HEADER VIRAL PROTEIN 14-MAR-17 5V5O
TITLE STRUCTURE OF NLS2K OF INFLUENZA A VIRUS NUCLEOPROTEIN BOUND TO
TITLE 2 IMPORTIN ALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;
COMPND 3 CHAIN: C;
COMPND 4 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE
COMPND 5 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-
COMPND 6 ALPHA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NUCLEOPROTEIN;
COMPND 10 CHAIN: A, B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KPNA2, RCH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE 14 ORGANISM_TAXID: 11320
KEYWDS NUCLEAR IMPORT, NLS, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.S.SANKHALA,R.K.LOKAREDDY,G.CINGOLANI
REVDAT 5 04-OCT-23 5V5O 1 REMARK
REVDAT 4 26-FEB-20 5V5O 1 REMARK
REVDAT 3 01-JAN-20 5V5O 1 REMARK
REVDAT 2 25-SEP-19 5V5O 1 JRNL
REVDAT 1 14-MAR-18 5V5O 0
JRNL AUTH W.WU,R.S.SANKHALA,T.J.FLORIO,L.ZHOU,N.L.T.NGUYEN,
JRNL AUTH 2 R.K.LOKAREDDY,G.CINGOLANI,N.PANTE
JRNL TITL SYNERGY OF TWO LOW-AFFINITY NLSS DETERMINES THE HIGH AVIDITY
JRNL TITL 2 OF INFLUENZA A VIRUS NUCLEOPROTEIN NP FOR HUMAN IMPORTIN
JRNL TITL 3 ALPHA ISOFORMS.
JRNL REF SCI REP V. 7 11381 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28900157
JRNL DOI 10.1038/S41598-017-11018-1
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2481)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 32817
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1641
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 14.9680 - 5.0742 0.94 2652 143 0.1489 0.1560
REMARK 3 2 5.0742 - 4.0539 0.98 2664 137 0.1266 0.1749
REMARK 3 3 4.0539 - 3.5493 0.99 2643 141 0.1362 0.1807
REMARK 3 4 3.5493 - 3.2283 0.99 2643 140 0.1668 0.1908
REMARK 3 5 3.2283 - 2.9989 0.99 2630 150 0.1805 0.2157
REMARK 3 6 2.9989 - 2.8233 0.99 2612 132 0.1894 0.2317
REMARK 3 7 2.8233 - 2.6828 0.98 2613 133 0.1953 0.2037
REMARK 3 8 2.6828 - 2.5666 0.98 2565 143 0.2112 0.2546
REMARK 3 9 2.5666 - 2.4683 0.98 2613 125 0.2287 0.2702
REMARK 3 10 2.4683 - 2.3834 0.98 2545 135 0.2612 0.2872
REMARK 3 11 2.3834 - 2.3092 0.97 2545 138 0.2923 0.3626
REMARK 3 12 2.3092 - 2.2434 0.93 2451 124 0.3189 0.3367
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 3389
REMARK 3 ANGLE : 0.531 4609
REMARK 3 CHIRALITY : 0.037 552
REMARK 3 PLANARITY : 0.004 592
REMARK 3 DIHEDRAL : 14.718 2063
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 75 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2459 1.9841 -15.4506
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.2295
REMARK 3 T33: 0.1925 T12: -0.0211
REMARK 3 T13: -0.0194 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 1.0371 L22: 3.7372
REMARK 3 L33: 0.9184 L12: -0.0434
REMARK 3 L13: 0.0456 L23: 1.3063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: -0.0457 S13: -0.0852
REMARK 3 S21: 0.1925 S22: 0.0444 S23: 0.1250
REMARK 3 S31: 0.1928 S32: -0.0844 S33: -0.1203
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 246 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1201 30.8736 -4.2003
REMARK 3 T TENSOR
REMARK 3 T11: 0.1816 T22: 0.1785
REMARK 3 T33: 0.2408 T12: 0.0084
REMARK 3 T13: -0.0156 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 2.1425 L22: 2.1993
REMARK 3 L33: 3.4316 L12: -1.0614
REMARK 3 L13: -1.8681 L23: 1.4469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0792 S12: -0.1355 S13: 0.1627
REMARK 3 S21: -0.1278 S22: -0.0228 S23: -0.0991
REMARK 3 S31: -0.2224 S32: 0.0439 S33: -0.0770
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 376 THROUGH 497 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8017 39.6215 23.8322
REMARK 3 T TENSOR
REMARK 3 T11: 0.4671 T22: 0.7482
REMARK 3 T33: 0.3922 T12: -0.0369
REMARK 3 T13: -0.0325 T23: -0.1527
REMARK 3 L TENSOR
REMARK 3 L11: 2.4792 L22: 4.6324
REMARK 3 L33: 4.6777 L12: -0.0983
REMARK 3 L13: 0.3812 L23: 0.3844
REMARK 3 S TENSOR
REMARK 3 S11: 0.1308 S12: -0.9990 S13: 0.2509
REMARK 3 S21: 1.0156 S22: 0.0159 S23: -0.4445
REMARK 3 S31: -0.0513 S32: 0.6090 S33: -0.0089
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8491 7.3931 -7.1092
REMARK 3 T TENSOR
REMARK 3 T11: 1.1577 T22: 0.6642
REMARK 3 T33: 0.9283 T12: 0.0421
REMARK 3 T13: 0.1257 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 9.0833 L22: 4.0819
REMARK 3 L33: 3.9441 L12: -1.9947
REMARK 3 L13: 0.6068 L23: 3.6183
REMARK 3 S TENSOR
REMARK 3 S11: -0.2739 S12: -0.6328 S13: 0.5897
REMARK 3 S21: -0.5607 S22: 0.3036 S23: 0.8307
REMARK 3 S31: 0.9848 S32: 0.1841 S33: -0.1895
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 212 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6132 32.2518 7.8400
REMARK 3 T TENSOR
REMARK 3 T11: 1.0390 T22: 0.9749
REMARK 3 T33: 0.8308 T12: 0.2446
REMARK 3 T13: 0.0700 T23: -0.1344
REMARK 3 L TENSOR
REMARK 3 L11: 4.0765 L22: 0.3364
REMARK 3 L33: 6.8596 L12: -0.7818
REMARK 3 L13: -0.4537 L23: -1.0402
REMARK 3 S TENSOR
REMARK 3 S11: 0.3004 S12: 0.1133 S13: -0.6145
REMARK 3 S21: -0.5267 S22: 0.3168 S23: -0.4888
REMARK 3 S31: 0.1142 S32: 0.1842 S33: -0.6312
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V5O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226910.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32858
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.71000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5HUY
REMARK 200
REMARK 200 REMARK: RECTANGULAR BLOCKS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 6.0, 0.6 M SODIUM
REMARK 280 CITRATE TRIBASIC DIHYDRATE, 10 MM B-MERCAPTOETHANOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 39.08250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.54300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.44650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.54300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.08250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.44650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 SER C 2
REMARK 465 THR C 3
REMARK 465 ASN C 4
REMARK 465 GLU C 5
REMARK 465 ASN C 6
REMARK 465 ALA C 7
REMARK 465 ASN C 8
REMARK 465 LEU C 9
REMARK 465 PRO C 10
REMARK 465 ALA C 11
REMARK 465 ALA C 12
REMARK 465 ARG C 13
REMARK 465 LEU C 14
REMARK 465 ASN C 15
REMARK 465 ARG C 16
REMARK 465 PHE C 17
REMARK 465 LYS C 18
REMARK 465 ASN C 19
REMARK 465 LYS C 20
REMARK 465 GLY C 21
REMARK 465 LYS C 22
REMARK 465 ASP C 23
REMARK 465 SER C 24
REMARK 465 THR C 25
REMARK 465 GLU C 26
REMARK 465 MET C 27
REMARK 465 ARG C 28
REMARK 465 ARG C 29
REMARK 465 ARG C 30
REMARK 465 ARG C 31
REMARK 465 ILE C 32
REMARK 465 GLU C 33
REMARK 465 VAL C 34
REMARK 465 ASN C 35
REMARK 465 VAL C 36
REMARK 465 GLU C 37
REMARK 465 LEU C 38
REMARK 465 ARG C 39
REMARK 465 LYS C 40
REMARK 465 ALA C 41
REMARK 465 LYS C 42
REMARK 465 LYS C 43
REMARK 465 ASP C 44
REMARK 465 GLU C 45
REMARK 465 GLN C 46
REMARK 465 MET C 47
REMARK 465 LEU C 48
REMARK 465 LYS C 49
REMARK 465 ARG C 50
REMARK 465 ARG C 51
REMARK 465 ASN C 52
REMARK 465 VAL C 53
REMARK 465 SER C 54
REMARK 465 SER C 55
REMARK 465 PHE C 56
REMARK 465 PRO C 57
REMARK 465 ASP C 58
REMARK 465 ASP C 59
REMARK 465 ALA C 60
REMARK 465 THR C 61
REMARK 465 SER C 62
REMARK 465 PRO C 63
REMARK 465 LEU C 64
REMARK 465 GLN C 65
REMARK 465 GLU C 66
REMARK 465 ASN C 67
REMARK 465 ARG C 68
REMARK 465 ASN C 69
REMARK 465 ASN C 70
REMARK 465 GLN C 71
REMARK 465 GLY C 72
REMARK 465 THR C 73
REMARK 465 VAL C 74
REMARK 465 VAL C 498
REMARK 465 GLU C 499
REMARK 465 GLU C 500
REMARK 465 GLU C 501
REMARK 465 GLU C 502
REMARK 465 ASP C 503
REMARK 465 GLN C 504
REMARK 465 ASN C 505
REMARK 465 VAL C 506
REMARK 465 VAL C 507
REMARK 465 PRO C 508
REMARK 465 GLU C 509
REMARK 465 THR C 510
REMARK 465 THR C 511
REMARK 465 SER C 512
REMARK 465 GLU C 513
REMARK 465 GLY C 514
REMARK 465 PHE C 515
REMARK 465 ALA C 516
REMARK 465 PHE C 517
REMARK 465 GLN C 518
REMARK 465 VAL C 519
REMARK 465 GLN C 520
REMARK 465 ASP C 521
REMARK 465 GLY C 522
REMARK 465 ALA C 523
REMARK 465 PRO C 524
REMARK 465 GLY C 525
REMARK 465 THR C 526
REMARK 465 PHE C 527
REMARK 465 ASN C 528
REMARK 465 PHE C 529
REMARK 465 LYS A 198
REMARK 465 ARG A 199
REMARK 465 GLY A 200
REMARK 465 ILE A 201
REMARK 465 ASN A 202
REMARK 465 ASP A 203
REMARK 465 ARG A 204
REMARK 465 ASN A 205
REMARK 465 PHE A 206
REMARK 465 TRP A 207
REMARK 465 ARG A 208
REMARK 465 LYS B 198
REMARK 465 ARG B 199
REMARK 465 GLY B 200
REMARK 465 ILE B 201
REMARK 465 ASN B 202
REMARK 465 ASP B 203
REMARK 465 ARG B 204
REMARK 465 ASN B 205
REMARK 465 PHE B 206
REMARK 465 TRP B 207
REMARK 465 ARG B 208
REMARK 465 GLY B 209
REMARK 465 GLU B 210
REMARK 465 ASN B 211
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL C 321 NH2 ARG B 213 1.66
REMARK 500 O HOH C 601 O HOH C 926 2.17
REMARK 500 O HOH C 763 O HOH C 905 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN C 109 74.91 52.87
REMARK 500 ASN C 239 78.73 66.04
REMARK 500 LYS C 240 178.06 -59.45
REMARK 500 ASP C 471 46.40 -88.14
REMARK 500 LYS C 472 -30.05 -130.46
REMARK 500 ARG C 478 57.98 -96.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZDU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF IMPORTIN-ALPHA BOUND TO A NON-CLASSICAL
REMARK 900 NUCLEAR LOCALIZATION SIGNAL OF THE INFLUENZA A VIRUS NUCLEOPROTEIN
REMARK 900 RELATED ID: 5V5P RELATED DB: PDB
DBREF 5V5O C 2 529 UNP P52293 IMA1_MOUSE 2 529
DBREF 5V5O A 198 216 PDB 5V5O 5V5O 198 216
DBREF 5V5O B 198 216 PDB 5V5O 5V5O 198 216
SEQRES 1 C 528 SER THR ASN GLU ASN ALA ASN LEU PRO ALA ALA ARG LEU
SEQRES 2 C 528 ASN ARG PHE LYS ASN LYS GLY LYS ASP SER THR GLU MET
SEQRES 3 C 528 ARG ARG ARG ARG ILE GLU VAL ASN VAL GLU LEU ARG LYS
SEQRES 4 C 528 ALA LYS LYS ASP GLU GLN MET LEU LYS ARG ARG ASN VAL
SEQRES 5 C 528 SER SER PHE PRO ASP ASP ALA THR SER PRO LEU GLN GLU
SEQRES 6 C 528 ASN ARG ASN ASN GLN GLY THR VAL ASN TRP SER VAL GLU
SEQRES 7 C 528 ASP ILE VAL LYS GLY ILE ASN SER ASN ASN LEU GLU SER
SEQRES 8 C 528 GLN LEU GLN ALA THR GLN ALA ALA ARG LYS LEU LEU SER
SEQRES 9 C 528 ARG GLU LYS GLN PRO PRO ILE ASP ASN ILE ILE ARG ALA
SEQRES 10 C 528 GLY LEU ILE PRO LYS PHE VAL SER PHE LEU GLY LYS THR
SEQRES 11 C 528 ASP CYS SER PRO ILE GLN PHE GLU SER ALA TRP ALA LEU
SEQRES 12 C 528 THR ASN ILE ALA SER GLY THR SER GLU GLN THR LYS ALA
SEQRES 13 C 528 VAL VAL ASP GLY GLY ALA ILE PRO ALA PHE ILE SER LEU
SEQRES 14 C 528 LEU ALA SER PRO HIS ALA HIS ILE SER GLU GLN ALA VAL
SEQRES 15 C 528 TRP ALA LEU GLY ASN ILE ALA GLY ASP GLY SER ALA PHE
SEQRES 16 C 528 ARG ASP LEU VAL ILE LYS HIS GLY ALA ILE ASP PRO LEU
SEQRES 17 C 528 LEU ALA LEU LEU ALA VAL PRO ASP LEU SER THR LEU ALA
SEQRES 18 C 528 CYS GLY TYR LEU ARG ASN LEU THR TRP THR LEU SER ASN
SEQRES 19 C 528 LEU CYS ARG ASN LYS ASN PRO ALA PRO PRO LEU ASP ALA
SEQRES 20 C 528 VAL GLU GLN ILE LEU PRO THR LEU VAL ARG LEU LEU HIS
SEQRES 21 C 528 HIS ASN ASP PRO GLU VAL LEU ALA ASP SER CYS TRP ALA
SEQRES 22 C 528 ILE SER TYR LEU THR ASP GLY PRO ASN GLU ARG ILE GLU
SEQRES 23 C 528 MET VAL VAL LYS LYS GLY VAL VAL PRO GLN LEU VAL LYS
SEQRES 24 C 528 LEU LEU GLY ALA THR GLU LEU PRO ILE VAL THR PRO ALA
SEQRES 25 C 528 LEU ARG ALA ILE GLY ASN ILE VAL THR GLY THR ASP GLU
SEQRES 26 C 528 GLN THR GLN LYS VAL ILE ASP ALA GLY ALA LEU ALA VAL
SEQRES 27 C 528 PHE PRO SER LEU LEU THR ASN PRO LYS THR ASN ILE GLN
SEQRES 28 C 528 LYS GLU ALA THR TRP THR MET SER ASN ILE THR ALA GLY
SEQRES 29 C 528 ARG GLN ASP GLN ILE GLN GLN VAL VAL ASN HIS GLY LEU
SEQRES 30 C 528 VAL PRO PHE LEU VAL GLY VAL LEU SER LYS ALA ASP PHE
SEQRES 31 C 528 LYS THR GLN LYS GLU ALA ALA TRP ALA ILE THR ASN TYR
SEQRES 32 C 528 THR SER GLY GLY THR VAL GLU GLN ILE VAL TYR LEU VAL
SEQRES 33 C 528 HIS CYS GLY ILE ILE GLU PRO LEU MET ASN LEU LEU SER
SEQRES 34 C 528 ALA LYS ASP THR LYS ILE ILE GLN VAL ILE LEU ASP ALA
SEQRES 35 C 528 ILE SER ASN ILE PHE GLN ALA ALA GLU LYS LEU GLY GLU
SEQRES 36 C 528 THR GLU LYS LEU SER ILE MET ILE GLU GLU CYS GLY GLY
SEQRES 37 C 528 LEU ASP LYS ILE GLU ALA LEU GLN ARG HIS GLU ASN GLU
SEQRES 38 C 528 SER VAL TYR LYS ALA SER LEU ASN LEU ILE GLU LYS TYR
SEQRES 39 C 528 PHE SER VAL GLU GLU GLU GLU ASP GLN ASN VAL VAL PRO
SEQRES 40 C 528 GLU THR THR SER GLU GLY PHE ALA PHE GLN VAL GLN ASP
SEQRES 41 C 528 GLY ALA PRO GLY THR PHE ASN PHE
SEQRES 1 A 19 LYS ARG GLY ILE ASN ASP ARG ASN PHE TRP ARG GLY GLU
SEQRES 2 A 19 ASN GLY ARG LYS THR ARG
SEQRES 1 B 19 LYS ARG GLY ILE ASN ASP ARG ASN PHE TRP ARG GLY GLU
SEQRES 2 B 19 ASN GLY ARG LYS THR ARG
FORMUL 4 HOH *406(H2 O)
HELIX 1 AA1 SER C 77 ASN C 86 1 10
HELIX 2 AA2 ASN C 89 LEU C 104 1 16
HELIX 3 AA3 PRO C 111 ALA C 118 1 8
HELIX 4 AA4 LEU C 120 GLY C 129 1 10
HELIX 5 AA5 CYS C 133 SER C 149 1 17
HELIX 6 AA6 THR C 151 GLY C 161 1 11
HELIX 7 AA7 GLY C 162 LEU C 171 1 10
HELIX 8 AA8 HIS C 175 GLY C 191 1 17
HELIX 9 AA9 GLY C 193 HIS C 203 1 11
HELIX 10 AB1 ALA C 205 LEU C 212 1 8
HELIX 11 AB2 ASP C 217 LEU C 221 5 5
HELIX 12 AB3 ALA C 222 LEU C 236 1 15
HELIX 13 AB4 PRO C 245 HIS C 261 1 17
HELIX 14 AB5 ASP C 264 ASP C 280 1 17
HELIX 15 AB6 PRO C 282 LYS C 292 1 11
HELIX 16 AB7 VAL C 294 GLY C 303 1 10
HELIX 17 AB8 GLU C 306 VAL C 321 1 16
HELIX 18 AB9 THR C 324 ALA C 334 1 11
HELIX 19 AC1 GLY C 335 ALA C 338 5 4
HELIX 20 AC2 VAL C 339 LEU C 344 1 6
HELIX 21 AC3 LYS C 348 THR C 363 1 16
HELIX 22 AC4 ARG C 366 HIS C 376 1 11
HELIX 23 AC5 LEU C 378 LYS C 388 1 11
HELIX 24 AC6 ASP C 390 GLY C 408 1 19
HELIX 25 AC7 THR C 409 CYS C 419 1 11
HELIX 26 AC8 ILE C 421 LEU C 428 1 8
HELIX 27 AC9 LEU C 429 ALA C 431 5 3
HELIX 28 AD1 ASP C 433 GLY C 455 1 23
HELIX 29 AD2 GLU C 456 CYS C 467 1 12
HELIX 30 AD3 GLY C 469 ARG C 478 1 10
HELIX 31 AD4 ASN C 481 PHE C 496 1 16
CISPEP 1 ASN C 241 PRO C 242 0 -3.80
CRYST1 78.165 90.893 97.086 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 0.012793 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011002 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010300 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
