HEADER PROTEIN BINDING 07-MAY-18 6GHD
TITLE STRUCTURAL ANALYSIS OF THE TERNARY COMPLEX BETWEEN LAMIN A/C, BAF AND
TITLE 2 EMERIN IDENTIFIES AN INTERFACE DISRUPTED IN AUTOSOMAL RECESSIVE
TITLE 3 PROGEROID DISEASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EMERIN;
COMPND 3 CHAIN: G, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BARRIER-TO-AUTOINTEGRATION FACTOR;
COMPND 7 CHAIN: D, E, A, C;
COMPND 8 SYNONYM: BREAKPOINT CLUSTER REGION PROTEIN 1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PRELAMIN-A/C;
COMPND 12 CHAIN: B, F;
COMPND 13 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: EMD, EDMD, STA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: BANF1, BAF, BCRG1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: LMNA, LMN1;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEAR ENVELOPE, GENE EXPRESSION, TERNARY COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SAMSON,A.PETITALOT,F.CELLI,I.HERRADA,V.ROPARS,M.H.LEDU,N.NHIRI,
AUTHOR 2 A.A.ARTENI,B.BUENDIA,S.ZINNJUSTIN
REVDAT 4 17-JAN-24 6GHD 1 REMARK
REVDAT 3 14-NOV-18 6GHD 1 JRNL
REVDAT 2 29-AUG-18 6GHD 1 JRNL
REVDAT 1 08-AUG-18 6GHD 0
JRNL AUTH C.SAMSON,A.PETITALOT,F.CELLI,I.HERRADA,V.ROPARS,M.H.LE DU,
JRNL AUTH 2 N.NHIRI,E.JACQUET,A.A.ARTENI,B.BUENDIA,S.ZINN-JUSTIN
JRNL TITL STRUCTURAL ANALYSIS OF THE TERNARY COMPLEX BETWEEN LAMIN
JRNL TITL 2 A/C, BAF AND EMERIN IDENTIFIES AN INTERFACE DISRUPTED IN
JRNL TITL 3 AUTOSOMAL RECESSIVE PROGEROID DISEASES.
JRNL REF NUCLEIC ACIDS RES. V. 46 10460 2018
JRNL REFN ESSN 1362-4962
JRNL PMID 30137533
JRNL DOI 10.1093/NAR/GKY736
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 83934
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 4187
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 49.1654 - 6.5203 0.97 2697 143 0.1411 0.1699
REMARK 3 2 6.5203 - 5.1772 0.99 2721 141 0.1588 0.2078
REMARK 3 3 5.1772 - 4.5233 0.96 2689 142 0.1292 0.1977
REMARK 3 4 4.5233 - 4.1099 0.96 2651 138 0.1268 0.1537
REMARK 3 5 4.1099 - 3.8155 0.94 2631 137 0.1391 0.2090
REMARK 3 6 3.8155 - 3.5906 0.96 2673 143 0.1490 0.2270
REMARK 3 7 3.5906 - 3.4108 0.96 2631 139 0.1598 0.2184
REMARK 3 8 3.4108 - 3.2624 0.97 2711 144 0.1691 0.2073
REMARK 3 9 3.2624 - 3.1368 0.97 2658 139 0.1838 0.2314
REMARK 3 10 3.1368 - 3.0286 0.97 2695 146 0.1885 0.2571
REMARK 3 11 3.0286 - 2.9339 0.97 2698 142 0.1786 0.2335
REMARK 3 12 2.9339 - 2.8500 0.96 2687 143 0.1884 0.2674
REMARK 3 13 2.8500 - 2.7750 0.97 2650 140 0.2104 0.2845
REMARK 3 14 2.7750 - 2.7073 0.96 2694 143 0.2302 0.3353
REMARK 3 15 2.7073 - 2.6458 0.96 2678 138 0.2301 0.3023
REMARK 3 16 2.6458 - 2.5895 0.96 2604 138 0.2498 0.2974
REMARK 3 17 2.5895 - 2.5377 0.96 2732 143 0.2471 0.3122
REMARK 3 18 2.5377 - 2.4898 0.96 2584 135 0.2579 0.2756
REMARK 3 19 2.4898 - 2.4453 0.95 2722 141 0.2583 0.3241
REMARK 3 20 2.4453 - 2.4039 0.96 2597 136 0.2731 0.3086
REMARK 3 21 2.4039 - 2.3651 0.95 2711 141 0.2950 0.3702
REMARK 3 22 2.3651 - 2.3287 0.95 2586 134 0.2968 0.3589
REMARK 3 23 2.3287 - 2.2945 0.93 2644 139 0.3064 0.3360
REMARK 3 24 2.2945 - 2.2621 0.95 2587 136 0.2982 0.3125
REMARK 3 25 2.2621 - 2.2316 0.95 2589 137 0.3163 0.3108
REMARK 3 26 2.2316 - 2.2026 0.95 2766 140 0.3135 0.3670
REMARK 3 27 2.2026 - 2.1751 0.95 2494 132 0.3216 0.3934
REMARK 3 28 2.1751 - 2.1489 0.94 2660 141 0.3422 0.3716
REMARK 3 29 2.1489 - 2.1239 0.95 2684 139 0.3688 0.3760
REMARK 3 30 2.1239 - 2.1000 0.95 2623 137 0.3809 0.4908
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.75
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 : 0.008 5490
REMARK 3 ANGLE : 0.929 7397
REMARK 3 CHIRALITY : 0.054 779
REMARK 3 PLANARITY : 0.006 962
REMARK 3 DIHEDRAL : 16.969 3262
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'G' AND RESID 1 THROUGH 45)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.0664 -54.3347 -11.6602
REMARK 3 T TENSOR
REMARK 3 T11: 0.3432 T22: 0.2097
REMARK 3 T33: 0.2946 T12: -0.0454
REMARK 3 T13: -0.0082 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 7.3328 L22: 6.0372
REMARK 3 L33: 6.3238 L12: 1.9550
REMARK 3 L13: 0.1515 L23: -0.8447
REMARK 3 S TENSOR
REMARK 3 S11: 0.3161 S12: -0.2213 S13: -0.6317
REMARK 3 S21: 0.3268 S22: -0.1591 S23: -0.0105
REMARK 3 S31: 0.9096 S32: -0.4144 S33: -0.1157
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'D' AND RESID 3 THROUGH 89)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0457 -33.2013 -3.0591
REMARK 3 T TENSOR
REMARK 3 T11: 0.2130 T22: 0.2292
REMARK 3 T33: 0.2015 T12: 0.0155
REMARK 3 T13: 0.0248 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 5.2375 L22: 4.8451
REMARK 3 L33: 5.0068 L12: 2.2401
REMARK 3 L13: -0.8615 L23: 0.6893
REMARK 3 S TENSOR
REMARK 3 S11: 0.1915 S12: -0.2598 S13: 0.1621
REMARK 3 S21: 0.1790 S22: -0.1480 S23: 0.1379
REMARK 3 S31: -0.0814 S32: -0.1383 S33: -0.0414
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 428 THROUGH 546)
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0914 -13.7589 -17.4312
REMARK 3 T TENSOR
REMARK 3 T11: 0.3226 T22: 0.2559
REMARK 3 T33: 0.2363 T12: 0.0010
REMARK 3 T13: 0.0017 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 3.3483 L22: 2.6347
REMARK 3 L33: 4.9294 L12: -0.0256
REMARK 3 L13: 0.6592 L23: 0.1371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: 0.1022 S13: 0.2152
REMARK 3 S21: -0.1290 S22: -0.0089 S23: -0.0119
REMARK 3 S31: -0.5224 S32: 0.1075 S33: 0.0939
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'E' AND RESID 2 THROUGH 89)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3008 -44.3476 -13.1617
REMARK 3 T TENSOR
REMARK 3 T11: 0.2034 T22: 0.2786
REMARK 3 T33: 0.2198 T12: 0.0792
REMARK 3 T13: -0.0295 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 3.7904 L22: 6.4309
REMARK 3 L33: 3.8006 L12: 0.0898
REMARK 3 L13: -0.7837 L23: 0.2669
REMARK 3 S TENSOR
REMARK 3 S11: 0.1448 S12: 0.1115 S13: -0.1827
REMARK 3 S21: -0.0929 S22: -0.1329 S23: -0.2549
REMARK 3 S31: 0.1803 S32: 0.3354 S33: -0.0031
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 2 THROUGH 89)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1239 -14.5217 14.6154
REMARK 3 T TENSOR
REMARK 3 T11: 0.2364 T22: 0.2311
REMARK 3 T33: 0.2404 T12: 0.0601
REMARK 3 T13: 0.0274 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 6.3875 L22: 3.0872
REMARK 3 L33: 5.1594 L12: 0.4793
REMARK 3 L13: 0.0124 L23: -1.4616
REMARK 3 S TENSOR
REMARK 3 S11: 0.1163 S12: -0.0019 S13: -0.2972
REMARK 3 S21: -0.1644 S22: -0.2107 S23: -0.2862
REMARK 3 S31: 0.3295 S32: 0.4667 S33: 0.0594
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'C' AND RESID 3 THROUGH 89)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1596 2.1436 5.6773
REMARK 3 T TENSOR
REMARK 3 T11: 0.1926 T22: 0.2240
REMARK 3 T33: 0.1988 T12: 0.0239
REMARK 3 T13: 0.0095 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 4.2376 L22: 5.9738
REMARK 3 L33: 6.3343 L12: 1.9301
REMARK 3 L13: 0.0026 L23: -1.2548
REMARK 3 S TENSOR
REMARK 3 S11: -0.1144 S12: 0.1544 S13: 0.1489
REMARK 3 S21: -0.0774 S22: 0.1910 S23: 0.2312
REMARK 3 S31: -0.1245 S32: -0.1629 S33: -0.0611
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'F' AND RESID 429 THROUGH 546)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9791 -18.4551 20.1501
REMARK 3 T TENSOR
REMARK 3 T11: 0.1996 T22: 0.2552
REMARK 3 T33: 0.2247 T12: 0.0172
REMARK 3 T13: -0.0100 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 2.7817 L22: 2.7750
REMARK 3 L33: 4.0341 L12: 0.2120
REMARK 3 L13: -0.6311 L23: 0.1819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0501 S12: 0.0264 S13: 0.0128
REMARK 3 S21: -0.0871 S22: 0.0162 S23: 0.1081
REMARK 3 S31: 0.1011 S32: -0.2536 S33: 0.0393
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'H' AND RESID 2 THROUGH 44)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6989 9.3206 13.7761
REMARK 3 T TENSOR
REMARK 3 T11: 0.2597 T22: 0.3342
REMARK 3 T33: 0.2763 T12: -0.0620
REMARK 3 T13: 0.0163 T23: 0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 5.5390 L22: 7.9790
REMARK 3 L33: 6.1946 L12: 3.6359
REMARK 3 L13: 0.2333 L23: 0.9603
REMARK 3 S TENSOR
REMARK 3 S11: -0.1885 S12: 0.2099 S13: 0.0742
REMARK 3 S21: -0.3640 S22: 0.1523 S23: -0.6616
REMARK 3 S31: -0.6188 S32: 0.7925 S33: 0.0528
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN G AND (RESID 2 THROUGH 10 OR
REMARK 3 (RESID 11 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 12
REMARK 3 THROUGH 44))
REMARK 3 SELECTION : CHAIN H
REMARK 3 ATOM PAIRS NUMBER : 432
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN B AND (RESID 429 THROUGH 452 OR
REMARK 3 RESID 454 THROUGH 546))
REMARK 3 SELECTION : (CHAIN F AND (RESID 429 THROUGH 452 OR
REMARK 3 RESID 454 THROUGH 546))
REMARK 3 ATOM PAIRS NUMBER : 1102
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 3 THROUGH 89)
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 1703
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 3 THROUGH 89)
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 1703
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 3 THROUGH 89)
REMARK 3 SELECTION : (CHAIN E AND RESID 3 THROUGH 89)
REMARK 3 ATOM PAIRS NUMBER : 1703
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6GHD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200007625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9725
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : APEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83934
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 49.152
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 3.520
REMARK 200 R MERGE (I) : 0.11730
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 6.52
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.79550
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: MOLREP
REMARK 200 STARTING MODEL: 2BZF, 1IFR, 2ODC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3.350, 20MM TRIS-BISPH5.5, 30MM
REMARK 280 NACL, 0.2M NH4SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, D, B, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, F, H
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 THR D 2
REMARK 465 THR C 2
REMARK 465 SER F 428
REMARK 465 GLY H 1
REMARK 465 ARG H 45
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 H 11 CG CD OE1 OE2
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 LEU G 7 NH2 ARG G 31 2.15
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 SER B 429 -32.63 64.18
REMARK 500 SER B 507 79.65 -157.31
REMARK 500 SER F 507 79.17 -155.63
REMARK 500 ASN H 3 -13.90 104.11
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 G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 101
DBREF 6GHD G 2 45 UNP P50402 EMD_HUMAN 2 45
DBREF 6GHD D 2 89 UNP O75531 BAF_HUMAN 2 89
DBREF 6GHD B 428 546 UNP P02545 LMNA_HUMAN 428 546
DBREF 6GHD E 2 89 UNP O75531 BAF_HUMAN 2 89
DBREF 6GHD A 2 89 UNP O75531 BAF_HUMAN 2 89
DBREF 6GHD C 2 89 UNP O75531 BAF_HUMAN 2 89
DBREF 6GHD F 428 546 UNP P02545 LMNA_HUMAN 428 546
DBREF 6GHD H 2 45 UNP P50402 EMD_HUMAN 2 45
SEQADV 6GHD GLY G 1 UNP P50402 EXPRESSION TAG
SEQADV 6GHD ALA D 67 UNP O75531 CYS 67 ENGINEERED MUTATION
SEQADV 6GHD ALA D 77 UNP O75531 CYS 77 ENGINEERED MUTATION
SEQADV 6GHD ALA D 80 UNP O75531 CYS 80 ENGINEERED MUTATION
SEQADV 6GHD ALA D 85 UNP O75531 CYS 85 ENGINEERED MUTATION
SEQADV 6GHD ALA E 67 UNP O75531 CYS 67 ENGINEERED MUTATION
SEQADV 6GHD ALA E 77 UNP O75531 CYS 77 ENGINEERED MUTATION
SEQADV 6GHD ALA E 80 UNP O75531 CYS 80 ENGINEERED MUTATION
SEQADV 6GHD ALA E 85 UNP O75531 CYS 85 ENGINEERED MUTATION
SEQADV 6GHD ALA A 67 UNP O75531 CYS 67 ENGINEERED MUTATION
SEQADV 6GHD ALA A 77 UNP O75531 CYS 77 ENGINEERED MUTATION
SEQADV 6GHD ALA A 80 UNP O75531 CYS 80 ENGINEERED MUTATION
SEQADV 6GHD ALA A 85 UNP O75531 CYS 85 ENGINEERED MUTATION
SEQADV 6GHD ALA C 67 UNP O75531 CYS 67 ENGINEERED MUTATION
SEQADV 6GHD ALA C 77 UNP O75531 CYS 77 ENGINEERED MUTATION
SEQADV 6GHD ALA C 80 UNP O75531 CYS 80 ENGINEERED MUTATION
SEQADV 6GHD ALA C 85 UNP O75531 CYS 85 ENGINEERED MUTATION
SEQADV 6GHD GLY H 1 UNP P50402 EXPRESSION TAG
SEQRES 1 G 45 GLY ASP ASN TYR ALA ASP LEU SER ASP THR GLU LEU THR
SEQRES 2 G 45 THR LEU LEU ARG ARG TYR ASN ILE PRO HIS GLY PRO VAL
SEQRES 3 G 45 VAL GLY SER THR ARG ARG LEU TYR GLU LYS LYS ILE PHE
SEQRES 4 G 45 GLU TYR GLU THR GLN ARG
SEQRES 1 D 88 THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU PRO
SEQRES 2 D 88 MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE GLY
SEQRES 3 D 88 GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE ASP
SEQRES 4 D 88 LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU LYS
SEQRES 5 D 88 LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP THR
SEQRES 6 D 88 ALA GLY ALA ASN ALA LYS GLN SER ARG ASP ALA PHE GLY
SEQRES 7 D 88 ALA LEU ARG GLU TRP ALA ASP ALA PHE LEU
SEQRES 1 B 119 SER SER PHE SER GLN HIS ALA ARG THR SER GLY ARG VAL
SEQRES 2 B 119 ALA VAL GLU GLU VAL ASP GLU GLU GLY LYS PHE VAL ARG
SEQRES 3 B 119 LEU ARG ASN LYS SER ASN GLU ASP GLN SER MET GLY ASN
SEQRES 4 B 119 TRP GLN ILE LYS ARG GLN ASN GLY ASP ASP PRO LEU LEU
SEQRES 5 B 119 THR TYR ARG PHE PRO PRO LYS PHE THR LEU LYS ALA GLY
SEQRES 6 B 119 GLN VAL VAL THR ILE TRP ALA ALA GLY ALA GLY ALA THR
SEQRES 7 B 119 HIS SER PRO PRO THR ASP LEU VAL TRP LYS ALA GLN ASN
SEQRES 8 B 119 THR TRP GLY CYS GLY ASN SER LEU ARG THR ALA LEU ILE
SEQRES 9 B 119 ASN SER THR GLY GLU GLU VAL ALA MET ARG LYS LEU VAL
SEQRES 10 B 119 ARG SER
SEQRES 1 E 88 THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU PRO
SEQRES 2 E 88 MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE GLY
SEQRES 3 E 88 GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE ASP
SEQRES 4 E 88 LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU LYS
SEQRES 5 E 88 LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP THR
SEQRES 6 E 88 ALA GLY ALA ASN ALA LYS GLN SER ARG ASP ALA PHE GLY
SEQRES 7 E 88 ALA LEU ARG GLU TRP ALA ASP ALA PHE LEU
SEQRES 1 A 88 THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU PRO
SEQRES 2 A 88 MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE GLY
SEQRES 3 A 88 GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE ASP
SEQRES 4 A 88 LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU LYS
SEQRES 5 A 88 LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP THR
SEQRES 6 A 88 ALA GLY ALA ASN ALA LYS GLN SER ARG ASP ALA PHE GLY
SEQRES 7 A 88 ALA LEU ARG GLU TRP ALA ASP ALA PHE LEU
SEQRES 1 C 88 THR THR SER GLN LYS HIS ARG ASP PHE VAL ALA GLU PRO
SEQRES 2 C 88 MET GLY GLU LYS PRO VAL GLY SER LEU ALA GLY ILE GLY
SEQRES 3 C 88 GLU VAL LEU GLY LYS LYS LEU GLU GLU ARG GLY PHE ASP
SEQRES 4 C 88 LYS ALA TYR VAL VAL LEU GLY GLN PHE LEU VAL LEU LYS
SEQRES 5 C 88 LYS ASP GLU ASP LEU PHE ARG GLU TRP LEU LYS ASP THR
SEQRES 6 C 88 ALA GLY ALA ASN ALA LYS GLN SER ARG ASP ALA PHE GLY
SEQRES 7 C 88 ALA LEU ARG GLU TRP ALA ASP ALA PHE LEU
SEQRES 1 F 119 SER SER PHE SER GLN HIS ALA ARG THR SER GLY ARG VAL
SEQRES 2 F 119 ALA VAL GLU GLU VAL ASP GLU GLU GLY LYS PHE VAL ARG
SEQRES 3 F 119 LEU ARG ASN LYS SER ASN GLU ASP GLN SER MET GLY ASN
SEQRES 4 F 119 TRP GLN ILE LYS ARG GLN ASN GLY ASP ASP PRO LEU LEU
SEQRES 5 F 119 THR TYR ARG PHE PRO PRO LYS PHE THR LEU LYS ALA GLY
SEQRES 6 F 119 GLN VAL VAL THR ILE TRP ALA ALA GLY ALA GLY ALA THR
SEQRES 7 F 119 HIS SER PRO PRO THR ASP LEU VAL TRP LYS ALA GLN ASN
SEQRES 8 F 119 THR TRP GLY CYS GLY ASN SER LEU ARG THR ALA LEU ILE
SEQRES 9 F 119 ASN SER THR GLY GLU GLU VAL ALA MET ARG LYS LEU VAL
SEQRES 10 F 119 ARG SER
SEQRES 1 H 45 GLY ASP ASN TYR ALA ASP LEU SER ASP THR GLU LEU THR
SEQRES 2 H 45 THR LEU LEU ARG ARG TYR ASN ILE PRO HIS GLY PRO VAL
SEQRES 3 H 45 VAL GLY SER THR ARG ARG LEU TYR GLU LYS LYS ILE PHE
SEQRES 4 H 45 GLU TYR GLU THR GLN ARG
HET SO4 G 101 5
HET SO4 D 101 5
HET SO4 D 102 5
HET SO4 E 101 5
HET SO4 E 102 5
HET SO4 A 101 5
HET EDO A 102 4
HET SO4 C 101 5
HET SO4 H 101 5
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 SO4 8(O4 S 2-)
FORMUL 15 EDO C2 H6 O2
FORMUL 18 HOH *280(H2 O)
HELIX 1 AA1 SER G 8 TYR G 19 1 12
HELIX 2 AA2 THR G 30 GLN G 44 1 15
HELIX 3 AA3 SER D 4 ALA D 12 1 9
HELIX 4 AA4 PRO D 19 LEU D 23 5 5
HELIX 5 AA5 GLY D 27 ARG D 37 1 11
HELIX 6 AA6 LYS D 41 LEU D 52 1 12
HELIX 7 AA7 ASP D 55 GLY D 68 1 14
HELIX 8 AA8 ASN D 70 LEU D 89 1 20
HELIX 9 AA9 GLY B 501 GLY B 503 5 3
HELIX 10 AB1 SER E 4 ALA E 12 1 9
HELIX 11 AB2 PRO E 19 LEU E 23 5 5
HELIX 12 AB3 GLY E 27 ARG E 37 1 11
HELIX 13 AB4 LYS E 41 LEU E 52 1 12
HELIX 14 AB5 ASP E 55 GLY E 68 1 14
HELIX 15 AB6 ASN E 70 LEU E 89 1 20
HELIX 16 AB7 SER A 4 ALA A 12 1 9
HELIX 17 AB8 PRO A 19 LEU A 23 5 5
HELIX 18 AB9 GLY A 27 ARG A 37 1 11
HELIX 19 AC1 LYS A 41 LEU A 52 1 12
HELIX 20 AC2 ASP A 55 GLY A 68 1 14
HELIX 21 AC3 ASN A 70 LEU A 89 1 20
HELIX 22 AC4 SER C 4 ALA C 12 1 9
HELIX 23 AC5 PRO C 19 LEU C 23 5 5
HELIX 24 AC6 GLY C 27 ARG C 37 1 11
HELIX 25 AC7 LYS C 41 LEU C 52 1 12
HELIX 26 AC8 ASP C 55 GLY C 68 1 14
HELIX 27 AC9 ASN C 70 LEU C 89 1 20
HELIX 28 AD1 GLY F 501 GLY F 503 5 3
HELIX 29 AD2 SER H 8 TYR H 19 1 12
HELIX 30 AD3 THR H 30 GLN H 44 1 15
SHEET 1 AA1 5 PHE B 430 THR B 436 0
SHEET 2 AA1 5 GLU B 537 ARG B 545 -1 O LYS B 542 N HIS B 433
SHEET 3 AA1 5 SER B 525 ILE B 531 -1 N LEU B 526 O LEU B 543
SHEET 4 AA1 5 GLN B 468 ASN B 473 -1 N GLN B 468 O ILE B 531
SHEET 5 AA1 5 LEU B 479 ARG B 482 -1 O LEU B 479 N ARG B 471
SHEET 1 AA2 4 VAL B 440 VAL B 445 0
SHEET 2 AA2 4 PHE B 451 ASN B 456 -1 O ARG B 453 N GLU B 444
SHEET 3 AA2 4 VAL B 494 ALA B 499 -1 O ILE B 497 N VAL B 452
SHEET 4 AA2 4 ASP B 511 TRP B 514 1 O TRP B 514 N TRP B 498
SHEET 1 AA3 2 GLN B 462 SER B 463 0
SHEET 2 AA3 2 THR B 488 LEU B 489 -1 O LEU B 489 N GLN B 462
SHEET 1 AA4 5 PHE F 430 THR F 436 0
SHEET 2 AA4 5 GLU F 537 ARG F 545 -1 O LYS F 542 N HIS F 433
SHEET 3 AA4 5 SER F 525 ILE F 531 -1 N LEU F 530 O VAL F 538
SHEET 4 AA4 5 GLN F 468 ASN F 473 -1 N GLN F 468 O ILE F 531
SHEET 5 AA4 5 LEU F 479 ARG F 482 -1 O LEU F 479 N ARG F 471
SHEET 1 AA5 4 VAL F 440 VAL F 445 0
SHEET 2 AA5 4 PHE F 451 ASN F 456 -1 O ARG F 455 N ALA F 441
SHEET 3 AA5 4 VAL F 494 ALA F 499 -1 O VAL F 495 N LEU F 454
SHEET 4 AA5 4 ASP F 511 TRP F 514 1 O TRP F 514 N TRP F 498
SHEET 1 AA6 2 GLN F 462 SER F 463 0
SHEET 2 AA6 2 THR F 488 LEU F 489 -1 O LEU F 489 N GLN F 462
CISPEP 1 PRO B 508 PRO B 509 0 5.48
CISPEP 2 PRO F 508 PRO F 509 0 5.83
SITE 1 AC1 5 ARG F 482 ARG G 17 HIS G 23 HOH G 201
SITE 2 AC1 5 HOH G 206
SITE 1 AC2 5 GLY D 27 GLU D 28 VAL D 29 LEU D 30
SITE 2 AC2 5 GLN D 73
SITE 1 AC3 2 ARG D 60 ARG D 75
SITE 1 AC4 8 SER E 4 LYS E 6 ALA E 24 GLY E 25
SITE 2 AC4 8 ASP E 76 HOH E 207 HOH E 211 HOH E 222
SITE 1 AC5 6 GLY C 27 GLU C 28 VAL C 29 ARG E 60
SITE 2 AC5 6 ARG E 75 HOH E 216
SITE 1 AC6 5 SER A 4 ALA A 24 GLY A 25 HOH A 203
SITE 2 AC6 5 HOH A 221
SITE 1 AC7 4 ARG A 60 ARG A 75 LYS D 6 HOH D 203
SITE 1 AC8 2 ARG C 60 ARG C 75
SITE 1 AC9 5 ARG B 482 ARG H 17 HIS H 23 HOH H 201
SITE 2 AC9 5 HOH H 208
CRYST1 57.770 62.750 64.340 66.44 66.55 88.05 P 1 4
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 0.017310 -0.000589 -0.008005 0.00000
SCALE2 0.000000 0.015945 -0.007405 0.00000
SCALE3 0.000000 0.000000 0.018679 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
