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PDBsum entry 3t8g

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Hydrolase/hydrolase inhibitor PDB id
3t8g
Jmol
Contents
Protein chain
316 a.a.
Ligands
UBT
GOL ×4
DMS ×5
Metals
_CA ×4
_ZN
Waters ×442
HEADER    HYDROLASE/HYDROLASE INHIBITOR           01-AUG-11   3T8G
TITLE     THERMOLYSIN IN COMPLEX WITH UBTLN26
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THERMOLYSIN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: MATURE FORM (UNP RESIDUES 233-548);
COMPND   5 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;
COMPND   6 EC: 3.4.24.27
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;
SOURCE   3 ORGANISM_TAXID: 1427
KEYWDS    PROTEASE, METALLOPROTEASE, HYDROLYSIS OF PEPTIDE BONDS,
KEYWDS   2 PHOSPHORAMIDON, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.BIELA,A.HEINE,G.KLEBE
REVDAT   2   12-FEB-14 3T8G    1       JRNL
REVDAT   1   01-AUG-12 3T8G    0
JRNL        AUTH   A.BIELA,M.BETZ,A.HEINE,G.KLEBE
JRNL        TITL   WATER MAKES THE DIFFERENCE: REARRANGEMENT OF WATER SOLVATION
JRNL        TITL 2 LAYER TRIGGERS NON-ADDITIVITY OF FUNCTIONAL GROUP
JRNL        TITL 3 CONTRIBUTIONS IN PROTEIN-LIGAND BINDING.
JRNL        REF    CHEMMEDCHEM                   V.   7  1423 2012
JRNL        REFN                   ISSN 1860-7179
JRNL        PMID   22733601
JRNL        DOI    10.1002/CMDC.201200206
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.14
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6
REMARK   3   NUMBER OF REFLECTIONS             : 52333
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.142
REMARK   3   R VALUE            (WORKING SET) : 0.142
REMARK   3   FREE R VALUE                     : 0.156
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060
REMARK   3   FREE R VALUE TEST SET COUNT      : 2649
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 40.1546 -  4.0014    1.00     2951   147  0.1531 0.1426
REMARK   3     2  4.0014 -  3.1764    1.00     2781   150  0.1344 0.1494
REMARK   3     3  3.1764 -  2.7750    1.00     2716   142  0.1402 0.1328
REMARK   3     4  2.7750 -  2.5214    1.00     2698   148  0.1421 0.1623
REMARK   3     5  2.5214 -  2.3407    0.99     2668   150  0.1405 0.1495
REMARK   3     6  2.3407 -  2.2027    0.99     2657   141  0.1370 0.1423
REMARK   3     7  2.2027 -  2.0924    1.00     2673   147  0.1370 0.1642
REMARK   3     8  2.0924 -  2.0013    0.99     2648   137  0.1429 0.1895
REMARK   3     9  2.0013 -  1.9242    0.99     2640   131  0.1387 0.1460
REMARK   3    10  1.9242 -  1.8578    0.98     2592   150  0.1312 0.1647
REMARK   3    11  1.8578 -  1.7998    0.97     2570   130  0.1300 0.1526
REMARK   3    12  1.7998 -  1.7483    0.97     2558   150  0.1354 0.1764
REMARK   3    13  1.7483 -  1.7023    0.97     2566   135  0.1390 0.1826
REMARK   3    14  1.7023 -  1.6607    0.96     2544   133  0.1395 0.1543
REMARK   3    15  1.6607 -  1.6230    0.96     2535   127  0.1408 0.1766
REMARK   3    16  1.6230 -  1.5885    0.95     2507   133  0.1428 0.1609
REMARK   3    17  1.5885 -  1.5567    0.95     2468   146  0.1525 0.1776
REMARK   3    18  1.5567 -  1.5273    0.94     2468   131  0.1631 0.1814
REMARK   3    19  1.5273 -  1.5000    0.93     2444   121  0.1714 0.2070
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   : 0.83
REMARK   3   K_SOL              : 0.35
REMARK   3   B_SOL              : 46.03
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.370
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) : -1.45430
REMARK   3    B22 (A**2) : -1.45430
REMARK   3    B33 (A**2) : 2.90860
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      :  0.012           2657
REMARK   3   ANGLE     :  1.054           3672
REMARK   3   CHIRALITY :  0.075            382
REMARK   3   PLANARITY :  0.005            470
REMARK   3   DIHEDRAL  : 15.241            932
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 9
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (chain A and resid 1:6)
REMARK   3    ORIGIN FOR THE GROUP (A):  37.4323  24.0218   4.7586
REMARK   3    T TENSOR
REMARK   3      T11:   0.1105 T22:   0.1454
REMARK   3      T33:   0.1178 T12:   0.0086
REMARK   3      T13:   0.0015 T23:   0.0283
REMARK   3    L TENSOR
REMARK   3      L11:   0.1736 L22:   0.1498
REMARK   3      L33:   0.6485 L12:  -0.1208
REMARK   3      L13:   0.0205 L23:   0.1920
REMARK   3    S TENSOR
REMARK   3      S11:   0.0533 S12:   0.1743 S13:   0.0831
REMARK   3      S21:  -0.0200 S22:  -0.0547 S23:  -0.0637
REMARK   3      S31:   0.0148 S32:   0.0157 S33:   0.0054
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (chain A and resid 7:125)
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4375  31.8916   3.3552
REMARK   3    T TENSOR
REMARK   3      T11:   0.0689 T22:   0.0830
REMARK   3      T33:   0.0537 T12:   0.0053
REMARK   3      T13:   0.0075 T23:   0.0026
REMARK   3    L TENSOR
REMARK   3      L11:   0.3689 L22:   0.3274
REMARK   3      L33:   0.1024 L12:   0.0115
REMARK   3      L13:   0.1848 L23:  -0.0423
REMARK   3    S TENSOR
REMARK   3      S11:   0.0123 S12:  -0.0255 S13:  -0.0190
REMARK   3      S21:   0.0442 S22:  -0.0078 S23:  -0.0155
REMARK   3      S31:  -0.0102 S32:  -0.0027 S33:  -0.0011
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (chain A and resid 126:131)
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5462  46.2013   7.6213
REMARK   3    T TENSOR
REMARK   3      T11:   0.0995 T22:   0.1219
REMARK   3      T33:   0.1366 T12:   0.0101
REMARK   3      T13:   0.0258 T23:  -0.0367
REMARK   3    L TENSOR
REMARK   3      L11:   0.2162 L22:   0.2213
REMARK   3      L33:   0.0912 L12:   0.0701
REMARK   3      L13:  -0.1349 L23:  -0.0769
REMARK   3    S TENSOR
REMARK   3      S11:   0.0513 S12:   0.0465 S13:   0.0394
REMARK   3      S21:   0.0068 S22:  -0.0118 S23:   0.0888
REMARK   3      S31:  -0.0570 S32:  -0.0662 S33:  -0.0141
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (chain A and resid 132:181)
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9593  30.5425  -6.2914
REMARK   3    T TENSOR
REMARK   3      T11:   0.0668 T22:   0.0876
REMARK   3      T33:   0.0700 T12:   0.0081
REMARK   3      T13:   0.0094 T23:   0.0007
REMARK   3    L TENSOR
REMARK   3      L11:   0.0688 L22:   0.0676
REMARK   3      L33:   0.0371 L12:  -0.0075
REMARK   3      L13:   0.0261 L23:   0.0400
REMARK   3    S TENSOR
REMARK   3      S11:   0.0007 S12:  -0.0075 S13:  -0.0117
REMARK   3      S21:  -0.0125 S22:  -0.0112 S23:   0.0099
REMARK   3      S31:   0.0090 S32:  -0.0014 S33:   0.0034
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (chain A and resid 182:201)
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6936  35.5900   7.6466
REMARK   3    T TENSOR
REMARK   3      T11:   0.0944 T22:   0.1488
REMARK   3      T33:   0.1166 T12:  -0.0109
REMARK   3      T13:   0.0348 T23:  -0.0280
REMARK   3    L TENSOR
REMARK   3      L11:   0.1111 L22:   0.0915
REMARK   3      L33:   0.1889 L12:   0.0816
REMARK   3      L13:   0.1415 L23:   0.1204
REMARK   3    S TENSOR
REMARK   3      S11:   0.0768 S12:  -0.1089 S13:   0.0852
REMARK   3      S21:   0.0773 S22:  -0.1029 S23:   0.0985
REMARK   3      S31:   0.0447 S32:  -0.1565 S33:   0.0324
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: (chain A and resid 202:220)
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.6385  36.7400  -5.6251
REMARK   3    T TENSOR
REMARK   3      T11:   0.0615 T22:   0.1287
REMARK   3      T33:   0.1488 T12:   0.0005
REMARK   3      T13:   0.0042 T23:  -0.0169
REMARK   3    L TENSOR
REMARK   3      L11:   0.0194 L22:   0.1746
REMARK   3      L33:   0.1620 L12:   0.0121
REMARK   3      L13:  -0.0516 L23:   0.0320
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0246 S12:  -0.0638 S13:   0.0768
REMARK   3      S21:  -0.0163 S22:  -0.0148 S23:   0.1999
REMARK   3      S31:  -0.0448 S32:  -0.0981 S33:   0.0068
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: (chain A and resid 221:227)
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6264  46.0795 -14.2781
REMARK   3    T TENSOR
REMARK   3      T11:   0.1438 T22:   0.0925
REMARK   3      T33:   0.1600 T12:   0.0065
REMARK   3      T13:  -0.0353 T23:   0.0094
REMARK   3    L TENSOR
REMARK   3      L11:   0.0743 L22:   0.1157
REMARK   3      L33:   0.2151 L12:  -0.0747
REMARK   3      L13:  -0.0370 L23:  -0.0482
REMARK   3    S TENSOR
REMARK   3      S11:   0.0157 S12:   0.0090 S13:   0.0202
REMARK   3      S21:  -0.1361 S22:   0.0201 S23:   0.1003
REMARK   3      S31:   0.0347 S32:   0.0082 S33:  -0.0274
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: (chain A and resid 228:297)
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7912  23.6149 -11.2936
REMARK   3    T TENSOR
REMARK   3      T11:   0.0690 T22:   0.0962
REMARK   3      T33:   0.1077 T12:  -0.0029
REMARK   3      T13:   0.0003 T23:  -0.0137
REMARK   3    L TENSOR
REMARK   3      L11:   0.1953 L22:   0.2205
REMARK   3      L33:   0.2154 L12:   0.0098
REMARK   3      L13:   0.1510 L23:  -0.0385
REMARK   3    S TENSOR
REMARK   3      S11:   0.0323 S12:   0.0018 S13:  -0.0599
REMARK   3      S21:  -0.0357 S22:  -0.0217 S23:   0.0932
REMARK   3      S31:   0.0523 S32:  -0.0739 S33:  -0.0088
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: (chain A and resid 298:316)
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.4921  19.7948 -12.9823
REMARK   3    T TENSOR
REMARK   3      T11:   0.0923 T22:   0.1429
REMARK   3      T33:   0.1925 T12:  -0.0229
REMARK   3      T13:  -0.0230 T23:  -0.0296
REMARK   3    L TENSOR
REMARK   3      L11:   0.0251 L22:   0.3883
REMARK   3      L33:   0.3140 L12:   0.0674
REMARK   3      L13:  -0.0606 L23:   0.0228
REMARK   3    S TENSOR
REMARK   3      S11:   0.0680 S12:   0.1160 S13:  -0.2209
REMARK   3      S21:  -0.0439 S22:  -0.0242 S23:   0.1273
REMARK   3      S31:   0.0456 S32:  -0.0986 S33:   0.0114
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 3T8G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-11.
REMARK 100 THE RCSB ID CODE IS RCSB067168.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06DA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : BARTELS
REMARK 200  OPTICS                         : COLLIMATING MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53702
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
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     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 20.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07900
REMARK 200   FOR THE DATA SET  : 41.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.50
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.49900
REMARK 200   FOR SHELL         : 6.600
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: PDB ENTRY 8TLN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS, 1.9 M CESIUM CHLORIDE, 50%
REMARK 280  DMSO, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/6
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       43.60000
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       87.20000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.40000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      109.00000
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       21.80000
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.60000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.20000
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      109.00000
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.40000
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.80000
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: 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 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 A 552  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 550  LIES ON A SPECIAL POSITION.
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 182    CG   CD   CE   NZ
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    THR A  26      -59.46     69.70
REMARK 500    SER A  92     -173.21     61.06
REMARK 500    SER A 107     -161.83     59.82
REMARK 500    ASN A 111       51.36    -90.75
REMARK 500    THR A 152     -100.56   -118.99
REMARK 500    ASN A 159     -144.31     55.75
REMARK 500    THR A 194       77.33     41.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: N-[(R)-({[(BENZYLOXY)CARBONYL]AMINO}METHYL)
REMARK 630 (HYDROXY)PHOSPHORYL]-L-LEUCYLGLYCINE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     UBT A   401
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP:    PHQ PGL LEU GLY
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UBT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 415
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3T73   RELATED DB: PDB
REMARK 900 RELATED ID: 3T74   RELATED DB: PDB
REMARK 900 RELATED ID: 3T87   RELATED DB: PDB
REMARK 900 RELATED ID: 3T8C   RELATED DB: PDB
REMARK 900 RELATED ID: 3T8D   RELATED DB: PDB
REMARK 900 RELATED ID: 3T8F   RELATED DB: PDB
REMARK 900 RELATED ID: 3T8H   RELATED DB: PDB
DBREF  3T8G A    1   316  UNP    P00800   THER_BACTH     233    548
SEQRES   1 A  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL
SEQRES   2 A  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR
SEQRES   3 A  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASN GLY ILE
SEQRES   4 A  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY
SEQRES   5 A  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER
SEQRES   6 A  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY
SEQRES   7 A  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU
SEQRES   8 A  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL
SEQRES   9 A  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY
SEQRES  10 A  316  SER GLN MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE
SEQRES  11 A  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU
SEQRES  12 A  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE
SEQRES  13 A  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER
SEQRES  14 A  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS
SEQRES  15 A  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO
SEQRES  16 A  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO
SEQRES  17 A  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR
SEQRES  18 A  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER
SEQRES  19 A  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY
SEQRES  20 A  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG
SEQRES  21 A  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN
SEQRES  22 A  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA
SEQRES  23 A  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR
SEQRES  24 A  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA
SEQRES  25 A  316  VAL GLY VAL LYS
HET    UBT  A 401      32
HET    GOL  A 402       6
HET    GOL  A 403       6
HET    GOL  A 404       6
HET    GOL  A 405       6
HET    DMS  A 406       4
HET    DMS  A 407       4
HET    DMS  A 408       4
HET    DMS  A 409       4
HET    DMS  A 410       4
HET     ZN  A 411       1
HET     CA  A 412       1
HET     CA  A 413       1
HET     CA  A 414       1
HET     CA  A 415       1
HETNAM     UBT N-[(R)-({[(BENZYLOXY)CARBONYL]AMINO}METHYL)(HYDROXY)
HETNAM   2 UBT  PHOSPHORYL]-L-LEUCYLGLYCINE
HETNAM     GOL GLYCEROL
HETNAM     DMS DIMETHYL SULFOXIDE
HETNAM      ZN ZINC ION
HETNAM      CA CALCIUM ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  UBT    C17 H26 N3 O7 P
FORMUL   3  GOL    4(C3 H8 O3)
FORMUL   7  DMS    5(C2 H6 O S)
FORMUL  12   ZN    ZN 2+
FORMUL  13   CA    4(CA 2+)
FORMUL  17  HOH   *442(H2 O)
HELIX    1   1 ALA A   64  TYR A   66  5                                   3
HELIX    2   2 ASP A   67  ASN A   89  1                                  23
HELIX    3   3 PRO A  132  GLY A  135  5                                   4
HELIX    4   4 GLY A  136  THR A  152  1                                  17
HELIX    5   5 GLN A  158  ASN A  181  1                                  24
HELIX    6   6 ASP A  207  GLY A  212  5                                   6
HELIX    7   7 HIS A  216  ARG A  220  5                                   5
HELIX    8   8 THR A  224  VAL A  230  1                                   7
HELIX    9   9 ASN A  233  GLY A  247  1                                  15
HELIX   10  10 GLY A  259  TYR A  274  1                                  16
HELIX   11  11 ASN A  280  GLY A  297  1                                  18
HELIX   12  12 SER A  300  VAL A  313  1                                  14
SHEET    1   A 5 ALA A  56  ASP A  57  0
SHEET    2   A 5 TYR A  28  TYR A  29 -1  N  TYR A  28   O  ASP A  57
SHEET    3   A 5 GLN A  17  TYR A  24 -1  N  THR A  23   O  TYR A  29
SHEET    4   A 5 THR A   4  ARG A  11 -1  N  THR A   4   O  TYR A  24
SHEET    5   A 5 GLN A  61  PHE A  62  1  O  PHE A  62   N  VAL A   9
SHEET    1   B 3 GLN A  31  ASP A  32  0
SHEET    2   B 3 ILE A  39  ASP A  43 -1  O  ILE A  39   N  ASP A  32
SHEET    3   B 3 SER A  53  LEU A  54 -1  O  SER A  53   N  ASP A  43
SHEET    1   C 5 GLN A  31  ASP A  32  0
SHEET    2   C 5 ILE A  39  ASP A  43 -1  O  ILE A  39   N  ASP A  32
SHEET    3   C 5 ILE A 100  TYR A 106  1  O  ILE A 100   N  PHE A  40
SHEET    4   C 5 MET A 120  GLY A 123  1  O  MET A 120   N  ARG A 101
SHEET    5   C 5 ALA A 113  TRP A 115 -1  N  PHE A 114   O  VAL A 121
SHEET    1   D 2 GLU A 187  ILE A 188  0
SHEET    2   D 2 ARG A 203  SER A 204 -1  O  ARG A 203   N  ILE A 188
SHEET    1   E 2 GLY A 248  HIS A 250  0
SHEET    2   E 2 VAL A 253  VAL A 255 -1  O  VAL A 255   N  GLY A 248
CISPEP   1 LEU A   50    PRO A   51          0         5.00
SITE     1 AC1 18 TYR A 106  ASN A 112  ALA A 113  PHE A 114
SITE     2 AC1 18 TRP A 115  HIS A 142  GLU A 143  HIS A 146
SITE     3 AC1 18 TYR A 157  GLU A 166  ARG A 203  HIS A 231
SITE     4 AC1 18 GOL A 404  DMS A 406   ZN A 411  HOH A 852
SITE     5 AC1 18 HOH A 858  HOH A 875
SITE     1 AC2 10 GLY A 247  GLY A 248  VAL A 255  GLN A 273
SITE     2 AC2 10 LEU A 275  HOH A 670  HOH A 680  HOH A 705
SITE     3 AC2 10 HOH A 753  HOH A 864
SITE     1 AC3  8 SER A  65  TYR A  66  PRO A  69  HIS A 105
SITE     2 AC3  8 ASP A 124  HOH A 577  HOH A 850  HOH A 871
SITE     1 AC4  8 PHE A 114  TRP A 115  HIS A 146  TYR A 157
SITE     2 AC4  8 UBT A 401  HOH A 621  HOH A 657  HOH A 676
SITE     1 AC5  9 GLY A 109  TYR A 110  ASN A 111  ASN A 112
SITE     2 AC5  9 GLN A 158  DMS A 406  HOH A 671  HOH A 800
SITE     3 AC5  9 HOH A 867
SITE     1 AC6  6 TYR A 110  ASN A 112  PHE A 114  UBT A 401
SITE     2 AC6  6 GOL A 405  HOH A 730
SITE     1 AC7  5 ILE A   1  THR A   2  GLY A   3  GLN A  31
SITE     2 AC7  5 ASN A  33
SITE     1 AC8  2 TYR A  24  SER A  25
SITE     1 AC9  4 TYR A  66  HIS A 216  TYR A 251  HOH A 767
SITE     1 BC1  5 GLY A  95  PRO A 184  TRP A 186  HOH A 686
SITE     2 BC1  5 HOH A 848
SITE     1 BC2  4 HIS A 142  HIS A 146  GLU A 166  UBT A 401
SITE     1 BC3  6 ASP A 138  GLU A 177  ASP A 185  GLU A 187
SITE     2 BC3  6 GLU A 190  HOH A 907
SITE     1 BC4  6 GLU A 177  ASN A 183  ASP A 185  GLU A 190
SITE     2 BC4  6 HOH A 912  HOH A 913
SITE     1 BC5  6 TYR A 193  THR A 194  ILE A 197  ASP A 200
SITE     2 BC5  6 HOH A 910  HOH A 914
SITE     1 BC6  6 ASP A  57  ASP A  59  GLN A  61  HOH A 908
SITE     2 BC6  6 HOH A 909  HOH A 911
CRYST1   92.700   92.700  130.800  90.00  90.00 120.00 P 61 2 2     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      0.010787  0.006228  0.000000        0.00000
SCALE2      0.000000  0.012456  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007645        0.00000
      
PROCHECK
Go to PROCHECK summary
 References