HEADER CELL CYCLE 11-FEB-01 1I2M
TITLE RAN-RCC1-SO4 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: RAN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: REGULATOR OF CHROMOSOME CONDENSATION 1;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: PROTEIN TRUNCATED FROM THE N-TERMINAL RESIDUES 1 TO 19;
COMPND 10 SYNONYM: RCC1;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: CK600K;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PTAC
KEYWDS BETA-PROPELLER, G FOLD OR GTPASE FOLD, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.RENAULT,J.KUHLMANN,A.HENKEL,A.WITTINGHOFER
REVDAT 5 09-AUG-23 1I2M 1 REMARK
REVDAT 4 14-FEB-18 1I2M 1 REMARK
REVDAT 3 04-OCT-17 1I2M 1 REMARK
REVDAT 2 24-FEB-09 1I2M 1 VERSN
REVDAT 1 02-MAY-01 1I2M 0
JRNL AUTH L.RENAULT,J.KUHLMANN,A.HENKEL,A.WITTINGHOFER
JRNL TITL STRUCTURAL BASIS FOR GUANINE NUCLEOTIDE EXCHANGE ON RAN BY
JRNL TITL 2 THE REGULATOR OF CHROMOSOME CONDENSATION (RCC1).
JRNL REF CELL(CAMBRIDGE,MASS.) V. 105 245 2001
JRNL REFN ISSN 0092-8674
JRNL PMID 11336674
JRNL DOI 10.1016/S0092-8674(01)00315-4
REMARK 2
REMARK 2 RESOLUTION. 1.76 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 101433
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) : 0.192
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.300
REMARK 3 FREE R VALUE TEST SET COUNT : 8466
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4487
REMARK 3 BIN R VALUE (WORKING SET) : 0.3043
REMARK 3 BIN FREE R VALUE : 0.3314
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 417
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8499
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 475
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.55000
REMARK 3 B22 (A**2) : -3.20000
REMARK 3 B33 (A**2) : 4.75000
REMARK 3 B12 (A**2) : 1.41000
REMARK 3 B13 (A**2) : 0.77000
REMARK 3 B23 (A**2) : -0.23000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.21
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.23
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
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) : 3.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.020 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.760 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.820 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 53.12
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-01.
REMARK 100 THE DEPOSITION ID IS D_1000012825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-99; 14-JUL-99
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ESRF; ESRF
REMARK 200 BEAMLINE : BM30A; ID2
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801; 0.9903
REMARK 200 MONOCHROMATOR : SI 111 AND 311 SINGLE CRYSTALS;
REMARK 200 SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS; MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 484600
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 19.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : 0.31600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1A12 (RCC1) AND HUMAN RAN-GDP-MG2+
REMARK 200 STRUCTURE (SCHEFFZEK, K. ET AL. (1995))
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-10% PEG 4000, 200 MM POTASSIUM
REMARK 280 FLUORIDE, 25 MM POTASSIUM PHOSPHATE, 25 MM AMMONIUM SULFATE, 2
REMARK 280 MM EDTA, 3MM DTE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 ALA A 2
REMARK 465 ALA A 3
REMARK 465 GLN A 4
REMARK 465 GLY A 5
REMARK 465 GLU A 6
REMARK 465 PRO A 7
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLU A 34
REMARK 465 PHE A 35
REMARK 465 GLU A 36
REMARK 465 ALA A 178
REMARK 465 MET A 179
REMARK 465 PRO A 180
REMARK 465 ALA A 181
REMARK 465 LEU A 182
REMARK 465 ALA A 183
REMARK 465 PRO A 184
REMARK 465 PRO A 185
REMARK 465 GLU A 186
REMARK 465 VAL A 187
REMARK 465 VAL A 188
REMARK 465 MET A 189
REMARK 465 ASP A 190
REMARK 465 PRO A 191
REMARK 465 ALA A 192
REMARK 465 LEU A 193
REMARK 465 ALA A 194
REMARK 465 ALA A 195
REMARK 465 GLN A 196
REMARK 465 TYR A 197
REMARK 465 GLU A 198
REMARK 465 HIS A 199
REMARK 465 ASP A 200
REMARK 465 LEU A 201
REMARK 465 GLU A 202
REMARK 465 VAL A 203
REMARK 465 ALA A 204
REMARK 465 GLN A 205
REMARK 465 THR A 206
REMARK 465 THR A 207
REMARK 465 ALA A 208
REMARK 465 LEU A 209
REMARK 465 PRO A 210
REMARK 465 ASP A 211
REMARK 465 GLU A 212
REMARK 465 ASP A 213
REMARK 465 ASP A 214
REMARK 465 ASP A 215
REMARK 465 LEU A 216
REMARK 465 SER B 20
REMARK 465 LYS B 21
REMARK 465 LYS B 22
REMARK 465 VAL B 23
REMARK 465 SER B 233
REMARK 465 ARG B 234
REMARK 465 GLY B 235
REMARK 465 SER B 236
REMARK 465 ARG B 237
REMARK 465 GLY B 238
REMARK 465 LYS B 418
REMARK 465 GLU B 419
REMARK 465 GLN B 420
REMARK 465 SER B 421
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 GLN C 4
REMARK 465 GLY C 5
REMARK 465 GLU C 6
REMARK 465 PRO C 7
REMARK 465 THR C 32
REMARK 465 GLY C 33
REMARK 465 GLU C 34
REMARK 465 PHE C 35
REMARK 465 GLU C 36
REMARK 465 LYS C 37
REMARK 465 ALA C 178
REMARK 465 MET C 179
REMARK 465 PRO C 180
REMARK 465 ALA C 181
REMARK 465 LEU C 182
REMARK 465 ALA C 183
REMARK 465 PRO C 184
REMARK 465 PRO C 185
REMARK 465 GLU C 186
REMARK 465 VAL C 187
REMARK 465 VAL C 188
REMARK 465 MET C 189
REMARK 465 ASP C 190
REMARK 465 PRO C 191
REMARK 465 ALA C 192
REMARK 465 LEU C 193
REMARK 465 ALA C 194
REMARK 465 ALA C 195
REMARK 465 GLN C 196
REMARK 465 TYR C 197
REMARK 465 GLU C 198
REMARK 465 HIS C 199
REMARK 465 ASP C 200
REMARK 465 LEU C 201
REMARK 465 GLU C 202
REMARK 465 VAL C 203
REMARK 465 ALA C 204
REMARK 465 GLN C 205
REMARK 465 THR C 206
REMARK 465 THR C 207
REMARK 465 ALA C 208
REMARK 465 LEU C 209
REMARK 465 PRO C 210
REMARK 465 ASP C 211
REMARK 465 GLU C 212
REMARK 465 ASP C 213
REMARK 465 ASP C 214
REMARK 465 ASP C 215
REMARK 465 LEU C 216
REMARK 465 SER D 20
REMARK 465 LYS D 21
REMARK 465 LYS D 22
REMARK 465 VAL D 23
REMARK 465 SER D 233
REMARK 465 ARG D 234
REMARK 465 GLY D 235
REMARK 465 SER D 236
REMARK 465 ARG D 237
REMARK 465 GLY D 238
REMARK 465 GLN D 420
REMARK 465 SER D 421
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 ARG A 76 -127.38 55.31
REMARK 500 ARG A 95 -6.36 -59.12
REMARK 500 GLU A 113 -138.06 83.23
REMARK 500 ILE A 126 46.02 -73.37
REMARK 500 LYS A 127 71.43 -152.13
REMARK 500 ASP A 128 104.96 164.00
REMARK 500 LYS A 130 54.56 -142.69
REMARK 500 ALA A 133 -34.17 -133.72
REMARK 500 ARG A 140 -155.78 -72.02
REMARK 500 LYS A 141 -100.02 75.56
REMARK 500 LYS A 142 -26.96 114.45
REMARK 500 LYS A 152 107.39 134.48
REMARK 500 ASN A 154 37.23 36.96
REMARK 500 ASN A 156 13.88 54.69
REMARK 500 ASP B 148 -166.50 -127.26
REMARK 500 LEU B 155 -75.82 -114.87
REMARK 500 ARG B 206 10.94 -149.75
REMARK 500 SER B 267 32.34 -148.99
REMARK 500 ASN B 291 -127.84 -72.44
REMARK 500 SER B 292 -56.85 151.79
REMARK 500 ARG B 343 29.73 -77.53
REMARK 500 SER B 355 25.81 -140.16
REMARK 500 TYR C 39 128.52 53.71
REMARK 500 ARG C 76 -124.38 52.05
REMARK 500 GLU C 113 -116.34 77.13
REMARK 500 ASN C 114 19.31 -66.81
REMARK 500 VAL C 124 168.95 -47.31
REMARK 500 ASP C 125 67.36 -33.66
REMARK 500 ILE C 126 81.09 162.37
REMARK 500 LYS C 127 48.34 -64.06
REMARK 500 ASP C 128 75.53 -106.99
REMARK 500 LYS C 132 0.35 40.96
REMARK 500 ARG C 140 -76.09 -41.78
REMARK 500 LYS C 141 -137.24 10.34
REMARK 500 LYS C 142 -72.51 -166.39
REMARK 500 ASN C 143 -86.58 -41.67
REMARK 500 ASN C 156 19.28 53.80
REMARK 500 PRO D 66 -1.61 -57.87
REMARK 500 MET D 77 32.71 -140.58
REMARK 500 ASP D 148 -168.10 -123.50
REMARK 500 ASN D 149 3.60 -67.62
REMARK 500 LEU D 155 -76.81 -115.59
REMARK 500 MET D 159 13.82 58.67
REMARK 500 ARG D 206 10.97 -152.22
REMARK 500 ARG D 217 13.17 85.31
REMARK 500 GLN D 218 -140.34 -133.08
REMARK 500 LEU D 231 148.00 172.68
REMARK 500 SER D 267 32.85 -147.13
REMARK 500 ARG D 343 46.65 -82.76
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 SO4 A 1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2250
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A12 RELATED DB: PDB
REMARK 900 1A12 CONTAINS THE REGULATOR OF CHROMOSOME CONDENSATION 1 (HUMAN
REMARK 900 RCC1) SOLVED ALONE
REMARK 900 RELATED ID: 1BYU RELATED DB: PDB
REMARK 900 1BYU CONTAINS THE SMALL NUCLEAR GTP-BINDING PROTEIN RAN (CANINE RAN)
REMARK 900 COMPLEXED WITH GDP-MG2+
REMARK 900 RELATED ID: 1RRP RELATED DB: PDB
REMARK 900 1RRP CONTAINS THE SMALL NUCLEAR GTP-BINDING PROTEIN RAN (HUMAN RAN)
REMARK 900 COMPLEXED WITH GPPNHP-MG2+ AND THE EFFECTOR RANBD1
DBREF 1I2M A 1 216 UNP P62826 RAN_HUMAN 1 216
DBREF 1I2M C 1 216 UNP P62826 RAN_HUMAN 1 216
DBREF 1I2M B 20 421 UNP P18754 RCC1_HUMAN 20 421
DBREF 1I2M D 20 421 UNP P18754 RCC1_HUMAN 20 421
SEQADV 1I2M ARG A 129 UNP P62826 SER 129 SEE REMARK 999
SEQADV 1I2M ARG C 129 UNP P62826 SER 129 SEE REMARK 999
SEQRES 1 A 216 MET ALA ALA GLN GLY GLU PRO GLN VAL GLN PHE LYS LEU
SEQRES 2 A 216 VAL LEU VAL GLY ASP GLY GLY THR GLY LYS THR THR PHE
SEQRES 3 A 216 VAL LYS ARG HIS LEU THR GLY GLU PHE GLU LYS LYS TYR
SEQRES 4 A 216 VAL ALA THR LEU GLY VAL GLU VAL HIS PRO LEU VAL PHE
SEQRES 5 A 216 HIS THR ASN ARG GLY PRO ILE LYS PHE ASN VAL TRP ASP
SEQRES 6 A 216 THR ALA GLY GLN GLU LYS PHE GLY GLY LEU ARG ASP GLY
SEQRES 7 A 216 TYR TYR ILE GLN ALA GLN CYS ALA ILE ILE MET PHE ASP
SEQRES 8 A 216 VAL THR SER ARG VAL THR TYR LYS ASN VAL PRO ASN TRP
SEQRES 9 A 216 HIS ARG ASP LEU VAL ARG VAL CYS GLU ASN ILE PRO ILE
SEQRES 10 A 216 VAL LEU CYS GLY ASN LYS VAL ASP ILE LYS ASP ARG LYS
SEQRES 11 A 216 VAL LYS ALA LYS SER ILE VAL PHE HIS ARG LYS LYS ASN
SEQRES 12 A 216 LEU GLN TYR TYR ASP ILE SER ALA LYS SER ASN TYR ASN
SEQRES 13 A 216 PHE GLU LYS PRO PHE LEU TRP LEU ALA ARG LYS LEU ILE
SEQRES 14 A 216 GLY ASP PRO ASN LEU GLU PHE VAL ALA MET PRO ALA LEU
SEQRES 15 A 216 ALA PRO PRO GLU VAL VAL MET ASP PRO ALA LEU ALA ALA
SEQRES 16 A 216 GLN TYR GLU HIS ASP LEU GLU VAL ALA GLN THR THR ALA
SEQRES 17 A 216 LEU PRO ASP GLU ASP ASP ASP LEU
SEQRES 1 B 402 SER LYS LYS VAL LYS VAL SER HIS ARG SER HIS SER THR
SEQRES 2 B 402 GLU PRO GLY LEU VAL LEU THR LEU GLY GLN GLY ASP VAL
SEQRES 3 B 402 GLY GLN LEU GLY LEU GLY GLU ASN VAL MET GLU ARG LYS
SEQRES 4 B 402 LYS PRO ALA LEU VAL SER ILE PRO GLU ASP VAL VAL GLN
SEQRES 5 B 402 ALA GLU ALA GLY GLY MET HIS THR VAL CYS LEU SER LYS
SEQRES 6 B 402 SER GLY GLN VAL TYR SER PHE GLY CYS ASN ASP GLU GLY
SEQRES 7 B 402 ALA LEU GLY ARG ASP THR SER VAL GLU GLY SER GLU MET
SEQRES 8 B 402 VAL PRO GLY LYS VAL GLU LEU GLN GLU LYS VAL VAL GLN
SEQRES 9 B 402 VAL SER ALA GLY ASP SER HIS THR ALA ALA LEU THR ASP
SEQRES 10 B 402 ASP GLY ARG VAL PHE LEU TRP GLY SER PHE ARG ASP ASN
SEQRES 11 B 402 ASN GLY VAL ILE GLY LEU LEU GLU PRO MET LYS LYS SER
SEQRES 12 B 402 MET VAL PRO VAL GLN VAL GLN LEU ASP VAL PRO VAL VAL
SEQRES 13 B 402 LYS VAL ALA SER GLY ASN ASP HIS LEU VAL MET LEU THR
SEQRES 14 B 402 ALA ASP GLY ASP LEU TYR THR LEU GLY CYS GLY GLU GLN
SEQRES 15 B 402 GLY GLN LEU GLY ARG VAL PRO GLU LEU PHE ALA ASN ARG
SEQRES 16 B 402 GLY GLY ARG GLN GLY LEU GLU ARG LEU LEU VAL PRO LYS
SEQRES 17 B 402 CYS VAL MET LEU LYS SER ARG GLY SER ARG GLY HIS VAL
SEQRES 18 B 402 ARG PHE GLN ASP ALA PHE CYS GLY ALA TYR PHE THR PHE
SEQRES 19 B 402 ALA ILE SER HIS GLU GLY HIS VAL TYR GLY PHE GLY LEU
SEQRES 20 B 402 SER ASN TYR HIS GLN LEU GLY THR PRO GLY THR GLU SER
SEQRES 21 B 402 CYS PHE ILE PRO GLN ASN LEU THR SER PHE LYS ASN SER
SEQRES 22 B 402 THR LYS SER TRP VAL GLY PHE SER GLY GLY GLN HIS HIS
SEQRES 23 B 402 THR VAL CYS MET ASP SER GLU GLY LYS ALA TYR SER LEU
SEQRES 24 B 402 GLY ARG ALA GLU TYR GLY ARG LEU GLY LEU GLY GLU GLY
SEQRES 25 B 402 ALA GLU GLU LYS SER ILE PRO THR LEU ILE SER ARG LEU
SEQRES 26 B 402 PRO ALA VAL SER SER VAL ALA CYS GLY ALA SER VAL GLY
SEQRES 27 B 402 TYR ALA VAL THR LYS ASP GLY ARG VAL PHE ALA TRP GLY
SEQRES 28 B 402 MET GLY THR ASN TYR GLN LEU GLY THR GLY GLN ASP GLU
SEQRES 29 B 402 ASP ALA TRP SER PRO VAL GLU MET MET GLY LYS GLN LEU
SEQRES 30 B 402 GLU ASN ARG VAL VAL LEU SER VAL SER SER GLY GLY GLN
SEQRES 31 B 402 HIS THR VAL LEU LEU VAL LYS ASP LYS GLU GLN SER
SEQRES 1 C 216 MET ALA ALA GLN GLY GLU PRO GLN VAL GLN PHE LYS LEU
SEQRES 2 C 216 VAL LEU VAL GLY ASP GLY GLY THR GLY LYS THR THR PHE
SEQRES 3 C 216 VAL LYS ARG HIS LEU THR GLY GLU PHE GLU LYS LYS TYR
SEQRES 4 C 216 VAL ALA THR LEU GLY VAL GLU VAL HIS PRO LEU VAL PHE
SEQRES 5 C 216 HIS THR ASN ARG GLY PRO ILE LYS PHE ASN VAL TRP ASP
SEQRES 6 C 216 THR ALA GLY GLN GLU LYS PHE GLY GLY LEU ARG ASP GLY
SEQRES 7 C 216 TYR TYR ILE GLN ALA GLN CYS ALA ILE ILE MET PHE ASP
SEQRES 8 C 216 VAL THR SER ARG VAL THR TYR LYS ASN VAL PRO ASN TRP
SEQRES 9 C 216 HIS ARG ASP LEU VAL ARG VAL CYS GLU ASN ILE PRO ILE
SEQRES 10 C 216 VAL LEU CYS GLY ASN LYS VAL ASP ILE LYS ASP ARG LYS
SEQRES 11 C 216 VAL LYS ALA LYS SER ILE VAL PHE HIS ARG LYS LYS ASN
SEQRES 12 C 216 LEU GLN TYR TYR ASP ILE SER ALA LYS SER ASN TYR ASN
SEQRES 13 C 216 PHE GLU LYS PRO PHE LEU TRP LEU ALA ARG LYS LEU ILE
SEQRES 14 C 216 GLY ASP PRO ASN LEU GLU PHE VAL ALA MET PRO ALA LEU
SEQRES 15 C 216 ALA PRO PRO GLU VAL VAL MET ASP PRO ALA LEU ALA ALA
SEQRES 16 C 216 GLN TYR GLU HIS ASP LEU GLU VAL ALA GLN THR THR ALA
SEQRES 17 C 216 LEU PRO ASP GLU ASP ASP ASP LEU
SEQRES 1 D 402 SER LYS LYS VAL LYS VAL SER HIS ARG SER HIS SER THR
SEQRES 2 D 402 GLU PRO GLY LEU VAL LEU THR LEU GLY GLN GLY ASP VAL
SEQRES 3 D 402 GLY GLN LEU GLY LEU GLY GLU ASN VAL MET GLU ARG LYS
SEQRES 4 D 402 LYS PRO ALA LEU VAL SER ILE PRO GLU ASP VAL VAL GLN
SEQRES 5 D 402 ALA GLU ALA GLY GLY MET HIS THR VAL CYS LEU SER LYS
SEQRES 6 D 402 SER GLY GLN VAL TYR SER PHE GLY CYS ASN ASP GLU GLY
SEQRES 7 D 402 ALA LEU GLY ARG ASP THR SER VAL GLU GLY SER GLU MET
SEQRES 8 D 402 VAL PRO GLY LYS VAL GLU LEU GLN GLU LYS VAL VAL GLN
SEQRES 9 D 402 VAL SER ALA GLY ASP SER HIS THR ALA ALA LEU THR ASP
SEQRES 10 D 402 ASP GLY ARG VAL PHE LEU TRP GLY SER PHE ARG ASP ASN
SEQRES 11 D 402 ASN GLY VAL ILE GLY LEU LEU GLU PRO MET LYS LYS SER
SEQRES 12 D 402 MET VAL PRO VAL GLN VAL GLN LEU ASP VAL PRO VAL VAL
SEQRES 13 D 402 LYS VAL ALA SER GLY ASN ASP HIS LEU VAL MET LEU THR
SEQRES 14 D 402 ALA ASP GLY ASP LEU TYR THR LEU GLY CYS GLY GLU GLN
SEQRES 15 D 402 GLY GLN LEU GLY ARG VAL PRO GLU LEU PHE ALA ASN ARG
SEQRES 16 D 402 GLY GLY ARG GLN GLY LEU GLU ARG LEU LEU VAL PRO LYS
SEQRES 17 D 402 CYS VAL MET LEU LYS SER ARG GLY SER ARG GLY HIS VAL
SEQRES 18 D 402 ARG PHE GLN ASP ALA PHE CYS GLY ALA TYR PHE THR PHE
SEQRES 19 D 402 ALA ILE SER HIS GLU GLY HIS VAL TYR GLY PHE GLY LEU
SEQRES 20 D 402 SER ASN TYR HIS GLN LEU GLY THR PRO GLY THR GLU SER
SEQRES 21 D 402 CYS PHE ILE PRO GLN ASN LEU THR SER PHE LYS ASN SER
SEQRES 22 D 402 THR LYS SER TRP VAL GLY PHE SER GLY GLY GLN HIS HIS
SEQRES 23 D 402 THR VAL CYS MET ASP SER GLU GLY LYS ALA TYR SER LEU
SEQRES 24 D 402 GLY ARG ALA GLU TYR GLY ARG LEU GLY LEU GLY GLU GLY
SEQRES 25 D 402 ALA GLU GLU LYS SER ILE PRO THR LEU ILE SER ARG LEU
SEQRES 26 D 402 PRO ALA VAL SER SER VAL ALA CYS GLY ALA SER VAL GLY
SEQRES 27 D 402 TYR ALA VAL THR LYS ASP GLY ARG VAL PHE ALA TRP GLY
SEQRES 28 D 402 MET GLY THR ASN TYR GLN LEU GLY THR GLY GLN ASP GLU
SEQRES 29 D 402 ASP ALA TRP SER PRO VAL GLU MET MET GLY LYS GLN LEU
SEQRES 30 D 402 GLU ASN ARG VAL VAL LEU SER VAL SER SER GLY GLY GLN
SEQRES 31 D 402 HIS THR VAL LEU LEU VAL LYS ASP LYS GLU GLN SER
HET SO4 A1250 5
HET SO4 C2250 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *475(H2 O)
HELIX 1 1 GLY A 22 ARG A 29 1 8
HELIX 2 2 GLY A 68 GLY A 73 1 6
HELIX 3 3 LEU A 75 TYR A 80 5 6
HELIX 4 4 SER A 94 LYS A 99 5 6
HELIX 5 5 ASN A 100 GLU A 113 1 14
HELIX 6 6 SER A 135 ARG A 140 1 6
HELIX 7 7 GLU A 158 GLY A 170 1 13
HELIX 8 8 GLY B 107 VAL B 111 5 5
HELIX 9 9 PRO B 208 ALA B 212 5 5
HELIX 10 10 GLY B 215 GLY B 219 5 5
HELIX 11 11 LEU B 220 VAL B 225 1 6
HELIX 12 12 THR B 287 LYS B 290 5 4
HELIX 13 13 ALA B 321 ARG B 325 5 5
HELIX 14 14 GLY B 393 GLU B 397 5 5
HELIX 15 15 GLY C 22 ARG C 29 1 8
HELIX 16 16 GLY C 68 GLY C 73 1 6
HELIX 17 17 ASP C 77 GLN C 82 1 6
HELIX 18 18 SER C 94 LYS C 99 5 6
HELIX 19 19 ASN C 100 CYS C 112 1 13
HELIX 20 20 SER C 135 LYS C 141 1 7
HELIX 21 21 ALA C 151 ASN C 154 5 4
HELIX 22 22 GLU C 158 GLY C 170 1 13
HELIX 23 23 GLY D 107 VAL D 111 5 5
HELIX 24 24 LEU D 220 VAL D 225 1 6
HELIX 25 25 THR D 287 LYS D 290 5 4
HELIX 26 26 ALA D 321 ARG D 325 5 5
HELIX 27 27 GLY D 393 GLU D 397 5 5
SHEET 1 A 7 TYR A 39 THR A 42 0
SHEET 2 A 7 VAL A 45 PHE A 52 -1 N VAL A 45 O THR A 42
SHEET 3 A 7 ILE A 59 ASP A 65 -1 O ILE A 59 N PHE A 52
SHEET 4 A 7 VAL A 9 GLY A 17 1 O VAL A 9 N LYS A 60
SHEET 5 A 7 CYS A 85 ASP A 91 1 O CYS A 85 N VAL A 14
SHEET 6 A 7 ILE A 117 ASN A 122 1 O VAL A 118 N ILE A 88
SHEET 7 A 7 GLN A 145 ILE A 149 1 O GLN A 145 N LEU A 119
SHEET 1 B 4 GLU B 56 VAL B 63 0
SHEET 2 B 4 LEU B 36 GLN B 42 -1 O VAL B 37 N VAL B 63
SHEET 3 B 4 HIS B 410 LYS B 416 -1 N THR B 411 O LEU B 40
SHEET 4 B 4 VAL B 400 SER B 406 -1 N VAL B 400 O LYS B 416
SHEET 1 C 4 VAL B 69 ALA B 74 0
SHEET 2 C 4 HIS B 78 SER B 83 -1 O VAL B 80 N GLU B 73
SHEET 3 C 4 VAL B 88 GLY B 92 -1 O TYR B 89 N CYS B 81
SHEET 4 C 4 GLY B 113 LYS B 114 -1 O GLY B 113 N SER B 90
SHEET 1 D 4 VAL B 121 ALA B 126 0
SHEET 2 D 4 HIS B 130 THR B 135 -1 N ALA B 132 O SER B 125
SHEET 3 D 4 VAL B 140 GLY B 144 -1 N PHE B 141 O ALA B 133
SHEET 4 D 4 SER B 162 VAL B 168 -1 O SER B 162 N GLY B 144
SHEET 1 E 2 PHE B 146 ASP B 148 0
SHEET 2 E 2 GLY B 151 GLY B 154 -1 O GLY B 151 N ASP B 148
SHEET 1 F 4 VAL B 174 SER B 179 0
SHEET 2 F 4 HIS B 183 THR B 188 -1 N VAL B 185 O ALA B 178
SHEET 3 F 4 LEU B 193 GLY B 197 -1 O TYR B 194 N MET B 186
SHEET 4 F 4 LYS B 227 CYS B 228 -1 O LYS B 227 N THR B 195
SHEET 1 G 4 PHE B 242 CYS B 247 0
SHEET 2 G 4 PHE B 251 SER B 256 -1 O PHE B 253 N PHE B 246
SHEET 3 G 4 VAL B 261 LEU B 266 -1 N TYR B 262 O ALA B 254
SHEET 4 G 4 SER B 279 ASN B 285 -1 N CYS B 280 O GLY B 265
SHEET 1 H 4 TRP B 296 GLY B 301 0
SHEET 2 H 4 HIS B 305 ASP B 310 -1 N VAL B 307 O SER B 300
SHEET 3 H 4 ALA B 315 GLY B 319 -1 N TYR B 316 O CYS B 308
SHEET 4 H 4 LYS B 335 LEU B 340 -1 O LYS B 335 N GLY B 319
SHEET 1 I 4 VAL B 347 CYS B 352 0
SHEET 2 I 4 VAL B 356 THR B 361 -1 N TYR B 358 O ALA B 351
SHEET 3 I 4 VAL B 366 GLY B 370 -1 N PHE B 367 O ALA B 359
SHEET 4 I 4 ALA B 385 GLU B 390 -1 O ALA B 385 N GLY B 370
SHEET 1 J 6 HIS C 48 PHE C 52 0
SHEET 2 J 6 ILE C 59 ASP C 65 -1 N ILE C 59 O PHE C 52
SHEET 3 J 6 VAL C 9 GLY C 17 1 O VAL C 9 N LYS C 60
SHEET 4 J 6 CYS C 85 ASP C 91 1 O CYS C 85 N VAL C 14
SHEET 5 J 6 ILE C 117 ASN C 122 1 O VAL C 118 N ILE C 88
SHEET 6 J 6 GLN C 145 ILE C 149 1 O GLN C 145 N LEU C 119
SHEET 1 K 4 GLU D 56 LEU D 62 0
SHEET 2 K 4 LEU D 36 GLN D 42 -1 O THR D 39 N ALA D 61
SHEET 3 K 4 HIS D 410 ASP D 417 -1 N THR D 411 O LEU D 40
SHEET 4 K 4 ARG D 399 SER D 406 -1 N VAL D 400 O LYS D 416
SHEET 1 L 4 VAL D 69 ALA D 74 0
SHEET 2 L 4 HIS D 78 SER D 83 -1 O VAL D 80 N GLU D 73
SHEET 3 L 4 VAL D 88 GLY D 92 -1 N TYR D 89 O CYS D 81
SHEET 4 L 4 GLY D 113 LYS D 114 -1 O GLY D 113 N SER D 90
SHEET 1 M 4 VAL D 121 ALA D 126 0
SHEET 2 M 4 HIS D 130 THR D 135 -1 N ALA D 132 O SER D 125
SHEET 3 M 4 VAL D 140 GLY D 144 -1 N PHE D 141 O ALA D 133
SHEET 4 M 4 SER D 162 GLN D 167 -1 O SER D 162 N GLY D 144
SHEET 1 N 2 PHE D 146 ASP D 148 0
SHEET 2 N 2 GLY D 151 GLY D 154 -1 O GLY D 151 N ASP D 148
SHEET 1 O 4 VAL D 174 SER D 179 0
SHEET 2 O 4 HIS D 183 THR D 188 -1 N VAL D 185 O ALA D 178
SHEET 3 O 4 LEU D 193 GLY D 197 -1 O TYR D 194 N MET D 186
SHEET 4 O 4 LYS D 227 CYS D 228 -1 O LYS D 227 N THR D 195
SHEET 1 P 4 PHE D 242 CYS D 247 0
SHEET 2 P 4 PHE D 251 SER D 256 -1 O PHE D 253 N PHE D 246
SHEET 3 P 4 VAL D 261 GLY D 265 -1 N TYR D 262 O ALA D 254
SHEET 4 P 4 CYS D 280 ASN D 285 -1 O CYS D 280 N GLY D 265
SHEET 1 Q 4 TRP D 296 GLY D 301 0
SHEET 2 Q 4 HIS D 305 ASP D 310 -1 N VAL D 307 O SER D 300
SHEET 3 Q 4 ALA D 315 GLY D 319 -1 N TYR D 316 O CYS D 308
SHEET 4 Q 4 LYS D 335 LEU D 340 -1 O LYS D 335 N GLY D 319
SHEET 1 R 4 VAL D 347 CYS D 352 0
SHEET 2 R 4 VAL D 356 THR D 361 -1 N TYR D 358 O ALA D 351
SHEET 3 R 4 VAL D 366 GLY D 370 -1 N PHE D 367 O ALA D 359
SHEET 4 R 4 ALA D 385 GLU D 390 -1 O ALA D 385 N GLY D 370
SITE 1 AC1 9 ASP A 18 GLY A 19 GLY A 20 THR A 21
SITE 2 AC1 9 GLY A 22 LYS A 23 THR A 24 HOH A1284
SITE 3 AC1 9 HOH A1286
SITE 1 AC2 9 ARG B 217 GLY C 20 THR C 21 GLY C 22
SITE 2 AC2 9 LYS C 23 THR C 24 HOH C2289 HOH C2301
SITE 3 AC2 9 HOH C2302
CRYST1 50.334 71.447 77.729 100.92 92.05 104.47 P 1 2
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 0.019867 0.005129 0.001799 0.00000
SCALE2 0.000000 0.014455 0.003027 0.00000
SCALE3 0.000000 0.000000 0.013153 0.00000
(ATOM LINES ARE NOT SHOWN.)
END