HEADER PROTEIN TRANSPORT/VIRAL PROTEIN 25-APR-16 5B56
TITLE CRYSTAL STRUCTURE OF HIV-1 VPR C-TERMINAL DOMAIN AND DIBB-M-IMPORTIN-
TITLE 2 ALPHA2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 70-529;
COMPND 5 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE
COMPND 6 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-
COMPND 7 ALPHA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN VPR;
COMPND 11 CHAIN: C, D, E, F;
COMPND 12 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 85-96;
COMPND 13 SYNONYM: R ORF PROTEIN,VIRAL PROTEIN R;
COMPND 14 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HIV-1 M:B_89.6;
SOURCE 11 ORGANISM_COMMON: HIV-1;
SOURCE 12 ORGANISM_TAXID: 401671;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS ARM REPEAT, ALL ALPHA PROTEIN, NUCLEAR IMPORT, IMPORTIN-BETA, NLS-
KEYWDS 2 CARGO, PROTEIN TRANSPORT-VIRAL PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MIYATAKE,A.SANJOH,G.MATUSDA,T.MURAKAMI,H.MURAKAMI,K.HAGIWARA,
AUTHOR 2 M.YOKOYAMA,H.SATO,Y.MIYAMOTO,N.DOHMAE,Y.AIDA
REVDAT 4 08-NOV-23 5B56 1 REMARK
REVDAT 3 26-FEB-20 5B56 1 JRNL REMARK
REVDAT 2 29-JUN-16 5B56 1 JRNL
REVDAT 1 01-JUN-16 5B56 0
JRNL AUTH H.MIYATAKE,A.SANJOH,T.MURAKAMI,H.MURAKAMI,G.MATSUDA,
JRNL AUTH 2 K.HAGIWARA,M.YOKOYAMA,H.SATO,Y.MIYAMOTO,N.DOHMAE,Y.AIDA
JRNL TITL MOLECULAR MECHANISM OF HIV-1 VPR FOR BINDING TO
JRNL TITL 2 IMPORTIN-ALPHA
JRNL REF J.MOL.BIOL. V. 428 2744 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27181198
JRNL DOI 10.1016/J.JMB.2016.05.003
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.210
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 57284
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2906
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 43.4064 - 6.3342 0.98 2989 174 0.1544 0.1867
REMARK 3 2 6.3342 - 5.0301 0.99 2962 168 0.1811 0.2278
REMARK 3 3 5.0301 - 4.3949 0.99 2987 159 0.1377 0.1727
REMARK 3 4 4.3949 - 3.9934 0.99 3002 136 0.1331 0.1480
REMARK 3 5 3.9934 - 3.7074 0.98 2899 161 0.1401 0.1997
REMARK 3 6 3.7074 - 3.4889 0.98 2921 157 0.1592 0.2229
REMARK 3 7 3.4889 - 3.3142 0.98 2910 164 0.1831 0.2200
REMARK 3 8 3.3142 - 3.1700 0.96 2863 145 0.1943 0.2402
REMARK 3 9 3.1700 - 3.0480 0.95 2845 151 0.1969 0.2535
REMARK 3 10 3.0480 - 2.9428 0.92 2744 141 0.1952 0.2369
REMARK 3 11 2.9428 - 2.8508 0.90 2660 146 0.2044 0.2680
REMARK 3 12 2.8508 - 2.7694 0.89 2659 121 0.2184 0.2790
REMARK 3 13 2.7694 - 2.6965 0.88 2584 142 0.2226 0.2863
REMARK 3 14 2.6965 - 2.6307 0.86 2530 128 0.2372 0.2743
REMARK 3 15 2.6307 - 2.5709 0.83 2502 120 0.2532 0.3171
REMARK 3 16 2.5709 - 2.5162 0.79 2327 123 0.2723 0.3254
REMARK 3 17 2.5162 - 2.4659 0.76 2239 112 0.2939 0.3302
REMARK 3 18 2.4659 - 2.4193 0.75 2229 130 0.3007 0.3364
REMARK 3 19 2.4193 - 2.3761 0.71 2100 120 0.3081 0.3318
REMARK 3 20 2.3761 - 2.3359 0.66 1911 121 0.3236 0.3302
REMARK 3 21 2.3359 - 2.2982 0.51 1515 87 0.3438 0.4092
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.74
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 : 0.003 7063
REMARK 3 ANGLE : 0.724 9601
REMARK 3 CHIRALITY : 0.028 1147
REMARK 3 PLANARITY : 0.003 1239
REMARK 3 DIHEDRAL : 14.235 2610
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 70:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 68.1292 -16.2423 45.5953
REMARK 3 T TENSOR
REMARK 3 T11: 0.7096 T22: 0.7267
REMARK 3 T33: 0.6193 T12: -0.0642
REMARK 3 T13: 0.0876 T23: 0.1212
REMARK 3 L TENSOR
REMARK 3 L11: 1.3210 L22: 1.4479
REMARK 3 L33: 1.1499 L12: 0.5620
REMARK 3 L13: -0.4905 L23: 0.9592
REMARK 3 S TENSOR
REMARK 3 S11: 0.0760 S12: 0.4480 S13: 0.1265
REMARK 3 S21: -0.7355 S22: 0.0048 S23: -0.5473
REMARK 3 S31: -0.1383 S32: 0.9289 S33: 0.0025
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 134:362)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2426 -8.6729 55.7619
REMARK 3 T TENSOR
REMARK 3 T11: 0.3233 T22: 0.3649
REMARK 3 T33: 0.5425 T12: -0.0352
REMARK 3 T13: -0.0499 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 3.8931 L22: 0.8217
REMARK 3 L33: -0.0197 L12: -2.4870
REMARK 3 L13: 0.6370 L23: -0.6147
REMARK 3 S TENSOR
REMARK 3 S11: -0.1173 S12: -0.2569 S13: 0.0103
REMARK 3 S21: 0.1165 S22: 0.0640 S23: 0.0282
REMARK 3 S31: -0.0630 S32: -0.0191 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 363:498)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6151 0.2210 36.6654
REMARK 3 T TENSOR
REMARK 3 T11: 0.4564 T22: 0.4634
REMARK 3 T33: 0.3729 T12: -0.0534
REMARK 3 T13: -0.0307 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 4.2438 L22: 2.9220
REMARK 3 L33: 2.1954 L12: -0.7699
REMARK 3 L13: -0.0816 L23: -0.6420
REMARK 3 S TENSOR
REMARK 3 S11: 0.2367 S12: 0.5257 S13: -0.2270
REMARK 3 S21: -0.7650 S22: -0.0483 S23: 0.2095
REMARK 3 S31: 0.4872 S32: -0.2497 S33: 0.0006
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND (RESID 71:222)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8855 -20.2957 -19.6548
REMARK 3 T TENSOR
REMARK 3 T11: 0.4806 T22: 0.4391
REMARK 3 T33: 0.3429 T12: 0.0514
REMARK 3 T13: 0.0003 T23: -0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 2.4582 L22: 3.8553
REMARK 3 L33: 3.9949 L12: -0.3580
REMARK 3 L13: -0.1811 L23: -0.4060
REMARK 3 S TENSOR
REMARK 3 S11: 0.1707 S12: 0.2184 S13: -0.2129
REMARK 3 S21: -0.1322 S22: -0.0030 S23: -0.4563
REMARK 3 S31: 0.2622 S32: 0.4060 S33: 0.0017
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESID 223:481)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2397 -33.8352 19.7313
REMARK 3 T TENSOR
REMARK 3 T11: 0.5467 T22: 0.4025
REMARK 3 T33: 0.3830 T12: 0.0736
REMARK 3 T13: 0.0409 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: 1.0239 L22: 2.1497
REMARK 3 L33: 4.4367 L12: -0.9219
REMARK 3 L13: 0.8374 L23: -2.1353
REMARK 3 S TENSOR
REMARK 3 S11: -0.2064 S12: -0.0929 S13: 0.0764
REMARK 3 S21: 0.1894 S22: 0.2366 S23: -0.0667
REMARK 3 S31: -0.3974 S32: -0.1731 S33: -0.0016
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESID 482:502)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8747 -30.5366 48.1630
REMARK 3 T TENSOR
REMARK 3 T11: 1.7336 T22: 0.9896
REMARK 3 T33: 1.1026 T12: -0.0764
REMARK 3 T13: -0.1562 T23: -0.3103
REMARK 3 L TENSOR
REMARK 3 L11: 0.7085 L22: 2.4465
REMARK 3 L33: 1.9851 L12: 0.2641
REMARK 3 L13: -0.2106 L23: -1.0138
REMARK 3 S TENSOR
REMARK 3 S11: -0.4752 S12: -0.5301 S13: 0.3854
REMARK 3 S21: -0.0271 S22: -0.1735 S23: -1.4478
REMARK 3 S31: -0.8843 S32: 1.5862 S33: -0.1377
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND (RESID 85:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1867 -11.9217 45.2395
REMARK 3 T TENSOR
REMARK 3 T11: 0.8831 T22: 0.5138
REMARK 3 T33: 0.9397 T12: 0.0010
REMARK 3 T13: 0.0700 T23: -0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 0.1382 L22: 0.0768
REMARK 3 L33: 1.0367 L12: 0.0854
REMARK 3 L13: -0.2858 L23: -0.2452
REMARK 3 S TENSOR
REMARK 3 S11: -0.3716 S12: -0.0426 S13: -1.4077
REMARK 3 S21: -0.2659 S22: -0.3698 S23: 0.1514
REMARK 3 S31: 1.3266 S32: 0.2081 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN D AND (RESID 85:96)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9276 -24.0354 22.2413
REMARK 3 T TENSOR
REMARK 3 T11: 1.1937 T22: 0.6849
REMARK 3 T33: 0.6920 T12: 0.1004
REMARK 3 T13: -0.0511 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 0.1988 L22: 0.4367
REMARK 3 L33: 0.2383 L12: 0.0124
REMARK 3 L13: 0.1611 L23: -0.1466
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: 0.2800 S13: 0.7450
REMARK 3 S21: 0.5575 S22: 0.0749 S23: -0.3470
REMARK 3 S31: -0.9015 S32: -0.2976 S33: 0.0091
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN E AND (RESID 85:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9768 -7.4701 46.0297
REMARK 3 T TENSOR
REMARK 3 T11: 1.3162 T22: 0.7493
REMARK 3 T33: 1.5097 T12: -0.0974
REMARK 3 T13: -0.1018 T23: 0.0946
REMARK 3 L TENSOR
REMARK 3 L11: 1.5742 L22: 0.2846
REMARK 3 L33: 0.0340 L12: 0.3031
REMARK 3 L13: 0.2020 L23: -0.0115
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: 0.1295 S13: 0.4696
REMARK 3 S21: -0.5145 S22: -0.1584 S23: -0.0898
REMARK 3 S31: -0.3631 S32: 0.1147 S33: 0.0079
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN F AND (RESID 85:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9659 -28.2288 -1.0976
REMARK 3 T TENSOR
REMARK 3 T11: 1.8033 T22: 1.1848
REMARK 3 T33: 1.0256 T12: -0.0188
REMARK 3 T13: 0.0180 T23: -0.0774
REMARK 3 L TENSOR
REMARK 3 L11: 0.0890 L22: 0.2337
REMARK 3 L33: 0.9740 L12: 0.0689
REMARK 3 L13: 0.2646 L23: 0.4073
REMARK 3 S TENSOR
REMARK 3 S11: -0.2277 S12: -0.9824 S13: -0.1572
REMARK 3 S21: 1.3303 S22: -0.3231 S23: -0.0930
REMARK 3 S31: -0.1207 S32: -0.2257 S33: 0.0116
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 5B56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1300000549.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57284
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.298
REMARK 200 RESOLUTION RANGE LOW (A) : 31.523
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.8.1_1168
REMARK 200 STARTING MODEL: 3KND
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES, 100MM AMMONIUM SULFATE, 10MM
REMARK 280 MGCL2, 20-23%(W/V) PEG8000, 5MM DTT, PH 6.2, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.77750
REMARK 290 SMTRY3 2 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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 GLU A 499
REMARK 465 GLU A 500
REMARK 465 GLU A 501
REMARK 465 GLU A 502
REMARK 465 ASP A 503
REMARK 465 GLN A 504
REMARK 465 ASN A 505
REMARK 465 VAL A 506
REMARK 465 VAL A 507
REMARK 465 PRO A 508
REMARK 465 GLU A 509
REMARK 465 THR A 510
REMARK 465 THR A 511
REMARK 465 SER A 512
REMARK 465 GLU A 513
REMARK 465 GLY A 514
REMARK 465 PHE A 515
REMARK 465 ALA A 516
REMARK 465 PHE A 517
REMARK 465 GLN A 518
REMARK 465 VAL A 519
REMARK 465 GLN A 520
REMARK 465 ASP A 521
REMARK 465 GLY A 522
REMARK 465 ALA A 523
REMARK 465 PRO A 524
REMARK 465 GLY A 525
REMARK 465 THR A 526
REMARK 465 PHE A 527
REMARK 465 ASN A 528
REMARK 465 PHE A 529
REMARK 465 ASN B 70
REMARK 465 ASP B 503
REMARK 465 GLN B 504
REMARK 465 ASN B 505
REMARK 465 VAL B 506
REMARK 465 VAL B 507
REMARK 465 PRO B 508
REMARK 465 GLU B 509
REMARK 465 THR B 510
REMARK 465 THR B 511
REMARK 465 SER B 512
REMARK 465 GLU B 513
REMARK 465 GLY B 514
REMARK 465 PHE B 515
REMARK 465 ALA B 516
REMARK 465 PHE B 517
REMARK 465 GLN B 518
REMARK 465 VAL B 519
REMARK 465 GLN B 520
REMARK 465 ASP B 521
REMARK 465 GLY B 522
REMARK 465 ALA B 523
REMARK 465 PRO B 524
REMARK 465 GLY B 525
REMARK 465 THR B 526
REMARK 465 PHE B 527
REMARK 465 ASN B 528
REMARK 465 PHE B 529
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 GLY A 150 NH1 ARG E 87 2.08
REMARK 500 O HOH A 640 O HOH A 703 2.11
REMARK 500 OE1 GLU A 250 O HOH A 601 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 A 71 166.09 62.45
REMARK 500 ASN A 75 67.45 61.88
REMARK 500 ASN A 239 155.73 72.66
REMARK 500 LYS A 432 55.36 -90.09
REMARK 500 GLU A 456 39.24 -140.96
REMARK 500 ARG A 478 50.62 -97.22
REMARK 500 THR B 73 -153.10 -171.14
REMARK 500 VAL B 74 -153.89 88.09
REMARK 500 ASN B 75 174.06 106.25
REMARK 500 LYS B 108 -154.99 -152.78
REMARK 500 CYS B 133 88.64 -162.58
REMARK 500 ASN B 239 159.64 70.87
REMARK 500 ARG B 478 -138.29 -88.17
REMARK 500 HIS B 479 150.37 67.28
REMARK 500 GLU B 480 -175.75 -66.31
REMARK 500 ASN B 481 148.65 69.34
REMARK 500 TYR B 485 -70.48 -55.53
REMARK 500 PHE B 496 -107.02 -129.54
REMARK 500 SER B 497 -147.32 60.42
REMARK 500 VAL B 498 -122.47 67.94
REMARK 500 GLU B 500 -37.35 -166.88
REMARK 500 GLU B 501 142.68 168.50
REMARK 500 GLN C 86 115.14 -162.39
REMARK 500 ALA C 93 -94.87 -91.39
REMARK 500 SER C 94 145.05 -175.58
REMARK 500 ALA D 93 -90.75 -71.16
REMARK 500 SER D 94 157.50 175.50
REMARK 500 LYS D 95 -71.62 -109.81
REMARK 500 ASN E 91 -55.91 -135.70
REMARK 500 ALA E 93 122.14 168.48
REMARK 500 SER E 94 -120.90 -147.95
REMARK 500 LYS E 95 127.35 -178.70
REMARK 500 GLN F 86 129.75 63.42
REMARK 500 ARG F 87 -145.42 -98.68
REMARK 500 ARG F 88 96.08 63.51
REMARK 500 ARG F 90 74.64 -176.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 864 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 865 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A 866 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A 867 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 868 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A 869 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A 870 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A 871 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH A 872 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH A 873 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH A 874 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH A 875 DISTANCE = 8.68 ANGSTROMS
REMARK 525 HOH B 803 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 804 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B 805 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 806 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B 807 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH B 808 DISTANCE = 7.59 ANGSTROMS
REMARK 525 HOH B 809 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH B 810 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH B 811 DISTANCE = 8.44 ANGSTROMS
REMARK 525 HOH B 812 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH B 813 DISTANCE = 9.59 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WPT RELATED DB: PDB
REMARK 900 3WPT CONTAINS HOMODIMERIC STRUCTURE OF DIBB-HUMAN-IMPORTIN-ALPHA1.
DBREF 5B56 A 70 529 UNP P52293 IMA1_MOUSE 70 529
DBREF 5B56 B 70 529 UNP P52293 IMA1_MOUSE 70 529
DBREF 5B56 C 85 96 UNP Q73369 VPR_HV1B9 85 96
DBREF 5B56 D 85 96 UNP Q73369 VPR_HV1B9 85 96
DBREF 5B56 E 85 96 UNP Q73369 VPR_HV1B9 85 96
DBREF 5B56 F 85 96 UNP Q73369 VPR_HV1B9 85 96
SEQRES 1 A 460 ASN GLN GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL
SEQRES 2 A 460 LYS GLY ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN
SEQRES 3 A 460 ALA THR GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS
SEQRES 4 A 460 GLN PRO PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE
SEQRES 5 A 460 PRO LYS PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER
SEQRES 6 A 460 PRO ILE GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE
SEQRES 7 A 460 ALA SER GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP
SEQRES 8 A 460 GLY GLY ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER
SEQRES 9 A 460 PRO HIS ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU
SEQRES 10 A 460 GLY ASN ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU
SEQRES 11 A 460 VAL ILE LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU
SEQRES 12 A 460 LEU ALA VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR
SEQRES 13 A 460 LEU ARG ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG
SEQRES 14 A 460 ASN LYS ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN
SEQRES 15 A 460 ILE LEU PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP
SEQRES 16 A 460 PRO GLU VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR
SEQRES 17 A 460 LEU THR ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL
SEQRES 18 A 460 LYS LYS GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY
SEQRES 19 A 460 ALA THR GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA
SEQRES 20 A 460 ILE GLY ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN
SEQRES 21 A 460 LYS VAL ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER
SEQRES 22 A 460 LEU LEU THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA
SEQRES 23 A 460 THR TRP THR MET SER ASN ILE THR ALA GLY ARG GLN ASP
SEQRES 24 A 460 GLN ILE GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE
SEQRES 25 A 460 LEU VAL GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN
SEQRES 26 A 460 LYS GLU ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY
SEQRES 27 A 460 GLY THR VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY
SEQRES 28 A 460 ILE ILE GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP
SEQRES 29 A 460 THR LYS ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN
SEQRES 30 A 460 ILE PHE GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS
SEQRES 31 A 460 LEU SER ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS
SEQRES 32 A 460 ILE GLU ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR
SEQRES 33 A 460 LYS ALA SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL
SEQRES 34 A 460 GLU GLU GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR
SEQRES 35 A 460 SER GLU GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO
SEQRES 36 A 460 GLY THR PHE ASN PHE
SEQRES 1 B 460 ASN GLN GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL
SEQRES 2 B 460 LYS GLY ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN
SEQRES 3 B 460 ALA THR GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS
SEQRES 4 B 460 GLN PRO PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE
SEQRES 5 B 460 PRO LYS PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER
SEQRES 6 B 460 PRO ILE GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE
SEQRES 7 B 460 ALA SER GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP
SEQRES 8 B 460 GLY GLY ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER
SEQRES 9 B 460 PRO HIS ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU
SEQRES 10 B 460 GLY ASN ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU
SEQRES 11 B 460 VAL ILE LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU
SEQRES 12 B 460 LEU ALA VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR
SEQRES 13 B 460 LEU ARG ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG
SEQRES 14 B 460 ASN LYS ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN
SEQRES 15 B 460 ILE LEU PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP
SEQRES 16 B 460 PRO GLU VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR
SEQRES 17 B 460 LEU THR ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL
SEQRES 18 B 460 LYS LYS GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY
SEQRES 19 B 460 ALA THR GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA
SEQRES 20 B 460 ILE GLY ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN
SEQRES 21 B 460 LYS VAL ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER
SEQRES 22 B 460 LEU LEU THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA
SEQRES 23 B 460 THR TRP THR MET SER ASN ILE THR ALA GLY ARG GLN ASP
SEQRES 24 B 460 GLN ILE GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE
SEQRES 25 B 460 LEU VAL GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN
SEQRES 26 B 460 LYS GLU ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY
SEQRES 27 B 460 GLY THR VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY
SEQRES 28 B 460 ILE ILE GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP
SEQRES 29 B 460 THR LYS ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN
SEQRES 30 B 460 ILE PHE GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS
SEQRES 31 B 460 LEU SER ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS
SEQRES 32 B 460 ILE GLU ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR
SEQRES 33 B 460 LYS ALA SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL
SEQRES 34 B 460 GLU GLU GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR
SEQRES 35 B 460 SER GLU GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO
SEQRES 36 B 460 GLY THR PHE ASN PHE
SEQRES 1 C 12 GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER
SEQRES 1 D 12 GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER
SEQRES 1 E 12 GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER
SEQRES 1 F 12 GLN GLN ARG ARG THR ARG ASN GLY ALA SER LYS SER
FORMUL 7 HOH *512(H2 O)
HELIX 1 AA1 SER A 77 ASN A 86 1 10
HELIX 2 AA2 ASN A 89 SER A 105 1 17
HELIX 3 AA3 PRO A 111 ALA A 118 1 8
HELIX 4 AA4 LEU A 120 GLY A 129 1 10
HELIX 5 AA5 CYS A 133 GLY A 150 1 18
HELIX 6 AA6 THR A 151 GLY A 161 1 11
HELIX 7 AA7 GLY A 162 LEU A 171 1 10
HELIX 8 AA8 HIS A 175 ASP A 192 1 18
HELIX 9 AA9 GLY A 193 HIS A 203 1 11
HELIX 10 AB1 ALA A 205 ALA A 214 1 10
HELIX 11 AB2 ASP A 217 LEU A 221 5 5
HELIX 12 AB3 ALA A 222 LEU A 236 1 15
HELIX 13 AB4 PRO A 245 HIS A 261 1 17
HELIX 14 AB5 ASP A 264 ASP A 280 1 17
HELIX 15 AB6 PRO A 282 LYS A 291 1 10
HELIX 16 AB7 VAL A 294 GLY A 303 1 10
HELIX 17 AB8 GLU A 306 VAL A 321 1 16
HELIX 18 AB9 THR A 324 ALA A 334 1 11
HELIX 19 AC1 GLY A 335 ALA A 338 5 4
HELIX 20 AC2 VAL A 339 THR A 345 1 7
HELIX 21 AC3 LYS A 348 THR A 363 1 16
HELIX 22 AC4 ARG A 366 HIS A 376 1 11
HELIX 23 AC5 LEU A 378 ALA A 389 1 12
HELIX 24 AC6 ASP A 390 GLY A 408 1 19
HELIX 25 AC7 THR A 409 CYS A 419 1 11
HELIX 26 AC8 ILE A 421 LEU A 428 1 8
HELIX 27 AC9 LEU A 429 ALA A 431 5 3
HELIX 28 AD1 ASP A 433 GLY A 455 1 23
HELIX 29 AD2 GLU A 456 CYS A 467 1 12
HELIX 30 AD3 GLY A 468 LEU A 476 1 9
HELIX 31 AD4 GLN A 477 HIS A 479 5 3
HELIX 32 AD5 ASN A 481 PHE A 496 1 16
HELIX 33 AD6 SER B 77 ASN B 86 1 10
HELIX 34 AD7 ASN B 89 ARG B 106 1 18
HELIX 35 AD8 PRO B 111 ALA B 118 1 8
HELIX 36 AD9 LEU B 120 LEU B 128 1 9
HELIX 37 AE1 CYS B 133 SER B 149 1 17
HELIX 38 AE2 THR B 151 GLY B 161 1 11
HELIX 39 AE3 GLY B 162 LEU B 171 1 10
HELIX 40 AE4 HIS B 175 GLY B 191 1 17
HELIX 41 AE5 GLY B 193 HIS B 203 1 11
HELIX 42 AE6 ALA B 205 ALA B 214 1 10
HELIX 43 AE7 ASP B 217 LEU B 221 5 5
HELIX 44 AE8 ALA B 222 CYS B 237 1 16
HELIX 45 AE9 PRO B 245 LEU B 260 1 16
HELIX 46 AF1 ASP B 264 THR B 279 1 16
HELIX 47 AF2 PRO B 282 LYS B 291 1 10
HELIX 48 AF3 VAL B 294 GLY B 303 1 10
HELIX 49 AF4 GLU B 306 THR B 322 1 17
HELIX 50 AF5 THR B 324 ALA B 334 1 11
HELIX 51 AF6 GLY B 335 ALA B 338 5 4
HELIX 52 AF7 VAL B 339 THR B 345 1 7
HELIX 53 AF8 LYS B 348 THR B 363 1 16
HELIX 54 AF9 ARG B 366 HIS B 376 1 11
HELIX 55 AG1 LEU B 378 LYS B 388 1 11
HELIX 56 AG2 ASP B 390 GLY B 408 1 19
HELIX 57 AG3 THR B 409 CYS B 419 1 11
HELIX 58 AG4 ILE B 421 LEU B 428 1 8
HELIX 59 AG5 LEU B 429 ALA B 431 5 3
HELIX 60 AG6 ASP B 433 LYS B 453 1 21
HELIX 61 AG7 GLU B 456 GLU B 466 1 11
HELIX 62 AG8 GLY B 468 LEU B 476 1 9
HELIX 63 AG9 GLU B 482 PHE B 496 1 15
CISPEP 1 ASN A 241 PRO A 242 0 -1.76
CISPEP 2 GLN B 71 GLY B 72 0 -1.90
CISPEP 3 GLU B 107 LYS B 108 0 1.37
CISPEP 4 ASN B 241 PRO B 242 0 -1.63
CISPEP 5 ASN E 91 GLY E 92 0 -5.19
CRYST1 91.021 81.555 101.545 90.00 97.78 90.00 P 1 21 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 0.010986 0.000000 0.001501 0.00000
SCALE2 0.000000 0.012262 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009939 0.00000
(ATOM LINES ARE NOT SHOWN.)
END