HEADER TRANSCRIPTION 09-NOV-12 4HX8
TITLE STRUCTURE OF METAL-FREE MNTR MUTANT E11K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR MNTR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MANGANESE TRANSPORT REGULATOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: MNTR, YQHN, BSU24520;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS WINGED HELIX-TURN-HELIX, TRANSCRIPTION REGULATOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.GLASFELD,A.MCGUIRE
REVDAT 3 20-SEP-23 4HX8 1 SEQADV
REVDAT 2 06-FEB-13 4HX8 1 JRNL
REVDAT 1 21-NOV-12 4HX8 0
JRNL AUTH A.M.MCGUIRE,B.J.CUTHBERT,Z.MA,K.D.GRAUER-GRAY,
JRNL AUTH 2 M.BRUNJES BROPHY,K.A.SPEAR,S.SOONSANGA,J.I.KLIEGMAN,
JRNL AUTH 3 S.L.GRINER,J.D.HELMANN,A.GLASFELD
JRNL TITL ROLES OF THE A AND C SITES IN THE MANGANESE-SPECIFIC
JRNL TITL 2 ACTIVATION OF MNTR.
JRNL REF BIOCHEMISTRY V. 52 701 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23298157
JRNL DOI 10.1021/BI301550T
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 21289
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1086
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.3652 - 4.0011 0.97 2642 120 0.2017 0.2467
REMARK 3 2 4.0011 - 3.1761 1.00 2597 128 0.2228 0.2620
REMARK 3 3 3.1761 - 2.7747 1.00 2529 130 0.2494 0.3471
REMARK 3 4 2.7747 - 2.5210 1.00 2533 156 0.2528 0.3266
REMARK 3 5 2.5210 - 2.3404 1.00 2495 140 0.2545 0.3236
REMARK 3 6 2.3404 - 2.2024 0.99 2489 149 0.2634 0.3446
REMARK 3 7 2.2024 - 2.0921 0.99 2488 123 0.2908 0.3510
REMARK 3 8 2.0921 - 2.0010 0.97 2430 140 0.3060 0.3899
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 : 0.34
REMARK 3 B_SOL : 45.87
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.180
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) : 3.02960
REMARK 3 B22 (A**2) : -1.46840
REMARK 3 B33 (A**2) : -1.56120
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 2223
REMARK 3 ANGLE : 1.006 2979
REMARK 3 CHIRALITY : 0.067 325
REMARK 3 PLANARITY : 0.003 374
REMARK 3 DIHEDRAL : 15.714 878
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 5:24)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0121 66.4964 38.8534
REMARK 3 T TENSOR
REMARK 3 T11: 0.4067 T22: 0.3075
REMARK 3 T33: 0.2046 T12: 0.0172
REMARK 3 T13: -0.1963 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 5.1440 L22: 3.4174
REMARK 3 L33: 4.2132 L12: 0.2054
REMARK 3 L13: -0.7903 L23: -3.6133
REMARK 3 S TENSOR
REMARK 3 S11: 1.2665 S12: 0.1852 S13: -0.4147
REMARK 3 S21: 0.2914 S22: -0.7413 S23: 0.0083
REMARK 3 S31: 0.1561 S32: 0.8941 S33: -0.1936
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 25:43)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2518 67.8293 32.2670
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.7426
REMARK 3 T33: 0.3008 T12: 0.0407
REMARK 3 T13: 0.0236 T23: -0.2142
REMARK 3 L TENSOR
REMARK 3 L11: 7.8641 L22: 2.4559
REMARK 3 L33: 9.9723 L12: 0.6073
REMARK 3 L13: 1.6005 L23: 4.7423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0486 S12: 0.7569 S13: -0.5838
REMARK 3 S21: -0.0030 S22: 1.5897 S23: -0.8554
REMARK 3 S31: -0.3899 S32: 2.5950 S33: -1.3458
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 44:62)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7520 70.7111 27.7892
REMARK 3 T TENSOR
REMARK 3 T11: 0.2583 T22: 0.2994
REMARK 3 T33: 0.1910 T12: 0.0266
REMARK 3 T13: 0.0166 T23: -0.0734
REMARK 3 L TENSOR
REMARK 3 L11: 1.5840 L22: 1.4345
REMARK 3 L33: 8.0907 L12: 0.5161
REMARK 3 L13: -1.5497 L23: -2.1859
REMARK 3 S TENSOR
REMARK 3 S11: 0.5291 S12: 0.1747 S13: 0.0951
REMARK 3 S21: -0.1889 S22: -0.0742 S23: 0.0489
REMARK 3 S31: -0.6956 S32: 1.1117 S33: -0.3891
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 63:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9450 59.0832 39.1697
REMARK 3 T TENSOR
REMARK 3 T11: 0.8912 T22: 0.1669
REMARK 3 T33: 0.2137 T12: -0.2647
REMARK 3 T13: -0.0748 T23: 0.0910
REMARK 3 L TENSOR
REMARK 3 L11: 2.8762 L22: 0.5450
REMARK 3 L33: 6.5699 L12: 1.1256
REMARK 3 L13: 3.1485 L23: 1.6276
REMARK 3 S TENSOR
REMARK 3 S11: 0.8029 S12: -0.8463 S13: -0.3027
REMARK 3 S21: 0.7194 S22: -0.2858 S23: 0.0061
REMARK 3 S31: 2.5546 S32: -1.0593 S33: -0.4080
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 78:105)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3468 50.3613 50.0136
REMARK 3 T TENSOR
REMARK 3 T11: 0.7887 T22: 0.0588
REMARK 3 T33: 0.1223 T12: -0.1639
REMARK 3 T13: 0.0958 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 4.3096 L22: 6.1960
REMARK 3 L33: 2.3533 L12: -2.2763
REMARK 3 L13: -3.1635 L23: 1.4385
REMARK 3 S TENSOR
REMARK 3 S11: 0.5878 S12: 0.1184 S13: 0.6474
REMARK 3 S21: -2.2543 S22: 0.1117 S23: -0.5154
REMARK 3 S31: -0.9090 S32: -0.0118 S33: -0.4435
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 106:136)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2643 45.4223 57.5947
REMARK 3 T TENSOR
REMARK 3 T11: 0.4097 T22: 0.1851
REMARK 3 T33: 0.1602 T12: -0.0140
REMARK 3 T13: -0.1122 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.9171 L22: 7.2885
REMARK 3 L33: 0.6128 L12: -0.1251
REMARK 3 L13: -0.1819 L23: 2.0599
REMARK 3 S TENSOR
REMARK 3 S11: -0.1982 S12: -0.1722 S13: -0.1155
REMARK 3 S21: -0.2983 S22: 0.2762 S23: 0.5478
REMARK 3 S31: -0.5514 S32: -0.0038 S33: 0.0513
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 4:29)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5595 23.7253 36.8829
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.4357
REMARK 3 T33: 0.1230 T12: -0.0228
REMARK 3 T13: 0.0194 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 4.3044 L22: 3.0335
REMARK 3 L33: 0.0897 L12: 1.7586
REMARK 3 L13: 0.1028 L23: 0.1242
REMARK 3 S TENSOR
REMARK 3 S11: 0.1362 S12: -1.2395 S13: 0.1325
REMARK 3 S21: -0.0450 S22: -0.2818 S23: 0.2654
REMARK 3 S31: -0.0348 S32: -0.0259 S33: 0.1140
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 30:60)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.9654 26.0414 32.9313
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.4094
REMARK 3 T33: 0.1654 T12: -0.1287
REMARK 3 T13: -0.0309 T23: -0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 5.2821 L22: 1.4030
REMARK 3 L33: 1.7701 L12: -1.2792
REMARK 3 L13: -2.8931 L23: 0.5663
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: -0.6083 S13: 0.6384
REMARK 3 S21: -0.3381 S22: 0.2952 S23: -0.0721
REMARK 3 S31: -0.2153 S32: 0.6788 S33: -0.3709
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 61:78)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1276 26.6351 47.1753
REMARK 3 T TENSOR
REMARK 3 T11: 0.0442 T22: 1.0282
REMARK 3 T33: 0.1140 T12: -0.0370
REMARK 3 T13: 0.0186 T23: -0.1805
REMARK 3 L TENSOR
REMARK 3 L11: 9.3812 L22: 1.9696
REMARK 3 L33: 5.2627 L12: -1.4738
REMARK 3 L13: -5.7333 L23: 2.3500
REMARK 3 S TENSOR
REMARK 3 S11: -0.0563 S12: -3.3442 S13: 0.4078
REMARK 3 S21: 0.1800 S22: 0.7277 S23: -0.2046
REMARK 3 S31: -0.1261 S32: 1.8758 S33: -0.7254
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 79:102)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2118 35.9068 44.0053
REMARK 3 T TENSOR
REMARK 3 T11: 0.5802 T22: 0.1865
REMARK 3 T33: 0.1358 T12: -0.1669
REMARK 3 T13: -0.0575 T23: -0.0536
REMARK 3 L TENSOR
REMARK 3 L11: 0.9772 L22: 8.8960
REMARK 3 L33: 0.1038 L12: -0.0063
REMARK 3 L13: -0.1360 L23: 0.8351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0609 S12: 0.0869 S13: -0.1462
REMARK 3 S21: -2.2582 S22: 0.3634 S23: 0.3955
REMARK 3 S31: -0.3549 S32: 0.1066 S33: -0.2284
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 103:118)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9522 39.4167 52.9914
REMARK 3 T TENSOR
REMARK 3 T11: 0.1954 T22: 0.2520
REMARK 3 T33: 0.2016 T12: -0.0396
REMARK 3 T13: -0.0418 T23: -0.0764
REMARK 3 L TENSOR
REMARK 3 L11: 5.4992 L22: 5.1259
REMARK 3 L33: 2.3076 L12: 4.3708
REMARK 3 L13: 0.9615 L23: 2.3921
REMARK 3 S TENSOR
REMARK 3 S11: -0.2284 S12: 0.7588 S13: -0.1625
REMARK 3 S21: -0.3886 S22: 0.7235 S23: -0.5079
REMARK 3 S31: -0.1656 S32: 0.0603 S33: -0.3442
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 119:136)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3718 38.3605 57.4236
REMARK 3 T TENSOR
REMARK 3 T11: 0.3306 T22: 0.1109
REMARK 3 T33: 0.3828 T12: -0.0313
REMARK 3 T13: 0.0102 T23: 0.0486
REMARK 3 L TENSOR
REMARK 3 L11: 2.4962 L22: 4.7719
REMARK 3 L33: 2.0333 L12: -3.2204
REMARK 3 L13: 0.5634 L23: -1.6501
REMARK 3 S TENSOR
REMARK 3 S11: 0.2108 S12: -0.2020 S13: -0.5592
REMARK 3 S21: 0.1887 S22: 0.0120 S23: 1.1256
REMARK 3 S31: -0.5787 S32: -0.1275 S33: -0.2775
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 4HX8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076033.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21377
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 45.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: EPMR
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 2HYF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 4000, 4% ETHANOL, 2% 1,4
REMARK 280 -BUTANEDIOL, 4 MM EDTA, 0.1 M SODIUM ACETATE , PH 4.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 19.46000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.59500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.35500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.59500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.46000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.35500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 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 A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 THR A 137
REMARK 465 GLU A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
REMARK 465 ASN A 141
REMARK 465 GLN A 142
REMARK 465 THR B 2
REMARK 465 THR B 3
REMARK 465 LYS B 56
REMARK 465 TYR B 57
REMARK 465 ARG B 58
REMARK 465 THR B 137
REMARK 465 GLU B 138
REMARK 465 HIS B 139
REMARK 465 HIS B 140
REMARK 465 ASN B 141
REMARK 465 GLN B 142
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 ASP B 123 115.84 -171.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HX4 RELATED DB: PDB
REMARK 900 RELATED ID: 4HX7 RELATED DB: PDB
REMARK 900 RELATED ID: 4HV6 RELATED DB: PDB
DBREF 4HX8 A 2 142 UNP P54512 MNTR_BACSU 2 142
DBREF 4HX8 B 2 142 UNP P54512 MNTR_BACSU 2 142
SEQADV 4HX8 LYS A 11 UNP P54512 GLU 11 ENGINEERED MUTATION
SEQADV 4HX8 LYS B 11 UNP P54512 GLU 11 ENGINEERED MUTATION
SEQRES 1 A 141 THR THR PRO SER MET GLU ASP TYR ILE LYS GLN ILE TYR
SEQRES 2 A 141 MET LEU ILE GLU GLU LYS GLY TYR ALA ARG VAL SER ASP
SEQRES 3 A 141 ILE ALA GLU ALA LEU ALA VAL HIS PRO SER SER VAL THR
SEQRES 4 A 141 LYS MET VAL GLN LYS LEU ASP LYS ASP GLU TYR LEU ILE
SEQRES 5 A 141 TYR GLU LYS TYR ARG GLY LEU VAL LEU THR SER LYS GLY
SEQRES 6 A 141 LYS LYS ILE GLY LYS ARG LEU VAL TYR ARG HIS GLU LEU
SEQRES 7 A 141 LEU GLU GLN PHE LEU ARG ILE ILE GLY VAL ASP GLU GLU
SEQRES 8 A 141 LYS ILE TYR ASN ASP VAL GLU GLY ILE GLU HIS HIS LEU
SEQRES 9 A 141 SER TRP ASN SER ILE ASP ARG ILE GLY ASP LEU VAL GLN
SEQRES 10 A 141 TYR PHE GLU GLU ASP ASP ALA ARG LYS LYS ASP LEU LYS
SEQRES 11 A 141 SER ILE GLN LYS LYS THR GLU HIS HIS ASN GLN
SEQRES 1 B 141 THR THR PRO SER MET GLU ASP TYR ILE LYS GLN ILE TYR
SEQRES 2 B 141 MET LEU ILE GLU GLU LYS GLY TYR ALA ARG VAL SER ASP
SEQRES 3 B 141 ILE ALA GLU ALA LEU ALA VAL HIS PRO SER SER VAL THR
SEQRES 4 B 141 LYS MET VAL GLN LYS LEU ASP LYS ASP GLU TYR LEU ILE
SEQRES 5 B 141 TYR GLU LYS TYR ARG GLY LEU VAL LEU THR SER LYS GLY
SEQRES 6 B 141 LYS LYS ILE GLY LYS ARG LEU VAL TYR ARG HIS GLU LEU
SEQRES 7 B 141 LEU GLU GLN PHE LEU ARG ILE ILE GLY VAL ASP GLU GLU
SEQRES 8 B 141 LYS ILE TYR ASN ASP VAL GLU GLY ILE GLU HIS HIS LEU
SEQRES 9 B 141 SER TRP ASN SER ILE ASP ARG ILE GLY ASP LEU VAL GLN
SEQRES 10 B 141 TYR PHE GLU GLU ASP ASP ALA ARG LYS LYS ASP LEU LYS
SEQRES 11 B 141 SER ILE GLN LYS LYS THR GLU HIS HIS ASN GLN
FORMUL 3 HOH *51(H2 O)
HELIX 1 1 SER A 5 GLY A 21 1 17
HELIX 2 2 ARG A 24 ALA A 33 1 10
HELIX 3 3 HIS A 35 ASP A 49 1 15
HELIX 4 4 THR A 63 ILE A 87 1 25
HELIX 5 5 ASP A 90 GLU A 92 5 3
HELIX 6 6 LYS A 93 HIS A 103 1 11
HELIX 7 7 SER A 106 ASP A 123 1 18
HELIX 8 8 ASP A 123 LYS A 135 1 13
HELIX 9 9 SER B 5 GLY B 21 1 17
HELIX 10 10 ARG B 24 ALA B 33 1 10
HELIX 11 11 HIS B 35 ASP B 49 1 15
HELIX 12 12 THR B 63 ILE B 87 1 25
HELIX 13 13 ASP B 90 HIS B 103 1 14
HELIX 14 14 SER B 106 GLU B 122 1 17
HELIX 15 15 ASP B 123 GLN B 134 1 12
SHEET 1 A 2 LEU A 52 GLU A 55 0
SHEET 2 A 2 GLY A 59 LEU A 62 -1 O VAL A 61 N ILE A 53
SHEET 1 B 2 LEU B 52 ILE B 53 0
SHEET 2 B 2 VAL B 61 LEU B 62 -1 O VAL B 61 N ILE B 53
CRYST1 38.920 86.710 91.190 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025694 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011533 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010966 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
