HEADER CELL CYCLE 19-JUL-07 2QNR
TITLE HUMAN SEPTIN 2 IN COMPLEX WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEPTIN-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 22-320;
COMPND 5 SYNONYM: PROTEIN NEDD5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SEPT2, DIFF6, KIAA0158, NEDD5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC
KEYWDS SEPTIN, STRUCTURAL GENOMICS CONSORTIUM, SGC, MITOSIS, GDP, CELL
KEYWDS 2 CYCLE, CELL DIVISION, GTP-BINDING, NUCLEOTIDE-BINDING,
KEYWDS 3 PHOSPHORYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR W.M.RABEH,L.NEDYALKOVA,W.TEMPEL,R.LANDRY,L.CROMBET,I.KOZIERADZKI,
AUTHOR 2 G.SENISTERRA,M.VEDADI,C.H.ARROWSMITH,A.M.EDWARDS,M.SUNDSTROM,
AUTHOR 3 J.WEIGELT,A.BOCHKAREV,H.PARK,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 25-OCT-17 2QNR 1 REMARK
REVDAT 4 13-JUL-11 2QNR 1 VERSN
REVDAT 3 24-FEB-09 2QNR 1 VERSN
REVDAT 2 21-AUG-07 2QNR 1 REMARK
REVDAT 1 31-JUL-07 2QNR 0
JRNL AUTH W.M.RABEH,L.NEDYALKOVA,W.TEMPEL,R.LANDRY,L.CROMBET,
JRNL AUTH 2 I.KOZIERADZKI,G.SENISTERRA,M.VEDADI,C.H.ARROWSMITH,
JRNL AUTH 3 A.M.EDWARDS,M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK
JRNL TITL HUMAN SEPTIN 2 IN COMPLEX WITH GDP.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 21100
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1036
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1366
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.4470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3515
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.87000
REMARK 3 B22 (A**2) : 0.94000
REMARK 3 B33 (A**2) : -3.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.491
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.330
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.290
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.037
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.905
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3632 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2413 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4921 ; 1.388 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5882 ; 0.889 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 442 ; 6.062 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;38.412 ;23.487
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;16.616 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.289 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 580 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3925 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 729 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 766 ; 0.225 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2426 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1757 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1986 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 78 ; 0.157 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 27 ; 0.341 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.179 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2325 ; 2.435 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 908 ; 0.516 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3620 ; 3.431 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1495 ; 2.324 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1301 ; 3.272 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 37 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): 59.9240 11.7990 8.0290
REMARK 3 T TENSOR
REMARK 3 T11: 0.2956 T22: 0.3727
REMARK 3 T33: 0.1444 T12: 0.0341
REMARK 3 T13: -0.0321 T23: -0.0751
REMARK 3 L TENSOR
REMARK 3 L11: 1.1934 L22: 1.3801
REMARK 3 L33: 7.7608 L12: 0.3281
REMARK 3 L13: -2.1672 L23: -0.7029
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.1126 S13: 0.2150
REMARK 3 S21: 0.1794 S22: 0.0448 S23: -0.0697
REMARK 3 S31: -0.1816 S32: -0.0987 S33: -0.0821
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 36 B 306
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6710 -1.5540 -27.6070
REMARK 3 T TENSOR
REMARK 3 T11: 0.3032 T22: 0.4065
REMARK 3 T33: 0.0775 T12: 0.0406
REMARK 3 T13: 0.0407 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.9423 L22: 3.1958
REMARK 3 L33: 4.5525 L12: 1.7210
REMARK 3 L13: 1.6760 L23: 2.8794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0432 S12: 0.2101 S13: -0.0346
REMARK 3 S21: -0.2275 S22: 0.0184 S23: -0.2062
REMARK 3 S31: -0.1079 S32: 0.0148 S33: -0.0615
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. COOT, O, MOLPROBITY PROGRAMS HAVE ALSO BEEN
REMARK 3 USED IN THE REFINEMENT. 3. ATOMIC B-FACTORS SHOWN ARE RESIDUALS
REMARK 3 FROM TLS REFINEMENT. 4. CAVEAT: RESIDUES 84-89 IN CHAIN A AND 74-
REMARK 3 90 IN CHAIN B COULD NOT BE RELIABLY ASSIGNED IN THE AMINO ACID
REMARK 3 SEQUENCE AND WERE MODELED AS ALANINES.
REMARK 4
REMARK 4 2QNR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043829.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97770
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22998
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 0.2M TRILITHIUM CITRATE,
REMARK 280 0.1M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 82.26800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.14750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 82.26800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.14750
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 PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION
REMARK 300 ON BURIED SURFACE AREA.
REMARK 300 AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN
REMARK 300 IS UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3530 ANGSTROM**2
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 20
REMARK 465 SER A 21
REMARK 465 ASN A 22
REMARK 465 LEU A 23
REMARK 465 PRO A 24
REMARK 465 ASN A 25
REMARK 465 GLN A 26
REMARK 465 VAL A 27
REMARK 465 HIS A 28
REMARK 465 ARG A 29
REMARK 465 LYS A 30
REMARK 465 SER A 31
REMARK 465 VAL A 32
REMARK 465 LYS A 33
REMARK 465 LYS A 34
REMARK 465 GLY A 35
REMARK 465 PHE A 36
REMARK 465 THR A 60
REMARK 465 ASP A 61
REMARK 465 LEU A 62
REMARK 465 TYR A 63
REMARK 465 PRO A 64
REMARK 465 GLU A 65
REMARK 465 ARG A 66
REMARK 465 VAL A 67
REMARK 465 ILE A 68
REMARK 465 SER A 69
REMARK 465 GLY A 70
REMARK 465 ALA A 71
REMARK 465 ALA A 72
REMARK 465 GLU A 73
REMARK 465 LYS A 74
REMARK 465 ILE A 75
REMARK 465 GLU A 76
REMARK 465 ARG A 77
REMARK 465 THR A 78
REMARK 465 VAL A 79
REMARK 465 GLN A 80
REMARK 465 ILE A 81
REMARK 465 GLU A 82
REMARK 465 ALA A 83
REMARK 465 GLU A 90
REMARK 465 ARG A 91
REMARK 465 GLY A 92
REMARK 465 GLY A 104
REMARK 465 TYR A 105
REMARK 465 GLY A 106
REMARK 465 ASP A 107
REMARK 465 ALA A 108
REMARK 465 ILE A 109
REMARK 465 ASN A 110
REMARK 465 CYS A 111
REMARK 465 ARG A 112
REMARK 465 ASP A 113
REMARK 465 CYS A 114
REMARK 465 ASP A 215
REMARK 465 ALA A 216
REMARK 465 GLU A 217
REMARK 465 SER A 218
REMARK 465 ASP A 219
REMARK 465 GLU A 220
REMARK 465 ASP A 221
REMARK 465 GLU A 222
REMARK 465 ASP A 223
REMARK 465 ALA A 248
REMARK 465 LYS A 249
REMARK 465 GLY A 250
REMARK 465 LYS A 251
REMARK 465 LYS A 252
REMARK 465 GLY A 307
REMARK 465 GLY A 308
REMARK 465 ARG A 309
REMARK 465 LYS A 310
REMARK 465 VAL A 311
REMARK 465 GLU A 312
REMARK 465 ASN A 313
REMARK 465 GLU A 314
REMARK 465 ASP A 315
REMARK 465 MSE A 316
REMARK 465 ASN A 317
REMARK 465 LYS A 318
REMARK 465 ASP A 319
REMARK 465 GLN A 320
REMARK 465 GLY B 20
REMARK 465 SER B 21
REMARK 465 ASN B 22
REMARK 465 LEU B 23
REMARK 465 PRO B 24
REMARK 465 ASN B 25
REMARK 465 GLN B 26
REMARK 465 VAL B 27
REMARK 465 HIS B 28
REMARK 465 ARG B 29
REMARK 465 LYS B 30
REMARK 465 SER B 31
REMARK 465 VAL B 32
REMARK 465 LYS B 33
REMARK 465 LYS B 34
REMARK 465 GLY B 35
REMARK 465 ASP B 61
REMARK 465 LEU B 62
REMARK 465 TYR B 63
REMARK 465 PRO B 64
REMARK 465 GLU B 65
REMARK 465 ARG B 66
REMARK 465 VAL B 67
REMARK 465 ILE B 68
REMARK 465 SER B 69
REMARK 465 GLY B 70
REMARK 465 ALA B 71
REMARK 465 ALA B 72
REMARK 465 GLU B 73
REMARK 465 ARG B 91
REMARK 465 GLY B 92
REMARK 465 GLY B 104
REMARK 465 TYR B 105
REMARK 465 GLY B 106
REMARK 465 ASP B 107
REMARK 465 ALA B 108
REMARK 465 ILE B 109
REMARK 465 ASN B 110
REMARK 465 ALA B 216
REMARK 465 GLU B 217
REMARK 465 SER B 218
REMARK 465 ASP B 219
REMARK 465 GLU B 220
REMARK 465 ASP B 221
REMARK 465 GLU B 222
REMARK 465 ASP B 223
REMARK 465 ALA B 248
REMARK 465 LYS B 249
REMARK 465 GLY B 250
REMARK 465 LYS B 251
REMARK 465 LYS B 252
REMARK 465 GLY B 307
REMARK 465 GLY B 308
REMARK 465 ARG B 309
REMARK 465 LYS B 310
REMARK 465 VAL B 311
REMARK 465 GLU B 312
REMARK 465 ASN B 313
REMARK 465 GLU B 314
REMARK 465 ASP B 315
REMARK 465 MSE B 316
REMARK 465 ASN B 317
REMARK 465 LYS B 318
REMARK 465 ASP B 319
REMARK 465 GLN B 320
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 GLU A 37 CG CD OE1 OE2
REMARK 470 SER A 84 OG
REMARK 470 THR A 85 OG1 CG2
REMARK 470 VAL A 86 CG1 CG2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 ILE A 88 CG1 CG2 CD1
REMARK 470 GLU A 89 CG CD OE1 OE2
REMARK 470 LEU A 95 CG CD1 CD2
REMARK 470 ARG A 96 CD NE CZ NH1 NH2
REMARK 470 PHE A 115 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 116 CG CD CE NZ
REMARK 470 ARG A 128 CD NE CZ NH1 NH2
REMARK 470 HIS A 140 ND1 CD2 CE1 NE2
REMARK 470 PHE A 167 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 169 CD CE NZ
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 GLU A 193 CD OE1 OE2
REMARK 470 LYS A 197 CG CD CE NZ
REMARK 470 GLU A 204 CD OE1 OE2
REMARK 470 ASN A 207 CG OD1 ND2
REMARK 470 PHE A 224 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 GLN A 227 CG CD OE1 NE2
REMARK 470 ARG A 229 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 230 CG CD1 CD2
REMARK 470 LEU A 231 CD1 CD2
REMARK 470 GLN A 244 CG CD OE1 NE2
REMARK 470 VAL A 253 CG1 CG2
REMARK 470 GLN A 292 CG CD OE1 NE2
REMARK 470 GLU A 302 CG CD OE1 OE2
REMARK 470 ARG A 306 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 59 CG CD1 CD2
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 ILE B 75 CG1 CG2 CD1
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 ARG B 77 CG CD NE CZ NH1 NH2
REMARK 470 THR B 78 OG1 CG2
REMARK 470 VAL B 79 CG1 CG2
REMARK 470 GLN B 80 CG CD OE1 NE2
REMARK 470 ILE B 81 CG1 CG2 CD1
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 SER B 84 OG
REMARK 470 THR B 85 OG1 CG2
REMARK 470 VAL B 86 CG1 CG2
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 ILE B 88 CG1 CG2 CD1
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 GLU B 90 CG CD OE1 OE2
REMARK 470 ARG B 112 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 128 CD NE CZ NH1 NH2
REMARK 470 ASN B 137 CG OD1 ND2
REMARK 470 HIS B 140 ND1 CD2 CE1 NE2
REMARK 470 HIS B 158 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 161 CE NZ
REMARK 470 LYS B 190 CD CE NZ
REMARK 470 GLU B 193 CD OE1 OE2
REMARK 470 ARG B 198 NE CZ NH1 NH2
REMARK 470 HIS B 212 CG ND1 CD2 CE1 NE2
REMARK 470 PHE B 224 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 225 CG CD CE NZ
REMARK 470 LEU B 230 CG CD1 CD2
REMARK 470 ASN B 243 CG OD1 ND2
REMARK 470 GLN B 244 CD OE1 NE2
REMARK 470 VAL B 253 CG1 CG2
REMARK 470 GLN B 288 CD OE1 NE2
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 139 34.32 -71.98
REMARK 500 HIS A 140 34.86 -156.54
REMARK 500 CYS A 148 144.21 -173.21
REMARK 500 LYS A 225 -71.63 -33.05
REMARK 500 LEU B 59 56.68 70.78
REMARK 500 ARG B 139 -72.01 -44.85
REMARK 500 LEU B 294 -74.00 -96.64
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 GDP A 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 4
DBREF 2QNR A 22 320 UNP Q15019 SEPT2_HUMAN 22 320
DBREF 2QNR B 22 320 UNP Q15019 SEPT2_HUMAN 22 320
SEQADV 2QNR GLY A 20 UNP Q15019 CLONING ARTIFACT
SEQADV 2QNR SER A 21 UNP Q15019 CLONING ARTIFACT
SEQADV 2QNR SER A 69 UNP Q15019 PRO 69 VARIANT
SEQADV 2QNR GLY B 20 UNP Q15019 CLONING ARTIFACT
SEQADV 2QNR SER B 21 UNP Q15019 CLONING ARTIFACT
SEQADV 2QNR SER B 69 UNP Q15019 PRO 69 VARIANT
SEQRES 1 A 301 GLY SER ASN LEU PRO ASN GLN VAL HIS ARG LYS SER VAL
SEQRES 2 A 301 LYS LYS GLY PHE GLU PHE THR LEU MSE VAL VAL GLY GLU
SEQRES 3 A 301 SER GLY LEU GLY LYS SER THR LEU ILE ASN SER LEU PHE
SEQRES 4 A 301 LEU THR ASP LEU TYR PRO GLU ARG VAL ILE SER GLY ALA
SEQRES 5 A 301 ALA GLU LYS ILE GLU ARG THR VAL GLN ILE GLU ALA SER
SEQRES 6 A 301 THR VAL GLU ILE GLU GLU ARG GLY VAL LYS LEU ARG LEU
SEQRES 7 A 301 THR VAL VAL ASP THR PRO GLY TYR GLY ASP ALA ILE ASN
SEQRES 8 A 301 CYS ARG ASP CYS PHE LYS THR ILE ILE SER TYR ILE ASP
SEQRES 9 A 301 GLU GLN PHE GLU ARG TYR LEU HIS ASP GLU SER GLY LEU
SEQRES 10 A 301 ASN ARG ARG HIS ILE ILE ASP ASN ARG VAL HIS CYS CYS
SEQRES 11 A 301 PHE TYR PHE ILE SER PRO PHE GLY HIS GLY LEU LYS PRO
SEQRES 12 A 301 LEU ASP VAL ALA PHE MSE LYS ALA ILE HIS ASN LYS VAL
SEQRES 13 A 301 ASN ILE VAL PRO VAL ILE ALA LYS ALA ASP THR LEU THR
SEQRES 14 A 301 LEU LYS GLU ARG GLU ARG LEU LYS LYS ARG ILE LEU ASP
SEQRES 15 A 301 GLU ILE GLU GLU HIS ASN ILE LYS ILE TYR HIS LEU PRO
SEQRES 16 A 301 ASP ALA GLU SER ASP GLU ASP GLU ASP PHE LYS GLU GLN
SEQRES 17 A 301 THR ARG LEU LEU LYS ALA SER ILE PRO PHE SER VAL VAL
SEQRES 18 A 301 GLY SER ASN GLN LEU ILE GLU ALA LYS GLY LYS LYS VAL
SEQRES 19 A 301 ARG GLY ARG LEU TYR PRO TRP GLY VAL VAL GLU VAL GLU
SEQRES 20 A 301 ASN PRO GLU HIS ASN ASP PHE LEU LYS LEU ARG THR MSE
SEQRES 21 A 301 LEU ILE THR HIS MSE GLN ASP LEU GLN GLU VAL THR GLN
SEQRES 22 A 301 ASP LEU HIS TYR GLU ASN PHE ARG SER GLU ARG LEU LYS
SEQRES 23 A 301 ARG GLY GLY ARG LYS VAL GLU ASN GLU ASP MSE ASN LYS
SEQRES 24 A 301 ASP GLN
SEQRES 1 B 301 GLY SER ASN LEU PRO ASN GLN VAL HIS ARG LYS SER VAL
SEQRES 2 B 301 LYS LYS GLY PHE GLU PHE THR LEU MSE VAL VAL GLY GLU
SEQRES 3 B 301 SER GLY LEU GLY LYS SER THR LEU ILE ASN SER LEU PHE
SEQRES 4 B 301 LEU THR ASP LEU TYR PRO GLU ARG VAL ILE SER GLY ALA
SEQRES 5 B 301 ALA GLU LYS ILE GLU ARG THR VAL GLN ILE GLU ALA SER
SEQRES 6 B 301 THR VAL GLU ILE GLU GLU ARG GLY VAL LYS LEU ARG LEU
SEQRES 7 B 301 THR VAL VAL ASP THR PRO GLY TYR GLY ASP ALA ILE ASN
SEQRES 8 B 301 CYS ARG ASP CYS PHE LYS THR ILE ILE SER TYR ILE ASP
SEQRES 9 B 301 GLU GLN PHE GLU ARG TYR LEU HIS ASP GLU SER GLY LEU
SEQRES 10 B 301 ASN ARG ARG HIS ILE ILE ASP ASN ARG VAL HIS CYS CYS
SEQRES 11 B 301 PHE TYR PHE ILE SER PRO PHE GLY HIS GLY LEU LYS PRO
SEQRES 12 B 301 LEU ASP VAL ALA PHE MSE LYS ALA ILE HIS ASN LYS VAL
SEQRES 13 B 301 ASN ILE VAL PRO VAL ILE ALA LYS ALA ASP THR LEU THR
SEQRES 14 B 301 LEU LYS GLU ARG GLU ARG LEU LYS LYS ARG ILE LEU ASP
SEQRES 15 B 301 GLU ILE GLU GLU HIS ASN ILE LYS ILE TYR HIS LEU PRO
SEQRES 16 B 301 ASP ALA GLU SER ASP GLU ASP GLU ASP PHE LYS GLU GLN
SEQRES 17 B 301 THR ARG LEU LEU LYS ALA SER ILE PRO PHE SER VAL VAL
SEQRES 18 B 301 GLY SER ASN GLN LEU ILE GLU ALA LYS GLY LYS LYS VAL
SEQRES 19 B 301 ARG GLY ARG LEU TYR PRO TRP GLY VAL VAL GLU VAL GLU
SEQRES 20 B 301 ASN PRO GLU HIS ASN ASP PHE LEU LYS LEU ARG THR MSE
SEQRES 21 B 301 LEU ILE THR HIS MSE GLN ASP LEU GLN GLU VAL THR GLN
SEQRES 22 B 301 ASP LEU HIS TYR GLU ASN PHE ARG SER GLU ARG LEU LYS
SEQRES 23 B 301 ARG GLY GLY ARG LYS VAL GLU ASN GLU ASP MSE ASN LYS
SEQRES 24 B 301 ASP GLN
MODRES 2QNR MSE A 41 MET SELENOMETHIONINE
MODRES 2QNR MSE A 168 MET SELENOMETHIONINE
MODRES 2QNR MSE A 279 MET SELENOMETHIONINE
MODRES 2QNR MSE A 284 MET SELENOMETHIONINE
MODRES 2QNR MSE B 41 MET SELENOMETHIONINE
MODRES 2QNR MSE B 168 MET SELENOMETHIONINE
MODRES 2QNR MSE B 279 MET SELENOMETHIONINE
MODRES 2QNR MSE B 284 MET SELENOMETHIONINE
HET MSE A 41 8
HET MSE A 168 8
HET MSE A 279 8
HET MSE A 284 8
HET MSE B 41 8
HET MSE B 168 8
HET MSE B 279 8
HET MSE B 284 8
HET GDP A1401 28
HET UNX A 1 1
HET UNX A 3 1
HET GDP B1401 28
HET UNX B 2 1
HET UNX B 4 1
HETNAM MSE SELENOMETHIONINE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 UNX 4(X)
HELIX 1 1 GLY A 49 LEU A 59 1 11
HELIX 2 2 THR A 117 SER A 134 1 18
HELIX 3 3 LYS A 161 HIS A 172 1 12
HELIX 4 4 LYS A 183 LEU A 187 5 5
HELIX 5 5 THR A 188 HIS A 206 1 19
HELIX 6 6 PHE A 224 ALA A 233 1 10
HELIX 7 7 ASP A 272 HIS A 283 1 12
HELIX 8 8 HIS A 283 LEU A 294 1 12
HELIX 9 9 LEU A 294 ARG A 306 1 13
HELIX 10 10 GLY B 49 LEU B 59 1 11
HELIX 11 11 ARG B 77 SER B 84 1 8
HELIX 12 12 ARG B 112 GLY B 135 1 24
HELIX 13 13 LYS B 161 HIS B 172 1 12
HELIX 14 14 LYS B 183 LEU B 187 5 5
HELIX 15 15 THR B 188 ASN B 207 1 20
HELIX 16 16 LYS B 225 ILE B 235 1 11
HELIX 17 17 ASP B 272 LEU B 294 1 23
HELIX 18 18 LEU B 294 ARG B 306 1 13
SHEET 1 A 6 THR A 85 ILE A 88 0
SHEET 2 A 6 LEU A 95 THR A 102 -1 O LEU A 97 N VAL A 86
SHEET 3 A 6 PHE A 38 GLU A 45 1 N LEU A 40 O ARG A 96
SHEET 4 A 6 CYS A 148 ILE A 153 1 O CYS A 148 N MSE A 41
SHEET 5 A 6 ILE A 177 ILE A 181 1 O VAL A 180 N TYR A 151
SHEET 6 A 6 PHE A 237 SER A 238 1 O PHE A 237 N ILE A 181
SHEET 1 B 2 GLY A 255 TYR A 258 0
SHEET 2 B 2 GLY A 261 GLU A 264 -1 O GLY A 261 N TYR A 258
SHEET 1 C 6 VAL B 86 ILE B 88 0
SHEET 2 C 6 LYS B 94 THR B 102 -1 O LEU B 95 N ILE B 88
SHEET 3 C 6 GLU B 37 GLU B 45 1 N VAL B 42 O VAL B 100
SHEET 4 C 6 CYS B 148 ILE B 153 1 O PHE B 150 N MSE B 41
SHEET 5 C 6 ILE B 177 ILE B 181 1 O VAL B 178 N TYR B 151
SHEET 6 C 6 PHE B 237 SER B 238 1 O PHE B 237 N ILE B 181
SHEET 1 D 2 GLY B 255 TYR B 258 0
SHEET 2 D 2 GLY B 261 GLU B 264 -1 O VAL B 263 N ARG B 256
LINK C LEU A 40 N MSE A 41 1555 1555 1.32
LINK C MSE A 41 N VAL A 42 1555 1555 1.32
LINK C PHE A 167 N MSE A 168 1555 1555 1.32
LINK C MSE A 168 N LYS A 169 1555 1555 1.34
LINK C THR A 278 N MSE A 279 1555 1555 1.33
LINK C MSE A 279 N LEU A 280 1555 1555 1.33
LINK C HIS A 283 N MSE A 284 1555 1555 1.32
LINK C MSE A 284 N GLN A 285 1555 1555 1.33
LINK C LEU B 40 N MSE B 41 1555 1555 1.33
LINK C MSE B 41 N VAL B 42 1555 1555 1.32
LINK C PHE B 167 N MSE B 168 1555 1555 1.32
LINK C MSE B 168 N LYS B 169 1555 1555 1.33
LINK C THR B 278 N MSE B 279 1555 1555 1.33
LINK C MSE B 279 N LEU B 280 1555 1555 1.33
LINK C HIS B 283 N MSE B 284 1555 1555 1.32
LINK C MSE B 284 N GLN B 285 1555 1555 1.33
CISPEP 1 ILE A 235 PRO A 236 0 -3.52
CISPEP 2 ILE B 235 PRO B 236 0 -4.59
SITE 1 AC1 14 GLY A 47 LEU A 48 GLY A 49 LYS A 50
SITE 2 AC1 14 SER A 51 THR A 52 LYS A 183 ASP A 185
SITE 3 AC1 14 VAL A 240 GLY A 241 ARG A 256 TYR A 258
SITE 4 AC1 14 THR B 186 GLU B 191
SITE 1 AC2 15 THR A 186 GLU A 191 SER B 46 GLY B 47
SITE 2 AC2 15 LEU B 48 GLY B 49 LYS B 50 SER B 51
SITE 3 AC2 15 THR B 52 LYS B 183 ASP B 185 VAL B 240
SITE 4 AC2 15 GLY B 241 ARG B 256 TYR B 258
SITE 1 AC3 3 TYR A 258 PRO A 259 LEU B 189
SITE 1 AC4 5 VAL A 175 ASN A 176 ILE A 177 LYS A 209
SITE 2 AC4 5 TYR A 211
SITE 1 AC5 4 GLY B 44 GLU B 45 LEU B 48 PHE B 152
CRYST1 164.536 52.295 110.944 90.00 132.48 90.00 C 1 2 1 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 0.006080 0.000000 0.005560 0.00000
SCALE2 0.000000 0.019120 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012220 0.00000
(ATOM LINES ARE NOT SHOWN.)
END