HEADER PEPTIDE BINDING PROTEIN 10-NOV-15 5EOU
TITLE PSEUDOMONAS AERUGINOSA PILM:PILN1-12 BOUND TO ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYPE 4 FIMBRIAL BIOGENESIS PROTEIN PILM,TYPE 4 FIMBRIAL
COMPND 3 BIOGENESIS PROTEIN PILN;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 /
SOURCE 3 PAO1 / 1C / PRS 101 / LMG 12228), PSEUDOMONAS AERUGINOSA;
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 6 ATCC: 15692;
SOURCE 7 GENE: PILM, PA5044, PILN, PA5043;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS PILM, PILN, TYPE IV PILUS, T4P, PEPTIDE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MCCALLUM,S.TAMMAM,H.ROBINSON,M.SHAH,C.CALMETTES,T.MORAES,L.BURROWS,
AUTHOR 2 L.P.HOWELL
REVDAT 3 27-SEP-23 5EOU 1 JRNL REMARK LINK ATOM
REVDAT 2 08-JUN-16 5EOU 1 JRNL
REVDAT 1 27-APR-16 5EOU 0
JRNL AUTH M.MCCALLUM,S.TAMMAM,D.J.LITTLE,H.ROBINSON,J.KOO,M.SHAH,
JRNL AUTH 2 C.CALMETTES,T.F.MORAES,L.L.BURROWS,P.L.HOWELL
JRNL TITL PILN BINDING MODULATES THE STRUCTURE AND BINDING PARTNERS OF
JRNL TITL 2 THE PSEUDOMONAS AERUGINOSA TYPE IVA PILUS PROTEIN PILM.
JRNL REF J.BIOL.CHEM. V. 291 11003 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27022027
JRNL DOI 10.1074/JBC.M116.718353
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1639
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29964
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1600
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 39.5018 - 6.7146 0.99 2543 161 0.1763 0.1857
REMARK 3 2 6.7146 - 5.3337 1.00 2572 174 0.1962 0.2308
REMARK 3 3 5.3337 - 4.6607 1.00 2708 0 0.1769 0.0000
REMARK 3 4 4.6607 - 4.2351 1.00 2586 170 0.1662 0.1793
REMARK 3 5 4.2351 - 3.9319 1.00 2528 182 0.1839 0.2027
REMARK 3 6 3.9319 - 3.7002 1.00 2580 178 0.1913 0.2372
REMARK 3 7 3.7002 - 3.5150 1.00 2525 184 0.2069 0.2275
REMARK 3 8 3.5150 - 3.3621 1.00 2729 0 0.2287 0.0000
REMARK 3 9 3.3621 - 3.2327 1.00 2567 184 0.2346 0.2618
REMARK 3 10 3.2327 - 3.1212 1.00 2524 178 0.2535 0.2948
REMARK 3 11 3.1212 - 3.0237 1.00 2540 186 0.2684 0.3385
REMARK 3 12 3.0237 - 2.9373 1.00 2757 0 0.2609 0.0000
REMARK 3 13 2.9373 - 2.8600 1.00 2512 180 0.2767 0.3108
REMARK 3 14 2.8600 - 2.7902 1.00 2564 182 0.2683 0.3112
REMARK 3 15 2.7902 - 2.7268 1.00 2561 182 0.2659 0.2593
REMARK 3 16 2.7268 - 2.6688 1.00 2714 0 0.2642 0.0000
REMARK 3 17 2.6688 - 2.6154 1.00 2553 183 0.2733 0.3233
REMARK 3 18 2.6154 - 2.5661 1.00 2527 186 0.2789 0.2794
REMARK 3 19 2.5661 - 2.5202 1.00 2542 186 0.2565 0.2975
REMARK 3 20 2.5202 - 2.4775 1.00 2687 0 0.2754 0.0000
REMARK 3 21 2.4775 - 2.4376 1.00 2521 185 0.2962 0.3324
REMARK 3 22 2.4376 - 2.4001 1.00 2550 178 0.3148 0.3386
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.080
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 : 0.003 5021
REMARK 3 ANGLE : 0.639 6835
REMARK 3 CHIRALITY : 0.025 844
REMARK 3 PLANARITY : 0.004 868
REMARK 3 DIHEDRAL : 11.227 1750
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 81)
REMARK 3 ORIGIN FOR THE GROUP (A): 332.4295 217.7378 179.3715
REMARK 3 T TENSOR
REMARK 3 T11: 0.2803 T22: 0.5940
REMARK 3 T33: 0.4932 T12: -0.0554
REMARK 3 T13: 0.0007 T23: -0.0664
REMARK 3 L TENSOR
REMARK 3 L11: 4.8018 L22: 5.1285
REMARK 3 L33: 5.6875 L12: 1.0473
REMARK 3 L13: 0.6584 L23: 1.0048
REMARK 3 S TENSOR
REMARK 3 S11: -0.1119 S12: -0.1163 S13: -0.1680
REMARK 3 S21: -0.0043 S22: -0.1035 S23: -0.3401
REMARK 3 S31: 0.0069 S32: 0.1335 S33: 0.2381
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 323.0865 242.9331 171.6443
REMARK 3 T TENSOR
REMARK 3 T11: 0.6781 T22: 0.8442
REMARK 3 T33: 0.6693 T12: 0.3056
REMARK 3 T13: 0.1354 T23: -0.1580
REMARK 3 L TENSOR
REMARK 3 L11: 8.4863 L22: 10.2971
REMARK 3 L33: 6.5373 L12: 0.9978
REMARK 3 L13: 1.5906 L23: -4.3598
REMARK 3 S TENSOR
REMARK 3 S11: 0.5706 S12: 0.2648 S13: 0.1101
REMARK 3 S21: -0.3192 S22: -0.0291 S23: 1.2491
REMARK 3 S31: -0.8330 S32: -1.5708 S33: -0.3432
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 148 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 329.8025 226.9749 176.0108
REMARK 3 T TENSOR
REMARK 3 T11: 0.3478 T22: 0.6418
REMARK 3 T33: 0.4922 T12: -0.0070
REMARK 3 T13: 0.0567 T23: -0.0873
REMARK 3 L TENSOR
REMARK 3 L11: 7.8302 L22: 3.3290
REMARK 3 L33: 2.3344 L12: 4.4628
REMARK 3 L13: 4.8374 L23: 0.9682
REMARK 3 S TENSOR
REMARK 3 S11: -0.2486 S12: -0.0656 S13: 0.6473
REMARK 3 S21: 0.0134 S22: -0.1378 S23: 0.4539
REMARK 3 S31: -0.0294 S32: -0.6051 S33: 0.3940
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): 311.9424 225.6468 179.0365
REMARK 3 T TENSOR
REMARK 3 T11: 0.4619 T22: 0.5297
REMARK 3 T33: 0.5072 T12: 0.0142
REMARK 3 T13: 0.0536 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 8.8516 L22: 6.4956
REMARK 3 L33: 6.3692 L12: -1.0568
REMARK 3 L13: -0.1878 L23: -2.5310
REMARK 3 S TENSOR
REMARK 3 S11: 0.0277 S12: 0.6805 S13: 0.2820
REMARK 3 S21: -0.2799 S22: 0.2515 S23: 0.1838
REMARK 3 S31: -0.9510 S32: -0.0902 S33: -0.3225
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 224 THROUGH 265 )
REMARK 3 ORIGIN FOR THE GROUP (A): 316.5019 211.7310 201.0026
REMARK 3 T TENSOR
REMARK 3 T11: 1.0208 T22: 1.0217
REMARK 3 T33: 0.6710 T12: 0.0327
REMARK 3 T13: -0.0284 T23: 0.1321
REMARK 3 L TENSOR
REMARK 3 L11: 8.9452 L22: 7.1122
REMARK 3 L33: 8.8754 L12: -1.7577
REMARK 3 L13: 1.8526 L23: -2.2701
REMARK 3 S TENSOR
REMARK 3 S11: -0.2795 S12: -0.0249 S13: -0.1504
REMARK 3 S21: 1.9526 S22: -0.2965 S23: -0.7521
REMARK 3 S31: 0.8425 S32: 0.5430 S33: 0.4442
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 266 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 305.3907 221.7692 185.0142
REMARK 3 T TENSOR
REMARK 3 T11: 0.3168 T22: 0.5353
REMARK 3 T33: 0.4657 T12: -0.0010
REMARK 3 T13: 0.0438 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 10.3350 L22: 8.8998
REMARK 3 L33: 7.6908 L12: -0.5066
REMARK 3 L13: 1.3735 L23: 0.0544
REMARK 3 S TENSOR
REMARK 3 S11: 0.0779 S12: -0.3685 S13: 0.0082
REMARK 3 S21: 0.0993 S22: 0.1145 S23: 1.0736
REMARK 3 S31: -0.4146 S32: -0.6810 S33: -0.2940
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): 323.2577 212.9322 173.4313
REMARK 3 T TENSOR
REMARK 3 T11: 0.3191 T22: 0.6301
REMARK 3 T33: 0.4464 T12: -0.0523
REMARK 3 T13: 0.0351 T23: -0.1818
REMARK 3 L TENSOR
REMARK 3 L11: 7.6113 L22: 6.6693
REMARK 3 L33: 6.7331 L12: 3.4000
REMARK 3 L13: -0.5202 L23: -3.0022
REMARK 3 S TENSOR
REMARK 3 S11: -0.2988 S12: 0.5028 S13: -0.3186
REMARK 3 S21: -0.4850 S22: 0.3790 S23: 0.0472
REMARK 3 S31: 0.5997 S32: -0.3078 S33: -0.0923
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 81)
REMARK 3 ORIGIN FOR THE GROUP (A): 355.4461 238.8668 179.5549
REMARK 3 T TENSOR
REMARK 3 T11: 0.2704 T22: 0.3734
REMARK 3 T33: 0.4704 T12: -0.0276
REMARK 3 T13: -0.0593 T23: -0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 2.3448 L22: 2.9494
REMARK 3 L33: 4.9087 L12: 0.1143
REMARK 3 L13: 0.9189 L23: -0.5448
REMARK 3 S TENSOR
REMARK 3 S11: -0.1015 S12: -0.1040 S13: 0.3298
REMARK 3 S21: -0.0178 S22: -0.0364 S23: 0.3803
REMARK 3 S31: -0.2993 S32: -0.2897 S33: 0.1652
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 82 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 363.5140 211.9026 171.1587
REMARK 3 T TENSOR
REMARK 3 T11: 0.6528 T22: 0.6048
REMARK 3 T33: 0.8568 T12: 0.1398
REMARK 3 T13: -0.0854 T23: 0.1467
REMARK 3 L TENSOR
REMARK 3 L11: 3.6671 L22: 4.7687
REMARK 3 L33: 9.9931 L12: 1.7833
REMARK 3 L13: -3.5826 L23: 1.3853
REMARK 3 S TENSOR
REMARK 3 S11: -0.5368 S12: -0.5465 S13: -0.8329
REMARK 3 S21: -0.4173 S22: -0.2352 S23: -0.2053
REMARK 3 S31: 0.9730 S32: 1.0124 S33: 0.8017
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 357.8679 229.7845 176.0171
REMARK 3 T TENSOR
REMARK 3 T11: 0.3397 T22: 0.5653
REMARK 3 T33: 0.4695 T12: -0.0125
REMARK 3 T13: -0.0993 T23: -0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 8.0132 L22: 1.5668
REMARK 3 L33: 0.5438 L12: 1.6556
REMARK 3 L13: -1.6508 L23: 0.0240
REMARK 3 S TENSOR
REMARK 3 S11: -0.0201 S12: -0.0704 S13: -0.3645
REMARK 3 S21: -0.1237 S22: -0.0517 S23: 0.1413
REMARK 3 S31: 0.0785 S32: -0.0067 S33: 0.0800
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 183 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): 376.0325 230.7078 179.1276
REMARK 3 T TENSOR
REMARK 3 T11: 0.4350 T22: 0.4634
REMARK 3 T33: 0.4308 T12: 0.1313
REMARK 3 T13: -0.0793 T23: -0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 9.3854 L22: 5.4539
REMARK 3 L33: 3.7952 L12: -0.5111
REMARK 3 L13: 0.8781 L23: 5.4505
REMARK 3 S TENSOR
REMARK 3 S11: 0.1274 S12: 0.8134 S13: -0.2170
REMARK 3 S21: -0.4253 S22: 0.0717 S23: 0.1740
REMARK 3 S31: 1.0820 S32: 0.7377 S33: -0.2020
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 224 THROUGH 265 )
REMARK 3 ORIGIN FOR THE GROUP (A): 371.8144 244.0460 201.4840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3029 T22: 0.2764
REMARK 3 T33: 0.5972 T12: 0.0349
REMARK 3 T13: -0.0416 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 9.9843 L22: 6.3155
REMARK 3 L33: 9.0538 L12: -3.3951
REMARK 3 L13: -5.5996 L23: 2.5527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: -0.2856 S13: 0.7777
REMARK 3 S21: 0.5049 S22: -0.0891 S23: 0.4318
REMARK 3 S31: -0.4617 S32: -0.1206 S33: 0.1517
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 266 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 382.7851 234.3321 184.6878
REMARK 3 T TENSOR
REMARK 3 T11: 0.3137 T22: 0.4485
REMARK 3 T33: 0.3567 T12: 0.0091
REMARK 3 T13: -0.0513 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 9.8477 L22: 2.4700
REMARK 3 L33: 8.5333 L12: -1.6883
REMARK 3 L13: 0.8856 L23: 0.3782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0759 S12: 0.2260 S13: -0.1060
REMARK 3 S21: 0.0909 S22: 0.0470 S23: -0.3124
REMARK 3 S31: 0.5037 S32: 1.0328 S33: -0.0203
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 319 THROUGH 355 )
REMARK 3 ORIGIN FOR THE GROUP (A): 364.5619 243.5460 173.5751
REMARK 3 T TENSOR
REMARK 3 T11: 0.4146 T22: 0.4979
REMARK 3 T33: 0.5146 T12: -0.0517
REMARK 3 T13: -0.0817 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 5.2954 L22: 6.8708
REMARK 3 L33: 4.0119 L12: 3.3179
REMARK 3 L13: 3.6335 L23: -2.8752
REMARK 3 S TENSOR
REMARK 3 S11: -0.6247 S12: 0.6466 S13: 0.2737
REMARK 3 S21: -0.2066 S22: 0.3560 S23: -0.0622
REMARK 3 S31: -0.9808 S32: 0.1858 S33: 0.3195
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 359 THROUGH 367)
REMARK 3 ORIGIN FOR THE GROUP (A): 333.0507 234.7527 168.8169
REMARK 3 T TENSOR
REMARK 3 T11: 0.7442 T22: 0.9318
REMARK 3 T33: 0.8740 T12: 0.2087
REMARK 3 T13: 0.0996 T23: -0.1165
REMARK 3 L TENSOR
REMARK 3 L11: 2.1779 L22: 2.2256
REMARK 3 L33: 6.0378 L12: 5.9106
REMARK 3 L13: -1.5372 L23: -4.4426
REMARK 3 S TENSOR
REMARK 3 S11: 0.2296 S12: 1.4041 S13: -1.5097
REMARK 3 S21: -2.0301 S22: -0.6297 S23: -0.4109
REMARK 3 S31: -1.0361 S32: 1.4623 S33: 0.4494
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 358 THROUGH 366)
REMARK 3 ORIGIN FOR THE GROUP (A): 357.8423 223.3802 168.8835
REMARK 3 T TENSOR
REMARK 3 T11: 0.5706 T22: 0.5047
REMARK 3 T33: 0.8239 T12: -0.0510
REMARK 3 T13: -0.1412 T23: -0.2491
REMARK 3 L TENSOR
REMARK 3 L11: 9.5698 L22: 7.1665
REMARK 3 L33: 8.1200 L12: 0.1907
REMARK 3 L13: -2.6455 L23: -6.9100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0208 S12: 1.5952 S13: -1.2480
REMARK 3 S21: -1.0341 S22: 0.1021 S23: -1.3425
REMARK 3 S31: 0.6614 S32: -0.7392 S33: 0.3051
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 5EOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0750
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37322
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 5EOY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, TRIS, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 523 LIES ON A SPECIAL POSITION.
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 GLY A 3
REMARK 465 LEU A 4
REMARK 465 ILE A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLU A 100
REMARK 465 ASP A 101
REMARK 465 GLU A 102
REMARK 465 LEU A 103
REMARK 465 GLU A 104
REMARK 465 ASN A 105
REMARK 465 GLN A 106
REMARK 465 LEU A 107
REMARK 465 LYS A 108
REMARK 465 ILE A 109
REMARK 465 GLU A 110
REMARK 465 ALA A 111
REMARK 465 ASP A 112
REMARK 465 GLN A 113
REMARK 465 TYR A 114
REMARK 465 ILE A 115
REMARK 465 GLN A 129
REMARK 465 GLY A 130
REMARK 465 LEU A 131
REMARK 465 GLY A 187
REMARK 465 GLU A 242
REMARK 465 ALA A 243
REMARK 465 SER A 355
REMARK 465 SER A 356
REMARK 465 GLY A 357
REMARK 465 MET A 358
REMARK 465 GLU A 368
REMARK 465 GLU A 369
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 GLY B 3
REMARK 465 LEU B 4
REMARK 465 ILE B 5
REMARK 465 LYS B 6
REMARK 465 LYS B 7
REMARK 465 LYS B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 133
REMARK 465 GLY B 187
REMARK 465 ALA B 188
REMARK 465 SER B 356
REMARK 465 GLY B 357
REMARK 465 ARG B 367
REMARK 465 GLU B 368
REMARK 465 GLU B 369
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 ASN A 10 CG OD1 ND2
REMARK 470 SER A 30 OG
REMARK 470 ASN A 74 OD1 ND2
REMARK 470 SER A 85 CB OG
REMARK 470 ILE A 88 CD1
REMARK 470 LYS A 90 CD CE NZ
REMARK 470 GLU A 93 CG CD OE1 OE2
REMARK 470 GLU A 95 CB CG CD OE1 OE2
REMARK 470 LEU A 98 CG CD1 CD2
REMARK 470 LEU A 119 CD1 CD2
REMARK 470 GLU A 120 CG CD OE1 OE2
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 PHE A 126 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 127 CG CD OE1 OE2
REMARK 470 ALA A 133 CB
REMARK 470 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 137 CG CD OE1 OE2
REMARK 470 ARG A 138 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 139 CG1 CG2
REMARK 470 VAL A 141 CG1 CG2
REMARK 470 ARG A 147 CD NE CZ NH1 NH2
REMARK 470 LYS A 148 CE NZ
REMARK 470 GLU A 149 CG CD OE1 OE2
REMARK 470 ALA A 188 CB
REMARK 470 ASP A 189 CG OD1 OD2
REMARK 470 ASP A 191 CG OD1 OD2
REMARK 470 GLN A 192 CG CD OE1 NE2
REMARK 470 ASN A 212 CG OD1 ND2
REMARK 470 ARG A 214 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 219 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 220 CD OE1 OE2
REMARK 470 GLN A 221 CD OE1 NE2
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 ILE A 232 CG1 CG2 CD1
REMARK 470 LEU A 238 CG CD1 CD2
REMARK 470 VAL A 240 CG1 CG2
REMARK 470 LEU A 245 CD1 CD2
REMARK 470 ALA A 246 CB
REMARK 470 LYS A 247 CG CD CE NZ
REMARK 470 LYS A 248 CD CE NZ
REMARK 470 GLN A 249 CD OE1 NE2
REMARK 470 LEU A 252 CG CD1 CD2
REMARK 470 GLN A 270 CG CD OE1 NE2
REMARK 470 ARG A 274 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 284 CG CD OE1 NE2
REMARK 470 ASN A 286 CG OD1 ND2
REMARK 470 LYS B 72 NZ
REMARK 470 ASN B 74 OD1 ND2
REMARK 470 LYS B 90 CE NZ
REMARK 470 GLU B 93 CG CD OE1 OE2
REMARK 470 GLU B 95 CD OE1 OE2
REMARK 470 ASP B 101 CG OD1 OD2
REMARK 470 ASN B 105 CG OD1 ND2
REMARK 470 LEU B 107 CG CD1 CD2
REMARK 470 ILE B 109 CG1 CG2 CD1
REMARK 470 ASP B 112 CG OD1 OD2
REMARK 470 GLN B 113 CG CD OE1 NE2
REMARK 470 TYR B 114 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE B 115 CG1 CG2 CD1
REMARK 470 LEU B 119 CG CD1 CD2
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 136 CB CG CD
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 LYS B 148 CE NZ
REMARK 470 GLU B 149 CG CD OE1 OE2
REMARK 470 ASP B 189 CG OD1 OD2
REMARK 470 THR B 190 CB OG1 CG2
REMARK 470 ASP B 191 CG OD1 OD2
REMARK 470 ASN B 212 CG OD1 ND2
REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 219 NE CZ NH1 NH2
REMARK 470 GLU B 220 CG CD OE1 OE2
REMARK 470 GLN B 227 CD OE1 NE2
REMARK 470 GLU B 241 CG CD OE1 OE2
REMARK 470 LYS B 248 CD CE NZ
REMARK 470 GLN B 249 CD OE1 NE2
REMARK 470 GLN B 270 CG CD OE1 NE2
REMARK 470 ASP B 354 CG OD1 OD2
REMARK 470 MET B 358 CG SD CE
REMARK 470 TRP B 366 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 366 CZ3 CH2
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 OG SER A 132 O ASN A 135 1.88
REMARK 500 NZ LYS B 52 O HOH B 501 2.12
REMARK 500 NE2 GLN B 192 O HOH B 502 2.16
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 A 18 -165.10 -105.26
REMARK 500 VAL A 260 -62.22 -127.82
REMARK 500 TYR B 114 -33.58 -130.55
REMARK 500 GLU B 137 -7.80 -54.76
REMARK 500 VAL B 260 -56.22 -127.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 407 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 39 O
REMARK 620 2 HOH A 509 O 113.8
REMARK 620 3 HOH A 510 O 83.2 137.6
REMARK 620 4 HOH A 531 O 66.6 74.8 144.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 408 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SO4 A 404 O1
REMARK 620 2 SO4 A 404 O2 52.9
REMARK 620 3 HOH A 529 O 119.3 74.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 408 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 46 O
REMARK 620 2 HOH B 561 O 120.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 409 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP B 401 O1G
REMARK 620 2 ATP B 401 O1B 69.8
REMARK 620 3 HOH B 501 O 84.8 97.7
REMARK 620 4 HOH B 535 O 150.5 82.2 90.1
REMARK 620 5 HOH B 547 O 86.3 153.4 91.3 122.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EOX RELATED DB: PDB
REMARK 900 RELATED ID: 5EOY RELATED DB: PDB
DBREF 5EOU A 1 354 UNP G3XD28 G3XD28_PSEAE 1 354
DBREF 5EOU A 358 369 UNP G3XD30 G3XD30_PSEAE 1 12
DBREF 5EOU B 1 354 UNP G3XD28 G3XD28_PSEAE 1 354
DBREF 5EOU B 358 369 UNP G3XD30 G3XD30_PSEAE 1 12
SEQADV 5EOU GLY A -2 UNP G3XD28 EXPRESSION TAG
SEQADV 5EOU SER A -1 UNP G3XD28 EXPRESSION TAG
SEQADV 5EOU HIS A 0 UNP G3XD28 EXPRESSION TAG
SEQADV 5EOU SER A 355 UNP G3XD28 LINKER
SEQADV 5EOU SER A 356 UNP G3XD28 LINKER
SEQADV 5EOU GLY A 357 UNP G3XD28 LINKER
SEQADV 5EOU GLY B -2 UNP G3XD28 EXPRESSION TAG
SEQADV 5EOU SER B -1 UNP G3XD28 EXPRESSION TAG
SEQADV 5EOU HIS B 0 UNP G3XD28 EXPRESSION TAG
SEQADV 5EOU SER B 355 UNP G3XD28 LINKER
SEQADV 5EOU SER B 356 UNP G3XD28 LINKER
SEQADV 5EOU GLY B 357 UNP G3XD28 LINKER
SEQRES 1 A 372 GLY SER HIS MET LEU GLY LEU ILE LYS LYS LYS ALA ASN
SEQRES 2 A 372 THR LEU LEU GLY ILE ASP ILE SER SER THR SER VAL LYS
SEQRES 3 A 372 LEU LEU GLU LEU SER ARG SER GLY GLY ARG TYR LYS VAL
SEQRES 4 A 372 GLU ALA TYR ALA VAL GLU PRO LEU PRO PRO ASN ALA VAL
SEQRES 5 A 372 VAL GLU LYS ASN ILE VAL GLU LEU GLU GLY VAL GLY GLN
SEQRES 6 A 372 ALA LEU SER ARG VAL LEU VAL LYS ALA LYS THR ASN LEU
SEQRES 7 A 372 LYS SER ALA VAL VAL ALA VAL ALA GLY SER ALA VAL ILE
SEQRES 8 A 372 THR LYS THR ILE GLU MET GLU ALA GLY LEU SER GLU ASP
SEQRES 9 A 372 GLU LEU GLU ASN GLN LEU LYS ILE GLU ALA ASP GLN TYR
SEQRES 10 A 372 ILE PRO TYR PRO LEU GLU GLU VAL ALA ILE ASP PHE GLU
SEQRES 11 A 372 VAL GLN GLY LEU SER ALA ARG ASN PRO GLU ARG VAL ASP
SEQRES 12 A 372 VAL LEU LEU ALA ALA CYS ARG LYS GLU ASN VAL GLU VAL
SEQRES 13 A 372 ARG GLU ALA ALA LEU ALA LEU ALA GLY LEU THR ALA LYS
SEQRES 14 A 372 VAL VAL ASP VAL GLU ALA TYR ALA LEU GLU ARG SER TYR
SEQRES 15 A 372 ALA LEU LEU SER SER GLN LEU GLY ALA ASP THR ASP GLN
SEQRES 16 A 372 LEU THR VAL ALA VAL VAL ASP ILE GLY ALA THR MET THR
SEQRES 17 A 372 THR LEU SER VAL LEU HIS ASN GLY ARG THR ILE TYR THR
SEQRES 18 A 372 ARG GLU GLN LEU PHE GLY GLY ARG GLN LEU THR GLU GLU
SEQRES 19 A 372 ILE GLN ARG ARG TYR GLY LEU SER VAL GLU GLU ALA GLY
SEQRES 20 A 372 LEU ALA LYS LYS GLN GLY GLY LEU PRO ASP ASP TYR ASP
SEQRES 21 A 372 SER GLU VAL LEU ARG PRO PHE LYS ASP ALA VAL VAL GLN
SEQRES 22 A 372 GLN VAL SER ARG SER LEU GLN PHE PHE PHE ALA ALA GLY
SEQRES 23 A 372 GLN PHE ASN ASP VAL ASP TYR ILE VAL LEU ALA GLY GLY
SEQRES 24 A 372 THR ALA SER ILE GLN ASP LEU ASP ARG LEU ILE GLN GLN
SEQRES 25 A 372 LYS ILE GLY THR PRO THR LEU VAL ALA ASN PRO PHE ALA
SEQRES 26 A 372 ASP MET ALA LEU ASN GLY LYS VAL ASN ALA GLY ALA LEU
SEQRES 27 A 372 ALA SER ASP ALA PRO ALA LEU MET ILE ALA CYS GLY LEU
SEQRES 28 A 372 ALA LEU ARG SER PHE ASP SER SER GLY MET ALA ARG ILE
SEQRES 29 A 372 ASN LEU LEU PRO TRP ARG GLU GLU
SEQRES 1 B 372 GLY SER HIS MET LEU GLY LEU ILE LYS LYS LYS ALA ASN
SEQRES 2 B 372 THR LEU LEU GLY ILE ASP ILE SER SER THR SER VAL LYS
SEQRES 3 B 372 LEU LEU GLU LEU SER ARG SER GLY GLY ARG TYR LYS VAL
SEQRES 4 B 372 GLU ALA TYR ALA VAL GLU PRO LEU PRO PRO ASN ALA VAL
SEQRES 5 B 372 VAL GLU LYS ASN ILE VAL GLU LEU GLU GLY VAL GLY GLN
SEQRES 6 B 372 ALA LEU SER ARG VAL LEU VAL LYS ALA LYS THR ASN LEU
SEQRES 7 B 372 LYS SER ALA VAL VAL ALA VAL ALA GLY SER ALA VAL ILE
SEQRES 8 B 372 THR LYS THR ILE GLU MET GLU ALA GLY LEU SER GLU ASP
SEQRES 9 B 372 GLU LEU GLU ASN GLN LEU LYS ILE GLU ALA ASP GLN TYR
SEQRES 10 B 372 ILE PRO TYR PRO LEU GLU GLU VAL ALA ILE ASP PHE GLU
SEQRES 11 B 372 VAL GLN GLY LEU SER ALA ARG ASN PRO GLU ARG VAL ASP
SEQRES 12 B 372 VAL LEU LEU ALA ALA CYS ARG LYS GLU ASN VAL GLU VAL
SEQRES 13 B 372 ARG GLU ALA ALA LEU ALA LEU ALA GLY LEU THR ALA LYS
SEQRES 14 B 372 VAL VAL ASP VAL GLU ALA TYR ALA LEU GLU ARG SER TYR
SEQRES 15 B 372 ALA LEU LEU SER SER GLN LEU GLY ALA ASP THR ASP GLN
SEQRES 16 B 372 LEU THR VAL ALA VAL VAL ASP ILE GLY ALA THR MET THR
SEQRES 17 B 372 THR LEU SER VAL LEU HIS ASN GLY ARG THR ILE TYR THR
SEQRES 18 B 372 ARG GLU GLN LEU PHE GLY GLY ARG GLN LEU THR GLU GLU
SEQRES 19 B 372 ILE GLN ARG ARG TYR GLY LEU SER VAL GLU GLU ALA GLY
SEQRES 20 B 372 LEU ALA LYS LYS GLN GLY GLY LEU PRO ASP ASP TYR ASP
SEQRES 21 B 372 SER GLU VAL LEU ARG PRO PHE LYS ASP ALA VAL VAL GLN
SEQRES 22 B 372 GLN VAL SER ARG SER LEU GLN PHE PHE PHE ALA ALA GLY
SEQRES 23 B 372 GLN PHE ASN ASP VAL ASP TYR ILE VAL LEU ALA GLY GLY
SEQRES 24 B 372 THR ALA SER ILE GLN ASP LEU ASP ARG LEU ILE GLN GLN
SEQRES 25 B 372 LYS ILE GLY THR PRO THR LEU VAL ALA ASN PRO PHE ALA
SEQRES 26 B 372 ASP MET ALA LEU ASN GLY LYS VAL ASN ALA GLY ALA LEU
SEQRES 27 B 372 ALA SER ASP ALA PRO ALA LEU MET ILE ALA CYS GLY LEU
SEQRES 28 B 372 ALA LEU ARG SER PHE ASP SER SER GLY MET ALA ARG ILE
SEQRES 29 B 372 ASN LEU LEU PRO TRP ARG GLU GLU
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET CL A 406 1
HET NA A 407 1
HET MG A 408 1
HET ATP B 401 31
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET CL B 405 1
HET CL B 406 1
HET CL B 407 1
HET NA B 408 1
HET MG B 409 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 8 CL 4(CL 1-)
FORMUL 9 NA 2(NA 1+)
FORMUL 10 MG 2(MG 2+)
FORMUL 11 ATP C10 H16 N5 O13 P3
FORMUL 20 HOH *101(H2 O)
HELIX 1 AA1 GLU A 56 LYS A 72 1 17
HELIX 2 AA2 PRO A 118 GLU A 120 5 3
HELIX 3 AA3 LYS A 148 ALA A 161 1 14
HELIX 4 AA4 GLU A 171 ALA A 180 1 10
HELIX 5 AA5 LEU A 181 SER A 183 5 3
HELIX 6 AA6 ASP A 189 GLN A 192 5 4
HELIX 7 AA7 GLY A 225 GLY A 237 1 13
HELIX 8 AA8 ASP A 255 VAL A 260 1 6
HELIX 9 AA9 VAL A 260 ALA A 281 1 22
HELIX 10 AB1 GLY A 295 ILE A 300 5 6
HELIX 11 AB2 ASP A 302 GLY A 312 1 11
HELIX 12 AB3 ASN A 331 ALA A 339 1 9
HELIX 13 AB4 LEU A 342 LEU A 350 1 9
HELIX 14 AB5 ARG A 351 PHE A 353 5 3
HELIX 15 AB6 GLU B 56 LYS B 72 1 17
HELIX 16 AB7 SER B 99 ASP B 112 1 14
HELIX 17 AB8 PRO B 118 GLU B 120 5 3
HELIX 18 AB9 LYS B 148 ALA B 161 1 14
HELIX 19 AC1 GLU B 171 ALA B 180 1 10
HELIX 20 AC2 LEU B 181 SER B 183 5 3
HELIX 21 AC3 ASP B 189 GLN B 192 5 4
HELIX 22 AC4 GLY B 225 GLY B 237 1 13
HELIX 23 AC5 SER B 239 GLY B 250 1 12
HELIX 24 AC6 ASP B 255 VAL B 260 1 6
HELIX 25 AC7 VAL B 260 GLY B 283 1 24
HELIX 26 AC8 GLY B 295 ILE B 300 5 6
HELIX 27 AC9 ASP B 302 GLY B 312 1 11
HELIX 28 AD1 ASN B 331 ALA B 339 1 9
HELIX 29 AD2 LEU B 342 LEU B 350 1 9
HELIX 30 AD3 ARG B 351 PHE B 353 5 3
SHEET 1 AA1 6 THR A 164 VAL A 170 0
SHEET 2 AA1 6 SER A 77 VAL A 82 1 N VAL A 80 O ASP A 169
SHEET 3 AA1 6 LEU A 13 ILE A 17 1 N LEU A 13 O VAL A 79
SHEET 4 AA1 6 SER A 21 ARG A 29 -1 O LYS A 23 N ASP A 16
SHEET 5 AA1 6 TYR A 34 PRO A 43 -1 O GLU A 42 N VAL A 22
SHEET 6 AA1 6 ALA A 325 LEU A 326 1 O ALA A 325 N TYR A 34
SHEET 1 AA2 2 VAL A 49 VAL A 50 0
SHEET 2 AA2 2 ASN A 53 ILE A 54 -1 O ASN A 53 N VAL A 50
SHEET 1 AA3 3 ILE A 88 GLU A 95 0
SHEET 2 AA3 3 ARG A 138 ARG A 147 -1 O VAL A 139 N MET A 94
SHEET 3 AA3 3 VAL A 122 GLU A 127 -1 N GLU A 127 O LEU A 142
SHEET 1 AA4 5 ARG A 214 GLN A 221 0
SHEET 2 AA4 5 THR A 205 HIS A 211 -1 N HIS A 211 O ARG A 214
SHEET 3 AA4 5 THR A 194 ILE A 200 -1 N VAL A 197 O SER A 208
SHEET 4 AA4 5 TYR A 290 ALA A 294 1 O VAL A 292 N VAL A 198
SHEET 5 AA4 5 THR A 315 VAL A 317 1 O LEU A 316 N LEU A 293
SHEET 1 AA5 6 THR B 164 VAL B 170 0
SHEET 2 AA5 6 SER B 77 VAL B 82 1 N VAL B 80 O ASP B 169
SHEET 3 AA5 6 LEU B 13 ILE B 17 1 N LEU B 13 O VAL B 79
SHEET 4 AA5 6 SER B 21 SER B 30 -1 O LYS B 23 N ASP B 16
SHEET 5 AA5 6 ARG B 33 PRO B 43 -1 O GLU B 42 N VAL B 22
SHEET 6 AA5 6 ALA B 325 LEU B 326 1 O ALA B 325 N TYR B 34
SHEET 1 AA6 2 VAL B 49 VAL B 50 0
SHEET 2 AA6 2 ASN B 53 ILE B 54 -1 O ASN B 53 N VAL B 50
SHEET 1 AA7 3 ILE B 88 GLU B 95 0
SHEET 2 AA7 3 ARG B 138 ARG B 147 -1 O LEU B 143 N LYS B 90
SHEET 3 AA7 3 VAL B 122 LEU B 131 -1 N ALA B 123 O CYS B 146
SHEET 1 AA8 5 ARG B 214 GLN B 221 0
SHEET 2 AA8 5 THR B 205 HIS B 211 -1 N HIS B 211 O ARG B 214
SHEET 3 AA8 5 THR B 194 ILE B 200 -1 N VAL B 197 O SER B 208
SHEET 4 AA8 5 TYR B 290 ALA B 294 1 O ALA B 294 N ILE B 200
SHEET 5 AA8 5 THR B 315 VAL B 317 1 O LEU B 316 N LEU B 293
LINK O TYR A 39 NA NA A 407 1555 1555 2.93
LINK O1 SO4 A 404 MG MG A 408 1555 1555 2.21
LINK O2 SO4 A 404 MG MG A 408 1555 1555 2.94
LINK NA NA A 407 O HOH A 509 1555 1555 3.11
LINK NA NA A 407 O HOH A 510 1555 1555 2.51
LINK NA NA A 407 O HOH A 531 1555 1555 3.20
LINK MG MG A 408 O HOH A 529 1555 1555 2.35
LINK O PRO B 46 NA NA B 408 1555 1555 3.16
LINK O1G ATP B 401 MG MG B 409 1555 1555 2.60
LINK O1B ATP B 401 MG MG B 409 1555 1555 1.82
LINK NA NA B 408 O HOH B 561 1555 1555 3.13
LINK MG MG B 409 O HOH B 501 1555 1555 2.18
LINK MG MG B 409 O HOH B 535 1555 1555 2.51
LINK MG MG B 409 O HOH B 547 1555 1555 2.25
SITE 1 AC1 8 SER A 18 SER A 19 LYS A 52 GLY A 201
SITE 2 AC1 8 ALA A 202 THR A 203 MET A 204 SO4 A 404
SITE 1 AC2 3 LYS A 35 ASN A 327 GLY A 328
SITE 1 AC3 5 SER A 21 LYS A 23 GLY A 296 SO4 A 401
SITE 2 AC3 5 MG A 408
SITE 1 AC4 2 LYS A 148 ARG A 367
SITE 1 AC5 2 ALA A 123 LEU A 363
SITE 1 AC6 2 TYR A 39 HOH A 510
SITE 1 AC7 2 SO4 A 404 HOH A 529
SITE 1 AC8 20 SER B 18 SER B 19 THR B 20 LYS B 23
SITE 2 AC8 20 GLY B 201 ALA B 202 THR B 203 MET B 204
SITE 3 AC8 20 LYS B 247 LYS B 248 GLY B 295 GLY B 296
SITE 4 AC8 20 THR B 297 SER B 299 CL B 406 MG B 409
SITE 5 AC8 20 HOH B 501 HOH B 503 HOH B 535 HOH B 541
SITE 1 AC9 1 GLY B 251
SITE 1 AD1 2 ASN B 327 LYS B 329
SITE 1 AD2 3 LYS B 35 ASN B 327 GLY B 328
SITE 1 AD3 4 ASN B 53 ILE B 54 ASN B 150 ARG B 154
SITE 1 AD4 2 THR B 229 ATP B 401
SITE 1 AD5 3 PRO B 46 ALA B 48 GLU B 56
SITE 1 AD6 5 LYS B 52 ATP B 401 HOH B 501 HOH B 535
SITE 2 AD6 5 HOH B 547
CRYST1 131.790 131.790 78.993 90.00 90.00 120.00 P 3 2 1 12
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 0.007588 0.004381 0.000000 0.00000
SCALE2 0.000000 0.008762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012659 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
