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HEADER HYDROLASE 06-OCT-22 8B9S
TITLE NATIVE FORM, THERMOSTABLE LIPASE FROM THERMOANAEROBACTER
TITLE 2 THERMOHYDROSULFURICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTER THERMOHYDROSULFURICUS;
SOURCE 3 ORGANISM_TAXID: 1516;
SOURCE 4 GENE: THESIDRAFT1_1468;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE, THERMOSTABLE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.PINOTSIS,M.WILMANNS
REVDAT 1 18-OCT-23 8B9S 0
JRNL AUTH N.PINOTSIS,M.WILMANNS
JRNL TITL NATIVE FORM, THERMOSTABLE LIPASE FROM THERMOANAEROBACTER
JRNL TITL 2 THERMOHYDROSULFURICUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 67669
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2051
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 19.9400 - 5.9200 1.00 4356 164 0.2048 0.2229
REMARK 3 2 5.9200 - 4.7200 1.00 4362 152 0.1920 0.2072
REMARK 3 3 4.7200 - 4.1300 1.00 4358 140 0.1865 0.2001
REMARK 3 4 4.1300 - 3.7500 1.00 4386 128 0.2006 0.2624
REMARK 3 5 3.7500 - 3.4900 1.00 4388 136 0.2079 0.2607
REMARK 3 6 3.4900 - 3.2800 1.00 4361 138 0.2235 0.2579
REMARK 3 7 3.2800 - 3.1200 1.00 4401 133 0.2336 0.2905
REMARK 3 8 3.1200 - 2.9800 1.00 4356 134 0.2435 0.3246
REMARK 3 9 2.9800 - 2.8700 1.00 4438 112 0.2543 0.3042
REMARK 3 10 2.8700 - 2.7700 1.00 4347 149 0.2594 0.3176
REMARK 3 11 2.7700 - 2.6800 1.00 4370 145 0.2523 0.3086
REMARK 3 12 2.6800 - 2.6100 1.00 4357 125 0.2527 0.3978
REMARK 3 13 2.6100 - 2.5400 1.00 4401 157 0.2555 0.2830
REMARK 3 14 2.5400 - 2.4800 1.00 4366 110 0.2590 0.2914
REMARK 3 15 2.4800 - 2.4200 0.99 4371 128 0.2749 0.3147
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.369
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 46.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.07
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 : 0.007 12538
REMARK 3 ANGLE : 1.026 16823
REMARK 3 CHIRALITY : 0.060 1831
REMARK 3 PLANARITY : 0.009 2150
REMARK 3 DIHEDRAL : 5.251 1657
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND ((RESID 1:140) OR (RESID 183:259)))
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6392 100.6051 31.1324
REMARK 3 T TENSOR
REMARK 3 T11: 0.3466 T22: 0.2452
REMARK 3 T33: 0.3559 T12: 0.0442
REMARK 3 T13: 0.1009 T23: 0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 2.7711 L22: 2.3005
REMARK 3 L33: 2.0812 L12: 0.1024
REMARK 3 L13: -0.0603 L23: 0.2560
REMARK 3 S TENSOR
REMARK 3 S11: 0.0555 S12: 0.0850 S13: 0.2193
REMARK 3 S21: 0.2592 S22: 0.1720 S23: 0.4765
REMARK 3 S31: -0.3228 S32: -0.2511 S33: -0.2146
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND ((RESID 1:140) OR (RESID 183:259)))
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7952 79.3222 25.1369
REMARK 3 T TENSOR
REMARK 3 T11: 0.2113 T22: 0.3225
REMARK 3 T33: 0.3196 T12: 0.0196
REMARK 3 T13: -0.0056 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 1.2986 L22: 2.6885
REMARK 3 L33: 1.9861 L12: 0.2723
REMARK 3 L13: -0.4476 L23: -0.4873
REMARK 3 S TENSOR
REMARK 3 S11: 0.0765 S12: 0.1549 S13: -0.2693
REMARK 3 S21: -0.0668 S22: 0.0014 S23: -0.3733
REMARK 3 S31: 0.0587 S32: 0.2697 S33: -0.0640
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN 'C' AND ((RESID 1:140) OR (RESID 183:259)))
REMARK 3 ORIGIN FOR THE GROUP (A): -57.9777 136.6097 25.2335
REMARK 3 T TENSOR
REMARK 3 T11: 0.3937 T22: 0.4496
REMARK 3 T33: 0.3753 T12: -0.0839
REMARK 3 T13: -0.0460 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 2.0259 L22: 3.8439
REMARK 3 L33: 3.2935 L12: -0.6715
REMARK 3 L13: 0.5131 L23: 1.2951
REMARK 3 S TENSOR
REMARK 3 S11: -0.0412 S12: 0.2508 S13: 0.2676
REMARK 3 S21: -0.4813 S22: -0.1730 S23: -0.2751
REMARK 3 S31: -0.4683 S32: 0.0259 S33: 0.2126
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN 'D' AND ((RESID 1:140) OR (RESID 183:259)))
REMARK 3 ORIGIN FOR THE GROUP (A): -39.1381 111.0364 19.4275
REMARK 3 T TENSOR
REMARK 3 T11: 0.4548 T22: 0.8559
REMARK 3 T33: 0.7714 T12: 0.0763
REMARK 3 T13: 0.0692 T23: -0.1459
REMARK 3 L TENSOR
REMARK 3 L11: 2.6768 L22: 2.9056
REMARK 3 L33: 2.0743 L12: -0.9320
REMARK 3 L13: 0.1847 L23: 1.0183
REMARK 3 S TENSOR
REMARK 3 S11: 0.0841 S12: 0.8371 S13: -0.2609
REMARK 3 S21: -0.1324 S22: 0.1796 S23: -0.9215
REMARK 3 S31: 0.3001 S32: 0.7906 S33: -0.2469
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN 'E' AND ((RESID 1:140) OR (RESID 183:259)))
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8988 128.5583 63.7180
REMARK 3 T TENSOR
REMARK 3 T11: 0.4752 T22: 0.5903
REMARK 3 T33: 0.4599 T12: -0.1234
REMARK 3 T13: 0.1016 T23: -0.1775
REMARK 3 L TENSOR
REMARK 3 L11: 2.0811 L22: 2.4320
REMARK 3 L33: 1.9604 L12: 0.4092
REMARK 3 L13: 0.5578 L23: -0.6245
REMARK 3 S TENSOR
REMARK 3 S11: -0.0921 S12: -0.1419 S13: -0.1546
REMARK 3 S21: -0.2328 S22: -0.0815 S23: 0.1086
REMARK 3 S31: 0.4540 S32: -0.6476 S33: 0.1714
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN 'F' AND ((RESID 1:140) OR (RESID 183:259)))
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6501 121.2967 71.2082
REMARK 3 T TENSOR
REMARK 3 T11: 0.6867 T22: 0.5031
REMARK 3 T33: 0.5832 T12: 0.1696
REMARK 3 T13: 0.0272 T23: 0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 2.2393 L22: 1.2823
REMARK 3 L33: 1.8525 L12: 0.5652
REMARK 3 L13: 0.6446 L23: -0.4462
REMARK 3 S TENSOR
REMARK 3 S11: 0.0313 S12: -0.1141 S13: -0.3004
REMARK 3 S21: 0.2819 S22: -0.1466 S23: -0.4556
REMARK 3 S31: 0.4025 S32: 0.2221 S33: 0.1219
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN 'A' AND (RESID 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6796 89.6886 52.0041
REMARK 3 T TENSOR
REMARK 3 T11: 0.6758 T22: 0.4083
REMARK 3 T33: 0.3390 T12: 0.0019
REMARK 3 T13: 0.1119 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 2.9132 L22: 4.2860
REMARK 3 L33: 1.0402 L12: 0.7559
REMARK 3 L13: -0.4001 L23: -0.6729
REMARK 3 S TENSOR
REMARK 3 S11: 0.2989 S12: -0.5353 S13: 0.1729
REMARK 3 S21: 0.5664 S22: -0.2242 S23: 0.0035
REMARK 3 S31: -0.6077 S32: -0.0705 S33: -0.0824
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN 'B' AND (RESID 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7514 70.8939 16.7734
REMARK 3 T TENSOR
REMARK 3 T11: 0.5180 T22: 0.4622
REMARK 3 T33: 0.4455 T12: -0.0889
REMARK 3 T13: -0.0574 T23: -0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 5.5244 L22: 0.7998
REMARK 3 L33: 0.1689 L12: -0.6978
REMARK 3 L13: 0.9690 L23: -0.1251
REMARK 3 S TENSOR
REMARK 3 S11: 0.3071 S12: 0.2615 S13: -0.9740
REMARK 3 S21: -0.1535 S22: 0.0061 S23: -0.1581
REMARK 3 S31: 0.4106 S32: -0.1999 S33: -0.3782
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN 'C' AND (RESID 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): -54.0390 124.7621 46.1057
REMARK 3 T TENSOR
REMARK 3 T11: 0.6600 T22: 0.4688
REMARK 3 T33: 0.4370 T12: 0.0196
REMARK 3 T13: -0.1387 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 2.7358 L22: 4.7068
REMARK 3 L33: 0.6425 L12: -0.6221
REMARK 3 L13: 0.2680 L23: 0.1763
REMARK 3 S TENSOR
REMARK 3 S11: -0.2243 S12: -0.5910 S13: 0.2196
REMARK 3 S21: 0.7967 S22: 0.0335 S23: -0.6490
REMARK 3 S31: 0.3424 S32: -0.2574 S33: 0.1524
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN 'D' AND (RESID 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): -61.3556 106.8503 10.8893
REMARK 3 T TENSOR
REMARK 3 T11: 0.5423 T22: 0.7663
REMARK 3 T33: 0.5075 T12: 0.0702
REMARK 3 T13: 0.0029 T23: -0.1153
REMARK 3 L TENSOR
REMARK 3 L11: 3.4431 L22: 1.9986
REMARK 3 L33: 1.5498 L12: -0.1437
REMARK 3 L13: 2.0940 L23: -0.8246
REMARK 3 S TENSOR
REMARK 3 S11: 0.2269 S12: 0.4415 S13: -0.4927
REMARK 3 S21: -0.0788 S22: -0.2874 S23: 0.1168
REMARK 3 S31: 0.1380 S32: 0.2964 S33: -0.0104
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN 'E' AND (RESID 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2845 129.6778 43.4287
REMARK 3 T TENSOR
REMARK 3 T11: 0.4974 T22: 0.4329
REMARK 3 T33: 0.4934 T12: -0.0367
REMARK 3 T13: 0.1119 T23: -0.1631
REMARK 3 L TENSOR
REMARK 3 L11: 6.8848 L22: 1.7068
REMARK 3 L33: 2.0835 L12: 1.6568
REMARK 3 L13: 0.3586 L23: -0.6408
REMARK 3 S TENSOR
REMARK 3 S11: -0.4218 S12: 0.2011 S13: -0.4778
REMARK 3 S21: -0.1867 S22: -0.1289 S23: 0.5028
REMARK 3 S31: 0.4495 S32: -0.5002 S33: 0.6039
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN 'F' AND (RESID 141:182))
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0196 143.6340 79.3224
REMARK 3 T TENSOR
REMARK 3 T11: 0.6077 T22: 0.4817
REMARK 3 T33: 0.4181 T12: 0.0969
REMARK 3 T13: -0.0729 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 6.5203 L22: 3.5643
REMARK 3 L33: 1.5007 L12: -2.9977
REMARK 3 L13: 1.6105 L23: 0.2259
REMARK 3 S TENSOR
REMARK 3 S11: -0.5805 S12: -0.4728 S13: 0.4104
REMARK 3 S21: 0.5123 S22: 0.3327 S23: -0.6276
REMARK 3 S31: 0.4098 S32: 0.5288 S33: 0.1973
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 1 through 2 or
REMARK 3 (resid 3 through 4 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 5 through 24 or (resid 25 and (name
REMARK 3 N or name CA or name C or name O or name
REMARK 3 CB )) or resid 26 through 55 or resid 57
REMARK 3 through 75 or resid 77 through 112 or
REMARK 3 resid 114 through 158 or resid 160
REMARK 3 through 259))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 1 through 2 or
REMARK 3 (resid 3 through 4 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 5 through 55 or resid 57 through 75
REMARK 3 or resid 77 through 112 or resid 114
REMARK 3 through 158 or resid 160 through 208 or
REMARK 3 (resid 209 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG or name
REMARK 3 CD )) or resid 210 through 259))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and (resid 1 through 2 or
REMARK 3 (resid 3 through 4 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 5 through 55 or resid 57 through 75
REMARK 3 or resid 77 through 112 or resid 114
REMARK 3 through 158 or resid 160 through 208 or
REMARK 3 (resid 209 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG or name
REMARK 3 CD )) or resid 210 through 259))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "D" and (resid 1 through 2 or
REMARK 3 (resid 3 through 4 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 5 through 55 or resid 57 through 75
REMARK 3 or resid 77 through 112 or resid 114
REMARK 3 through 158 or resid 160 through 208 or
REMARK 3 (resid 209 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG or name
REMARK 3 CD )) or resid 210 through 259))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "E" and (resid 1 through 55 or
REMARK 3 resid 57 through 75 or resid 77 through
REMARK 3 112 or resid 114 through 158 or resid 160
REMARK 3 through 208 or (resid 209 and (name N or
REMARK 3 name CA or name C or name O or name CB or
REMARK 3 name CG or name CD )) or resid 210
REMARK 3 through 259))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "F" and (resid 1 through 2 or
REMARK 3 (resid 3 through 4 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 5 through 55 or resid 57 through 75
REMARK 3 or resid 77 through 112 or resid 114
REMARK 3 through 158 or resid 160 through 208 or
REMARK 3 (resid 209 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG or name
REMARK 3 CD )) or resid 210 through 259))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8B9S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1292125995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67696
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.61900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.710
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: 7Q4H
REMARK 200
REMARK 200 REMARK: RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 6000 0.1 M TRIS-HCL, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 67.61267
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 33.80633
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 LYS A 209 CE NZ
REMARK 470 LYS A 258 CG CD CE NZ
REMARK 470 LYS B 25 CG CD CE NZ
REMARK 470 LYS B 258 CG CD CE NZ
REMARK 470 LYS C 25 CG CD CE NZ
REMARK 470 LYS C 258 CG CD CE NZ
REMARK 470 LYS D 25 CG CD CE NZ
REMARK 470 GLU D 56 CG CD OE1 OE2
REMARK 470 LYS D 258 CG CD CE NZ
REMARK 470 LYS E 3 CG CD CE NZ
REMARK 470 LYS E 25 CG CD CE NZ
REMARK 470 LYS E 258 CG CD CE NZ
REMARK 470 LYS F 25 CG CD CE NZ
REMARK 470 LYS F 258 CG CD CE NZ
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 PRO F 104 O HOH F 401 2.19
REMARK 500 O HOH A 455 O HOH A 462 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PHE F 163 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 PHE F 175 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
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 GLU A 43 177.24 60.84
REMARK 500 SER A 113 -116.87 58.34
REMARK 500 ALA A 137 56.11 38.20
REMARK 500 ASN A 230 -4.38 76.15
REMARK 500 GLU B 43 178.19 59.60
REMARK 500 HIS B 45 41.02 39.20
REMARK 500 SER B 113 -124.26 59.99
REMARK 500 ASN B 230 -4.97 75.14
REMARK 500 GLU C 43 176.32 62.39
REMARK 500 HIS C 45 42.81 39.78
REMARK 500 SER C 113 -118.51 54.18
REMARK 500 ASN C 202 31.19 -96.62
REMARK 500 ASN C 230 -4.93 79.05
REMARK 500 LEU C 257 42.67 -73.71
REMARK 500 ASP D 23 24.13 -74.93
REMARK 500 GLU D 43 177.81 62.41
REMARK 500 SER D 113 -123.07 56.53
REMARK 500 GLN D 153 -51.28 -121.64
REMARK 500 ASN D 202 30.11 -96.15
REMARK 500 ASN D 230 -4.74 74.20
REMARK 500 LYS D 258 48.37 -141.68
REMARK 500 GLU E 43 179.53 73.40
REMARK 500 SER E 113 -121.55 59.48
REMARK 500 ASN E 202 30.22 -96.02
REMARK 500 ASN E 230 -5.29 76.92
REMARK 500 GLU F 43 -178.90 65.01
REMARK 500 HIS F 45 42.74 38.80
REMARK 500 SER F 113 -120.81 57.01
REMARK 500 ALA F 137 55.87 39.55
REMARK 500 ASN F 202 30.49 -97.59
REMARK 500 ASN F 230 -3.55 71.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 64 0.08 SIDE CHAIN
REMARK 500 ARG E 64 0.08 SIDE CHAIN
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 D 419 DISTANCE = 7.20 ANGSTROMS
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 K F 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY F 69 O
REMARK 620 2 SER F 73 O 137.2
REMARK 620 3 GLY F 75 O 92.1 105.3
REMARK 620 4 HOH F 425 O 51.3 171.5 71.8
REMARK 620 5 HOH F 430 O 95.7 101.1 131.0 76.1
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7Q4H RELATED DB: PDB
REMARK 900 METHYLATED PROTEIN
REMARK 900 RELATED ID: 7Q4J RELATED DB: PDB
REMARK 900 METHYLATED PROTEIN
DBREF 8B9S A 1 259 UNP I9KU82 I9KU82_9THEO 1 259
DBREF 8B9S B 1 259 UNP I9KU82 I9KU82_9THEO 1 259
DBREF 8B9S C 1 259 UNP I9KU82 I9KU82_9THEO 1 259
DBREF 8B9S D 1 259 UNP I9KU82 I9KU82_9THEO 1 259
DBREF 8B9S E 1 259 UNP I9KU82 I9KU82_9THEO 1 259
DBREF 8B9S F 1 259 UNP I9KU82 I9KU82_9THEO 1 259
SEQRES 1 A 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 A 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 A 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 A 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 A 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 A 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 A 259 GLU MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 A 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 A 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MET GLY GLY ALA
SEQRES 10 A 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 A 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 A 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 A 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 A 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 A 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 A 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 A 259 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 A 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 A 259 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 A 259 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY
SEQRES 1 B 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 B 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 B 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 B 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 B 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 B 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 B 259 GLU MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 B 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 B 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MET GLY GLY ALA
SEQRES 10 B 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 B 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 B 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 B 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 B 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 B 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 B 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 B 259 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 B 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 B 259 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 B 259 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY
SEQRES 1 C 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 C 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 C 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 C 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 C 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 C 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 C 259 GLU MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 C 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 C 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MET GLY GLY ALA
SEQRES 10 C 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 C 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 C 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 C 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 C 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 C 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 C 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 C 259 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 C 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 C 259 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 C 259 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY
SEQRES 1 D 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 D 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 D 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 D 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 D 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 D 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 D 259 GLU MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 D 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 D 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MET GLY GLY ALA
SEQRES 10 D 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 D 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 D 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 D 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 D 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 D 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 D 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 D 259 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 D 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 D 259 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 D 259 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY
SEQRES 1 E 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 E 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 E 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 E 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 E 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 E 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 E 259 GLU MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 E 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 E 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MET GLY GLY ALA
SEQRES 10 E 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 E 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 E 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 E 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 E 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 E 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 E 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 E 259 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 E 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 E 259 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 E 259 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY
SEQRES 1 F 259 MET GLN LYS ALA VAL GLU ILE THR TYR ASN GLY LYS THR
SEQRES 2 F 259 LEU ARG GLY MET MET HIS LEU PRO ASP ASP VAL LYS GLY
SEQRES 3 F 259 LYS VAL PRO MET VAL ILE MET PHE HIS GLY PHE THR GLY
SEQRES 4 F 259 ASN LYS VAL GLU SER HIS PHE ILE PHE VAL LYS MET SER
SEQRES 5 F 259 ARG ALA LEU GLU LYS VAL GLY ILE GLY SER VAL ARG PHE
SEQRES 6 F 259 ASP PHE TYR GLY SER GLY GLU SER ASP GLY ASP PHE SER
SEQRES 7 F 259 GLU MET THR PHE SER SER GLU LEU GLU ASP ALA ARG GLN
SEQRES 8 F 259 ILE LEU LYS PHE VAL LYS GLU GLN PRO THR THR ASP PRO
SEQRES 9 F 259 GLU ARG ILE GLY LEU LEU GLY LEU SER MET GLY GLY ALA
SEQRES 10 F 259 ILE ALA GLY ILE VAL ALA ARG GLU TYR LYS ASP GLU ILE
SEQRES 11 F 259 LYS ALA LEU VAL LEU TRP ALA PRO ALA PHE ASN MET PRO
SEQRES 12 F 259 GLU LEU ILE MET ASN GLU SER VAL LYS GLN TYR GLY ALA
SEQRES 13 F 259 ILE MET GLU GLN LEU GLY PHE VAL ASP ILE GLY GLY HIS
SEQRES 14 F 259 LYS LEU SER LYS ASP PHE VAL GLU ASP ILE SER LYS LEU
SEQRES 15 F 259 ASN ILE PHE GLU LEU SER LYS GLY TYR ASP LYS LYS VAL
SEQRES 16 F 259 LEU ILE VAL HIS GLY THR ASN ASP GLU ALA VAL GLU TYR
SEQRES 17 F 259 LYS VAL SER ASP ARG ILE LEU LYS GLU VAL TYR GLY ASP
SEQRES 18 F 259 ASN ALA THR ARG VAL THR ILE GLU ASN ALA ASP HIS THR
SEQRES 19 F 259 PHE LYS SER LEU GLU TRP GLU LYS LYS ALA ILE GLU GLU
SEQRES 20 F 259 SER VAL GLU PHE PHE LYS LYS GLU LEU LEU LYS GLY
HET GOL A 301 6
HET D10 A 302 10
HET GOL B 301 6
HET PO4 B 302 5
HET PO4 B 303 5
HET GOL C 301 6
HET PO4 D 301 5
HET GOL E 301 6
HET PO4 E 302 5
HET PO4 E 303 5
HET GOL F 301 6
HET K F 302 1
HETNAM GOL GLYCEROL
HETNAM D10 DECANE
HETNAM PO4 PHOSPHATE ION
HETNAM K POTASSIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 5(C3 H8 O3)
FORMUL 8 D10 C10 H22
FORMUL 10 PO4 5(O4 P 3-)
FORMUL 18 K K 1+
FORMUL 19 HOH *340(H2 O)
HELIX 1 AA1 GLU A 43 HIS A 45 5 3
HELIX 2 AA2 PHE A 46 LYS A 57 1 12
HELIX 3 AA3 ASP A 76 MET A 80 5 5
HELIX 4 AA4 THR A 81 GLN A 99 1 19
HELIX 5 AA5 SER A 113 TYR A 126 1 14
HELIX 6 AA6 ASN A 141 GLU A 149 1 9
HELIX 7 AA7 LYS A 152 GLY A 162 1 11
HELIX 8 AA8 LYS A 173 SER A 180 1 8
HELIX 9 AA9 ASN A 183 LYS A 189 1 7
HELIX 10 AB1 GLU A 207 VAL A 218 1 12
HELIX 11 AB2 SER A 237 LEU A 257 1 21
HELIX 12 AB3 GLU B 43 HIS B 45 5 3
HELIX 13 AB4 PHE B 46 LYS B 57 1 12
HELIX 14 AB5 ASP B 76 MET B 80 5 5
HELIX 15 AB6 THR B 81 GLN B 99 1 19
HELIX 16 AB7 SER B 113 TYR B 126 1 14
HELIX 17 AB8 ASN B 141 GLN B 153 1 13
HELIX 18 AB9 GLY B 155 GLY B 162 1 8
HELIX 19 AC1 LYS B 173 LYS B 181 1 9
HELIX 20 AC2 ASN B 183 LYS B 189 1 7
HELIX 21 AC3 GLU B 207 VAL B 218 1 12
HELIX 22 AC4 SER B 237 LEU B 257 1 21
HELIX 23 AC5 GLU C 43 HIS C 45 5 3
HELIX 24 AC6 PHE C 46 VAL C 58 1 13
HELIX 25 AC7 ASP C 76 MET C 80 5 5
HELIX 26 AC8 THR C 81 GLN C 99 1 19
HELIX 27 AC9 SER C 113 TYR C 126 1 14
HELIX 28 AD1 ASN C 141 GLU C 149 1 9
HELIX 29 AD2 LYS C 152 GLY C 162 1 11
HELIX 30 AD3 LYS C 173 LYS C 181 1 9
HELIX 31 AD4 ASN C 183 LYS C 189 1 7
HELIX 32 AD5 GLU C 207 VAL C 218 1 12
HELIX 33 AD6 SER C 237 LEU C 256 1 20
HELIX 34 AD7 GLU D 43 HIS D 45 5 3
HELIX 35 AD8 PHE D 46 VAL D 58 1 13
HELIX 36 AD9 ASP D 76 MET D 80 5 5
HELIX 37 AE1 THR D 81 GLN D 99 1 19
HELIX 38 AE2 MET D 114 TYR D 126 1 13
HELIX 39 AE3 ASN D 141 GLN D 153 1 13
HELIX 40 AE4 GLY D 155 GLY D 162 1 8
HELIX 41 AE5 LYS D 173 LYS D 181 1 9
HELIX 42 AE6 ASN D 183 LYS D 189 1 7
HELIX 43 AE7 GLU D 207 VAL D 218 1 12
HELIX 44 AE8 SER D 237 LEU D 257 1 21
HELIX 45 AE9 GLU E 43 HIS E 45 5 3
HELIX 46 AF1 PHE E 46 VAL E 58 1 13
HELIX 47 AF2 ASP E 76 MET E 80 5 5
HELIX 48 AF3 THR E 81 GLN E 99 1 19
HELIX 49 AF4 SER E 113 TYR E 126 1 14
HELIX 50 AF5 ASN E 141 GLU E 149 1 9
HELIX 51 AF6 LYS E 152 GLY E 162 1 11
HELIX 52 AF7 LYS E 173 LYS E 181 1 9
HELIX 53 AF8 ASN E 183 LYS E 189 1 7
HELIX 54 AF9 GLU E 207 VAL E 218 1 12
HELIX 55 AG1 SER E 237 LEU E 256 1 20
HELIX 56 AG2 GLU F 43 HIS F 45 5 3
HELIX 57 AG3 PHE F 46 LYS F 57 1 12
HELIX 58 AG4 ASP F 76 MET F 80 5 5
HELIX 59 AG5 THR F 81 GLN F 99 1 19
HELIX 60 AG6 MET F 114 TYR F 126 1 13
HELIX 61 AG7 ASN F 141 GLN F 153 1 13
HELIX 62 AG8 ALA F 156 LEU F 161 1 6
HELIX 63 AG9 LYS F 173 LYS F 181 1 9
HELIX 64 AH1 ASN F 183 LYS F 189 1 7
HELIX 65 AH2 GLU F 207 VAL F 218 1 12
HELIX 66 AH3 SER F 237 LEU F 256 1 20
SHEET 1 AA1 8 GLN A 2 TYR A 9 0
SHEET 2 AA1 8 LYS A 12 HIS A 19 -1 O GLY A 16 N VAL A 5
SHEET 3 AA1 8 GLY A 61 PHE A 65 -1 O SER A 62 N HIS A 19
SHEET 4 AA1 8 VAL A 28 PHE A 34 1 N PRO A 29 O GLY A 61
SHEET 5 AA1 8 THR A 102 LEU A 112 1 O GLY A 108 N MET A 30
SHEET 6 AA1 8 ALA A 132 TRP A 136 1 O TRP A 136 N GLY A 111
SHEET 7 AA1 8 VAL A 195 GLY A 200 1 O LEU A 196 N LEU A 135
SHEET 8 AA1 8 ALA A 223 ILE A 228 1 O ILE A 228 N HIS A 199
SHEET 1 AA2 2 PHE A 163 ASP A 165 0
SHEET 2 AA2 2 LYS A 170 SER A 172 -1 O LEU A 171 N VAL A 164
SHEET 1 AA3 8 GLN B 2 TYR B 9 0
SHEET 2 AA3 8 LYS B 12 HIS B 19 -1 O GLY B 16 N VAL B 5
SHEET 3 AA3 8 GLY B 61 PHE B 65 -1 O SER B 62 N HIS B 19
SHEET 4 AA3 8 VAL B 28 PHE B 34 1 N PRO B 29 O GLY B 61
SHEET 5 AA3 8 THR B 102 LEU B 112 1 O GLY B 108 N ILE B 32
SHEET 6 AA3 8 ALA B 132 TRP B 136 1 O VAL B 134 N LEU B 109
SHEET 7 AA3 8 VAL B 195 GLY B 200 1 O LEU B 196 N LEU B 135
SHEET 8 AA3 8 ALA B 223 ILE B 228 1 O VAL B 226 N ILE B 197
SHEET 1 AA4 2 PHE B 163 ASP B 165 0
SHEET 2 AA4 2 LYS B 170 SER B 172 -1 O LEU B 171 N VAL B 164
SHEET 1 AA5 8 GLN C 2 TYR C 9 0
SHEET 2 AA5 8 LYS C 12 HIS C 19 -1 O GLY C 16 N VAL C 5
SHEET 3 AA5 8 GLY C 61 PHE C 65 -1 O SER C 62 N HIS C 19
SHEET 4 AA5 8 VAL C 28 PHE C 34 1 N PRO C 29 O GLY C 61
SHEET 5 AA5 8 THR C 102 LEU C 112 1 O LEU C 110 N ILE C 32
SHEET 6 AA5 8 ALA C 132 TRP C 136 1 O TRP C 136 N GLY C 111
SHEET 7 AA5 8 LYS C 194 GLY C 200 1 O LEU C 196 N LEU C 135
SHEET 8 AA5 8 ALA C 223 ILE C 228 1 O VAL C 226 N ILE C 197
SHEET 1 AA6 2 PHE C 163 ASP C 165 0
SHEET 2 AA6 2 LYS C 170 SER C 172 -1 O LEU C 171 N VAL C 164
SHEET 1 AA7 8 GLN D 2 TYR D 9 0
SHEET 2 AA7 8 LYS D 12 HIS D 19 -1 O MET D 18 N LYS D 3
SHEET 3 AA7 8 GLY D 61 PHE D 65 -1 O SER D 62 N HIS D 19
SHEET 4 AA7 8 VAL D 28 PHE D 34 1 N PRO D 29 O GLY D 61
SHEET 5 AA7 8 THR D 102 LEU D 112 1 O LEU D 110 N ILE D 32
SHEET 6 AA7 8 ALA D 132 TRP D 136 1 O VAL D 134 N LEU D 109
SHEET 7 AA7 8 VAL D 195 GLY D 200 1 O VAL D 198 N LEU D 135
SHEET 8 AA7 8 ALA D 223 ILE D 228 1 O VAL D 226 N ILE D 197
SHEET 1 AA8 2 PHE D 163 ASP D 165 0
SHEET 2 AA8 2 LYS D 170 SER D 172 -1 O LEU D 171 N VAL D 164
SHEET 1 AA9 8 GLN E 2 TYR E 9 0
SHEET 2 AA9 8 LYS E 12 HIS E 19 -1 O MET E 18 N LYS E 3
SHEET 3 AA9 8 GLY E 61 PHE E 65 -1 O SER E 62 N HIS E 19
SHEET 4 AA9 8 VAL E 28 PHE E 34 1 N PRO E 29 O GLY E 61
SHEET 5 AA9 8 THR E 102 LEU E 112 1 O GLY E 108 N MET E 30
SHEET 6 AA9 8 ALA E 132 TRP E 136 1 O TRP E 136 N GLY E 111
SHEET 7 AA9 8 VAL E 195 GLY E 200 1 O LEU E 196 N LEU E 135
SHEET 8 AA9 8 ALA E 223 ILE E 228 1 O THR E 224 N ILE E 197
SHEET 1 AB1 2 PHE E 163 ASP E 165 0
SHEET 2 AB1 2 LYS E 170 SER E 172 -1 O LEU E 171 N VAL E 164
SHEET 1 AB2 8 GLN F 2 TYR F 9 0
SHEET 2 AB2 8 LYS F 12 HIS F 19 -1 O GLY F 16 N VAL F 5
SHEET 3 AB2 8 GLY F 61 PHE F 65 -1 O SER F 62 N HIS F 19
SHEET 4 AB2 8 VAL F 28 PHE F 34 1 N PRO F 29 O GLY F 61
SHEET 5 AB2 8 THR F 102 LEU F 112 1 O ASP F 103 N VAL F 28
SHEET 6 AB2 8 ALA F 132 TRP F 136 1 O TRP F 136 N GLY F 111
SHEET 7 AB2 8 VAL F 195 GLY F 200 1 O LEU F 196 N LEU F 135
SHEET 8 AB2 8 ALA F 223 ILE F 228 1 O VAL F 226 N ILE F 197
SHEET 1 AB3 2 PHE F 163 ASP F 165 0
SHEET 2 AB3 2 LYS F 170 SER F 172 -1 O LEU F 171 N VAL F 164
LINK O GLY F 69 K K F 302 1555 1555 3.24
LINK O SER F 73 K K F 302 1555 1555 3.14
LINK O GLY F 75 K K F 302 1555 1555 2.50
LINK K K F 302 O HOH F 425 1555 1555 3.50
LINK K K F 302 O HOH F 430 1555 1555 2.59
CRYST1 125.237 125.237 101.419 90.00 90.00 120.00 P 32 18
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 0.007985 0.004610 0.000000 0.00000
SCALE2 0.000000 0.009220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009860 0.00000
MTRIX1 1 -0.429385 0.763298 -0.482706 -39.18833 1
MTRIX2 1 0.762649 0.020178 -0.646498 98.03189 1
MTRIX3 1 -0.483730 -0.645731 -0.590793 108.18582 1
MTRIX1 2 0.980471 0.196112 -0.014725 -76.55745 1
MTRIX2 2 -0.196081 0.980581 0.003533 37.75174 1
MTRIX3 2 0.015132 -0.000577 0.999885 -5.89289 1
MTRIX1 3 -0.264815 0.757264 -0.597012 -96.80757 1
MTRIX2 3 0.831294 -0.134484 -0.539318 142.00823 1
MTRIX3 3 -0.488695 -0.639112 -0.593896 101.92053 1
MTRIX1 4 0.569417 -0.820542 0.049740 57.46220 1
MTRIX2 4 -0.821687 -0.569919 0.004825 185.15511 1
MTRIX3 4 0.024388 -0.043618 -0.998751 99.27799 1
MTRIX1 5 -0.893163 0.388029 0.227361 -40.12512 1
MTRIX2 5 -0.079889 -0.634397 0.768868 161.01801 1
MTRIX3 5 0.442580 0.668561 0.597619 -14.37667 1
TER 2045 GLY A 259
TER 4088 GLY B 259
TER 6131 GLY C 259
TER 8170 GLY D 259
TER 10209 GLY E 259
TER 12261 GLY F 259
MASTER 617 0 12 66 60 0 0 2112652 6 72 120
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