ALA T 793 1 22
HELIX 46 46 GLY T 797 GLY T 822 1 26
HELIX 47 47 GLY T 824 THR T 829 1 6
HELIX 48 48 GLU T 830 VAL T 834 5 5
HELIX 49 49 TYR T 835 ASN T 848 1 14
HELIX 50 50 PRO T 853 TRP T 870 1 18
HELIX 51 51 PHE T 879 LEU T 886 1 8
HELIX 52 52 LEU T 886 MET T 893 1 8
HELIX 53 53 PRO T 894 ASN T 896 5 3
HELIX 54 54 GLN T 905 LEU T 921 1 17
HELIX 55 55 SER T 930 VAL T 935 1 6
HELIX 56 56 VAL T 935 VAL T 940 1 6
HELIX 57 57 PRO T 943 LEU T 957 1 15
HELIX 58 58 SER T 959 SER T 975 1 17
HELIX 59 59 GLY B 24 THR B 34 1 11
HELIX 60 60 ASP B 79 ILE B 83 5 5
HELIX 61 61 ARG B 97 ASN B 102 1 6
HELIX 62 62 ASN B 102 CYS B 114 1 13
HELIX 63 63 THR B 139 LYS B 144 1 6
HELIX 64 64 GLU B 160 ALA B 171 1 12
HELIX 65 65 SER U 2 ALA U 13 1 12
HELIX 66 66 ILE U 21 ARG U 34 1 14
HELIX 67 67 GLY U 39 GLU U 49 1 11
HELIX 68 68 LYS U 54 GLU U 71 1 18
HELIX 69 69 ASN U 73 GLU U 94 1 22
HELIX 70 70 LEU U 95 ASP U 99 5 5
HELIX 71 71 PRO U 101 TYR U 120 1 20
HELIX 72 72 ASP U 126 SER U 139 1 14
HELIX 73 73 GLN U 140 ALA U 159 1 20
HELIX 74 74 THR U 166 ASP U 184 1 19
HELIX 75 75 ASP U 184 LYS U 203 1 20
HELIX 76 76 ASN U 204 SER U 220 1 17
HELIX 77 77 ASN U 223 VAL U 228 1 6
HELIX 78 78 ASN U 229 LEU U 240 1 12
HELIX 79 79 ILE U 242 LYS U 259 1 18
HELIX 80 80 LYS U 262 LEU U 273 1 12
HELIX 81 81 ASN U 274 SER U 282 1 9
HELIX 82 82 ASP U 288 ASP U 312 1 25
HELIX 83 83 SER U 317 ASP U 341 1 25
HELIX 84 84 TYR U 343 ALA U 349 1 7
HELIX 85 85 VAL U 350 GLU U 364 1 15
HELIX 86 86 SER U 371 LYS U 390 1 20
HELIX 87 87 SER U 403 ASP U 427 1 25
HELIX 88 88 ASP U 427 THR U 448 1 22
HELIX 89 89 LEU U 449 ASN U 453 5 5
HELIX 90 90 SER U 454 GLY U 469 1 16
HELIX 91 91 THR U 487 SER U 499 1 13
HELIX 92 92 HIS U 506 TYR U 520 1 15
HELIX 93 93 ALA U 521 TYR U 526 5 6
HELIX 94 94 GLU U 527 ALA U 529 5 3
HELIX 95 95 ALA U 530 GLY U 540 1 11
HELIX 96 96 ARG U 550 ILE U 566 1 17
HELIX 97 97 TYR U 573 GLY U 582 1 10
HELIX 98 98 ASP U 583 LEU U 585 5 3
HELIX 99 99 THR U 601 ARG U 607 1 7
HELIX 100 100 ASP U 610 SER U 627 1 18
HELIX 101 101 THR U 631 LEU U 654 1 24
HELIX 102 102 ALA U 660 LYS U 679 1 20
HELIX 103 103 ALA U 690 MET U 709 1 20
HELIX 104 104 ASN U 712 GLY U 731 1 20
HELIX 105 105 MET U 734 PRO U 736 5 3
HELIX 106 106 LYS U 737 LEU U 746 1 10
HELIX 107 107 ASP U 750 TYR U 768 1 19
HELIX 108 108 TYR U 768 MET U 773 1 6
HELIX 109 109 GLU U 774 ARG U 778 5 5
HELIX 110 110 MET U 779 LEU U 791 1 13
HELIX 111 111 GLY U 797 LYS U 821 1 25
HELIX 112 112 GLY U 822 PHE U 828 5 7
HELIX 113 113 THR U 829 ALA U 847 1 19
HELIX 114 114 PRO U 853 GLY U 871 1 19
HELIX 115 115 GLY U 878 LEU U 886 1 9
HELIX 116 116 LEU U 886 PHE U 891 1 6
HELIX 117 117 GLU U 892 ASN U 896 5 5
HELIX 118 118 GLN U 905 LEU U 924 1 20
HELIX 119 119 TYR U 928 VAL U 935 1 8
HELIX 120 120 SER U 948 SER U 955 1 8
HELIX 121 121 ASP U 958 SER U 975 1 18
HELIX 122 122 GLY C 24 THR C 34 1 11
HELIX 123 123 ASP C 79 ILE C 83 5 5
HELIX 124 124 ARG C 97 ASN C 102 1 6
HELIX 125 125 ASN C 102 CYS C 114 1 13
HELIX 126 126 LYS C 134 ILE C 138 5 5
HELIX 127 127 THR C 139 LYS C 144 1 6
HELIX 128 128 GLU C 160 ALA C 171 1 12
SHEET 1 A 6 VAL B 47 TYR B 55 0
SHEET 2 A 6 GLU B 60 THR B 68 -1 O PHE B 63 N LEU B 52
SHEET 3 A 6 THR B 12 GLY B 19 1 N LEU B 15 O TRP B 66
SHEET 4 A 6 CYS B 87 ASP B 93 1 O ILE B 89 N VAL B 18
SHEET 5 A 6 ILE B 119 ASN B 124 1 O CYS B 122 N ILE B 90
SHEET 6 A 6 GLN B 147 ASP B 150 1 O GLN B 147 N LEU B 121
SHEET 1 B 6 VAL C 47 LEU C 52 0
SHEET 2 B 6 LYS C 62 THR C 68 -1 O ASP C 67 N GLU C 48
SHEET 3 B 6 THR C 12 GLY C 19 1 N PHE C 13 O ASP C 64
SHEET 4 B 6 CYS C 87 ASP C 93 1 O ILE C 89 N VAL C 18
SHEET 5 B 6 ILE C 119 ASN C 124 1 O CYS C 122 N ILE C 90
SHEET 6 B 6 GLN C 147 ASP C 150 1 O TYR C 149 N GLY C 123
LINK MG MG B 2 OG1 THR B 26 1555 1555 2.09
LINK MG MG B 2 OG1 THR B 44 1555 1555 2.15
LINK MG MG B 2 OD1 ASP B 67 1555 1555 2.46
LINK MG MG B 2 O1G GTP B 250 1555 1555 2.17
LINK MG MG C 5 OG1 THR C 26 1555 1555 2.00
LINK MG MG C 5 OG1 THR C 44 1555 1555 2.23
LINK MG MG C 5 O1G GTP C 250 1555 1555 2.21
LINK MG MG C 5 O2B GTP C 250 1555 1555 2.43
SITE 1 AC1 28 HOH B 1 MG B 2 HOH B 3 GLY B 21
SITE 2 AC1 28 GLY B 22 GLY B 24 LYS B 25 THR B 26
SITE 3 AC1 28 THR B 27 PHE B 37 GLU B 38 LYS B 39
SITE 4 AC1 28 LYS B 40 TYR B 41 ILE B 42 ALA B 43
SITE 5 AC1 28 THR B 44 THR B 68 ALA B 69 GLY B 70
SITE 6 AC1 28 ASN B 124 LYS B 125 ASP B 127 SER B 152
SITE 7 AC1 28 ALA B 153 LYS B 154 THR T 798 ASP T 799
SITE 1 AC2 4 THR B 26 THR B 44 ASP B 67 GTP B 250
SITE 1 AC3 27 HOH C 4 MG C 5 HOH C 6 GLY C 21
SITE 2 AC3 27 GLY C 22 GLY C 24 LYS C 25 THR C 26
SITE 3 AC3 27 THR C 27 GLU C 38 LYS C 39 LYS C 40
SITE 4 AC3 27 TYR C 41 ILE C 42 ALA C 43 THR C 44
SITE 5 AC3 27 THR C 68 GLY C 70 ASN C 124 LYS C 125
SITE 6 AC3 27 ASP C 127 SER C 152 ALA C 153 LYS C 154
SITE 7 AC3 27 GLY U 797 THR U 798 ASP U 799
SITE 1 AC4 4 THR C 26 THR C 44 ASP C 67 GTP C 250
CRYST1 143.000 143.800 166.900 90.00 90.00 90.00 P 21 21 21 8
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 0.006993 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005992 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
