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PDBsum entry 3lwb

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Ligase PDB id
3lwb
Jmol
Contents
Protein chains
323 a.a.
298 a.a.
Ligands
NO3 ×2
Waters ×383
HEADER    LIGASE                                  23-FEB-10   3LWB
TITLE     CRYSTAL STRUCTURE OF APO D-ALANINE:D-ALANINE LIGASE (DDL) FROM
TITLE    2 MYCOBACTERIUM TUBERCULOSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;
COMPND   5 EC: 6.3.2.4;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE   3 ORGANISM_TAXID: 1773;
SOURCE   4 GENE: DDL, DDLA, MT3059, MTCY349.06, RV2981C;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PVP16
KEYWDS    D-ALANINE--D-ALANINE LIGASE, DDL, D-ALANYL--D-ALANINE LIGASE,
KEYWDS   2 RV2981C, D-ALANINE, STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS
KEYWDS   3 CONSORTIUM, TBSGC, ATP-BINDING, CELL SHAPE, CELL WALL BIOGENESIS,
KEYWDS   4 DEGRADATION, LIGASE, MAGNESIUM, MANGANESE, METAL-BINDING,
KEYWDS   5 NUCLEOTIDE-BINDING, PEPTIDOGLYCAN SYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.B.BRUNING,A.C.MURILLO,O.CHACON,R.G.BARLETTA,J.C.SACCHETTINI,TB
AUTHOR   2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT   3   05-JAN-11 3LWB    1       JRNL
REVDAT   2   08-DEC-10 3LWB    1       JRNL
REVDAT   1   09-MAR-10 3LWB    0
JRNL        AUTH   J.B.BRUNING,A.C.MURILLO,O.CHACON,R.G.BARLETTA,
JRNL        AUTH 2 J.C.SACCHETTINI
JRNL        TITL   STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS
JRNL        TITL 2 D-ALANINE:D-ALANINE LIGASE, A TARGET OF THE ANTITUBERCULOSIS
JRNL        TITL 3 DRUG D-CYCLOSERINE.
JRNL        REF    ANTIMICROB.AGENTS CHEMOTHER.  V.  55   291 2011
JRNL        REFN                   ISSN 0066-4804
JRNL        PMID   20956591
JRNL        DOI    10.1128/AAC.00558-10
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.20
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.8
REMARK   3   NUMBER OF REFLECTIONS             : 38758
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.173
REMARK   3   FREE R VALUE                     : 0.221
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890
REMARK   3   FREE R VALUE TEST SET COUNT      : 1896
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 19.2040 -  8.5520    0.93      569     0  0.1700 0.0000
REMARK   3     2  8.5520 -  6.8910    0.95      585     0  0.1540 0.0000
REMARK   3     3  6.8910 -  6.0510    0.94      566     0  0.1820 0.0000
REMARK   3     4  6.0510 -  5.5120    0.95      566     0  0.1900 0.0000
REMARK   3     5  5.5120 -  5.1250    0.95      550     0  0.1670 0.0000
REMARK   3     6  5.1250 -  4.8280    0.95      581     0  0.1450 0.0000
REMARK   3     7  4.8280 -  4.5890    0.94      540     0  0.1320 0.0000
REMARK   3     8  4.5890 -  4.3920    0.94      565     0  0.1290 0.0000
REMARK   3     9  4.3920 -  4.2250    0.94      566     0  0.1440 0.0000
REMARK   3    10  4.2250 -  4.0810    0.94      550     0  0.1470 0.0000
REMARK   3    11  4.0810 -  3.9540    0.94      559     0  0.1490 0.0000
REMARK   3    12  3.9540 -  3.8420    0.93      556     0  0.1420 0.0000
REMARK   3    13  3.8420 -  3.7420    0.94      546     0  0.1520 0.0000
REMARK   3    14  3.7420 -  3.6510    0.94      549     0  0.1610 0.0000
REMARK   3    15  3.6510 -  3.5690    0.94      568     0  0.1660 0.0000
REMARK   3    16  3.5690 -  3.4930    0.94      567     0  0.1480 0.0000
REMARK   3    17  3.4930 -  3.4240    0.94      530     0  0.1640 0.0000
REMARK   3    18  3.4240 -  3.3590    0.92      565     0  0.1660 0.0000
REMARK   3    19  3.3590 -  3.3000    0.93      552     0  0.1670 0.0000
REMARK   3    20  3.3000 -  3.2440    0.93      530     0  0.1830 0.0000
REMARK   3    21  3.2440 -  3.1920    0.93      551     0  0.1830 0.0000
REMARK   3    22  3.1920 -  3.1430    0.94      561     0  0.1670 0.0000
REMARK   3    23  3.1430 -  3.0970    0.91      536     0  0.1710 0.0000
REMARK   3    24  3.0970 -  3.0530    0.93      535     0  0.1790 0.0000
REMARK   3    25  3.0530 -  3.0120    0.91      548     0  0.1910 0.0000
REMARK   3    26  3.0120 -  2.9730    0.91      553     0  0.1830 0.0000
REMARK   3    27  2.9730 -  2.9360    0.90      524     0  0.1860 0.0000
REMARK   3    28  2.9360 -  2.9010    0.89      527     0  0.1650 0.0000
REMARK   3    29  2.9010 -  2.8680    0.90      511     0  0.1750 0.0000
REMARK   3    30  2.8680 -  2.8350    0.87      526     0  0.1860 0.0000
REMARK   3    31  2.8350 -  2.8050    0.88      519     0  0.1880 0.0000
REMARK   3    32  2.8050 -  2.7750    0.88      507     0  0.2020 0.0000
REMARK   3    33  2.7750 -  2.7470    0.88      517     0  0.1790 0.0000
REMARK   3    34  2.7470 -  2.7200    0.89      512     0  0.1740 0.0000
REMARK   3    35  2.7200 -  2.6940    0.84      521     0  0.1760 0.0000
REMARK   3    36  2.6940 -  2.6690    0.85      491     0  0.1880 0.0000
REMARK   3    37  2.6690 -  2.6450    0.87      532     0  0.1860 0.0000
REMARK   3    38  2.6450 -  2.6210    0.84      473     0  0.1670 0.0000
REMARK   3    39  2.6210 -  2.5990    0.86      507     0  0.1740 0.0000
REMARK   3    40  2.5990 -  2.5770    0.86      508     0  0.1860 0.0000
REMARK   3    41  2.5770 -  2.5560    0.82      487     0  0.1850 0.0000
REMARK   3    42  2.5560 -  2.5350    0.83      492     0  0.1900 0.0000
REMARK   3    43  2.5350 -  2.5160    0.82      486     0  0.1680 0.0000
REMARK   3    44  2.5160 -  2.4960    0.83      483     0  0.1590 0.0000
REMARK   3    45  2.4960 -  2.4780    0.85      483     0  0.1700 0.0000
REMARK   3    46  2.4780 -  2.4600    0.82      470     0  0.1650 0.0000
REMARK   3    47  2.4600 -  2.4420    0.79      500     0  0.1800 0.0000
REMARK   3    48  2.4420 -  2.4250    0.80      468     0  0.1750 0.0000
REMARK   3    49  2.4250 -  2.4090    0.80      476     0  0.1580 0.0000
REMARK   3    50  2.4090 -  2.3920    0.81      454     0  0.1720 0.0000
REMARK   3    51  2.3920 -  2.3770    0.80      459     0  0.1780 0.0000
REMARK   3    52  2.3770 -  2.3620    0.81      491     0  0.1710 0.0000
REMARK   3    53  2.3620 -  2.3460    0.79      463     0  0.1700 0.0000
REMARK   3    54  2.3460 -  2.3320    0.76      456     0  0.1770 0.0000
REMARK   3    55  2.3320 -  2.3180    0.80      457     0  0.1900 0.0000
REMARK   3    56  2.3180 -  2.3040    0.76      447     0  0.1900 0.0000
REMARK   3    57  2.3040 -  2.2900    0.78      476     0  0.2060 0.0000
REMARK   3    58  2.2900 -  2.2770    0.76      440     0  0.1950 0.0000
REMARK   3    59  2.2770 -  2.2640    0.77      431     0  0.2000 0.0000
REMARK   3    60  2.2640 -  2.2520    0.81      476     0  0.2250 0.0000
REMARK   3    61  2.2520 -  2.2390    0.75      452     0  0.2310 0.0000
REMARK   3    62  2.2390 -  2.2270    0.69      390     0  0.2220 0.0000
REMARK   3    63  2.2270 -  2.2150    0.75      472     0  0.2200 0.0000
REMARK   3    64  2.2150 -  2.2040    0.76      426     0  0.2240 0.0000
REMARK   3    65  2.2040 -  2.1930    0.77      465     0  0.2350 0.0000
REMARK   3    66  2.1930 -  2.1810    0.74      420     0  0.2450 0.0000
REMARK   3    67  2.1810 -  2.1710    0.73      427     0  0.2470 0.0000
REMARK   3    68  2.1710 -  2.1600    0.72      411     0  0.2590 0.0000
REMARK   3    69  2.1600 -  2.1490    0.70      415     0  0.2500 0.0000
REMARK   3    70  2.1490 -  2.1390    0.70      424     0  0.2690 0.0000
REMARK   3    71  2.1390 -  2.1290    0.73      423     0  0.2660 0.0000
REMARK   3    72  2.1290 -  2.1190    0.69      415     0  0.2690 0.0000
REMARK   3    73  2.1190 -  2.1090    0.65      373     0  0.3020 0.0000
REMARK   3    74  2.1090 -  2.1000    0.57      335     0  0.2910 0.0000
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : NULL
REMARK   3   SOLVENT RADIUS     : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3   K_SOL              : 0.33
REMARK   3   B_SOL              : 66.98
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.16
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.29
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.40100
REMARK   3    B22 (A**2) : 0.82000
REMARK   3    B33 (A**2) : -0.42000
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.40400
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      :  0.004           NULL
REMARK   3   ANGLE     :  0.622           NULL
REMARK   3   CHIRALITY :  0.046           NULL
REMARK   3   PLANARITY :  0.002           NULL
REMARK   3   DIHEDRAL  :  9.793           NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (CHAIN A AND RESID 7:187)
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1404  12.0113   1.9266
REMARK   3    T TENSOR
REMARK   3      T11:   0.1148 T22:   0.0563
REMARK   3      T33:   0.1175 T12:   0.0085
REMARK   3      T13:   0.0032 T23:  -0.0015
REMARK   3    L TENSOR
REMARK   3      L11:   0.8244 L22:   0.8305
REMARK   3      L33:   0.4929 L12:   0.1870
REMARK   3      L13:   0.0426 L23:  -0.1246
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0357 S12:  -0.0533 S13:   0.2260
REMARK   3      S21:   0.1454 S22:   0.0107 S23:   0.1164
REMARK   3      S31:  -0.1717 S32:  -0.0181 S33:   0.0258
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (CHAIN A AND RESID 188:368)
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1267  -3.0499  -2.4732
REMARK   3    T TENSOR
REMARK   3      T11:   0.1252 T22:   0.0350
REMARK   3      T33:   0.1094 T12:  -0.0032
REMARK   3      T13:   0.0066 T23:  -0.0172
REMARK   3    L TENSOR
REMARK   3      L11:   0.7541 L22:   0.5992
REMARK   3      L33:   1.0906 L12:  -0.1292
REMARK   3      L13:   0.4830 L23:  -0.7162
REMARK   3    S TENSOR
REMARK   3      S11:   0.0409 S12:   0.0518 S13:  -0.0571
REMARK   3      S21:  -0.0579 S22:  -0.0297 S23:   0.0080
REMARK   3      S31:   0.2010 S32:   0.0277 S33:  -0.0099
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (CHAIN B AND RESID 10:129)
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1185  20.5808  33.6831
REMARK   3    T TENSOR
REMARK   3      T11:   0.7596 T22:   0.7020
REMARK   3      T33:   0.5283 T12:  -0.0817
REMARK   3      T13:   0.1832 T23:  -0.1233
REMARK   3    L TENSOR
REMARK   3      L11:   2.7205 L22:   0.6435
REMARK   3      L33:   1.4012 L12:   0.0973
REMARK   3      L13:  -2.4217 L23:  -0.3755
REMARK   3    S TENSOR
REMARK   3      S11:   0.5905 S12:  -0.1627 S13:   0.4739
REMARK   3      S21:  -0.3491 S22:   0.1334 S23:  -0.0767
REMARK   3      S31:  -0.6788 S32:   0.4941 S33:  -0.4717
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (CHAIN B AND RESID 130:373)
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6611   6.4360  25.1753
REMARK   3    T TENSOR
REMARK   3      T11:   0.0968 T22:   0.1513
REMARK   3      T33:   0.1029 T12:   0.0526
REMARK   3      T13:   0.0147 T23:  -0.0101
REMARK   3    L TENSOR
REMARK   3      L11:   1.1168 L22:   0.4999
REMARK   3      L33:   2.4430 L12:   0.0291
REMARK   3      L13:   0.2416 L23:   0.0677
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0058 S12:  -0.0947 S13:   0.0452
REMARK   3      S21:   0.0461 S22:   0.0493 S23:   0.0120
REMARK   3      S31:   0.1143 S32:   0.2030 S33:  -0.0403
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 3LWB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB057810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96411
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40957
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.05200
REMARK 200  R SYM                      (I) : 0.05200
REMARK 200   FOR THE DATA SET  : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.40600
REMARK 200  R SYM FOR SHELL            (I) : 0.40600
REMARK 200   FOR SHELL         : 2.700
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: HOMOLOGY MODEL DERIVED FROM PDB ENTRY 2I87
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION CONSISTED OF 20% PEG
REMARK 280  3350, 0.1M POTASSIUM NITRATE. 1UL OF WELL SOLUTION WAS MIXED WITH
REMARK 280  1UL PROTEIN SOLUTION (10MG/ML) AND EQUILIBRATED OVER 500UL WELL
REMARK 280  SOLUTION., PH 8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       54.15100
REMARK 290   SMTRY3   2  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: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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     MET A     1
REMARK 465     SER A     2
REMARK 465     ALA A     3
REMARK 465     ASN A     4
REMARK 465     ASP A     5
REMARK 465     ARG A     6
REMARK 465     ARG A    20
REMARK 465     SER A    21
REMARK 465     ASN A    22
REMARK 465     GLU A    23
REMARK 465     HIS A    24
REMARK 465     PRO A    63
REMARK 465     ASP A    64
REMARK 465     ALA A    65
REMARK 465     LEU A    66
REMARK 465     THR A    67
REMARK 465     ILE A    68
REMARK 465     THR A    69
REMARK 465     ASN A    70
REMARK 465     ARG A    71
REMARK 465     GLU A    72
REMARK 465     LEU A    73
REMARK 465     PRO A    74
REMARK 465     GLN A    75
REMARK 465     VAL A    76
REMARK 465     LYS A    77
REMARK 465     SER A    78
REMARK 465     GLY A    79
REMARK 465     SER A    80
REMARK 465     GLY A    81
REMARK 465     THR A    82
REMARK 465     GLU A    83
REMARK 465     LEU A    84
REMARK 465     ALA A    85
REMARK 465     LEU A    86
REMARK 465     PRO A    87
REMARK 465     ALA A    88
REMARK 465     ASP A    89
REMARK 465     PRO A    90
REMARK 465     ARG A    91
REMARK 465     ARG A    92
REMARK 465     GLY A    93
REMARK 465     GLY A    94
REMARK 465     GLN A    95
REMARK 465     LEU A    96
REMARK 465     GLY A   369
REMARK 465     VAL A   370
REMARK 465     GLY A   371
REMARK 465     LEU A   372
REMARK 465     HIS A   373
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     ALA B     3
REMARK 465     ASN B     4
REMARK 465     ASP B     5
REMARK 465     ARG B     6
REMARK 465     ARG B     7
REMARK 465     ASP B     8
REMARK 465     ARG B     9
REMARK 465     GLY B    18
REMARK 465     GLY B    19
REMARK 465     ARG B    20
REMARK 465     SER B    21
REMARK 465     ASN B    22
REMARK 465     GLU B    23
REMARK 465     ALA B    53
REMARK 465     GLY B    54
REMARK 465     SER B    55
REMARK 465     TRP B    56
REMARK 465     VAL B    57
REMARK 465     LEU B    58
REMARK 465     THR B    59
REMARK 465     ASP B    60
REMARK 465     ALA B    61
REMARK 465     ASN B    62
REMARK 465     PRO B    63
REMARK 465     ASP B    64
REMARK 465     ALA B    65
REMARK 465     LEU B    66
REMARK 465     THR B    67
REMARK 465     ILE B    68
REMARK 465     THR B    69
REMARK 465     ASN B    70
REMARK 465     ARG B    71
REMARK 465     GLU B    72
REMARK 465     LEU B    73
REMARK 465     PRO B    74
REMARK 465     GLN B    75
REMARK 465     VAL B    76
REMARK 465     LYS B    77
REMARK 465     SER B    78
REMARK 465     GLY B    79
REMARK 465     SER B    80
REMARK 465     GLY B    81
REMARK 465     THR B    82
REMARK 465     GLU B    83
REMARK 465     LEU B    84
REMARK 465     ALA B    85
REMARK 465     LEU B    86
REMARK 465     PRO B    87
REMARK 465     ALA B    88
REMARK 465     ASP B    89
REMARK 465     PRO B    90
REMARK 465     ARG B    91
REMARK 465     ARG B    92
REMARK 465     GLY B    93
REMARK 465     GLY B    94
REMARK 465     GLN B    95
REMARK 465     LEU B    96
REMARK 465     VAL B    97
REMARK 465     SER B    98
REMARK 465     LEU B    99
REMARK 465     PRO B   100
REMARK 465     PRO B   101
REMARK 465     GLY B   102
REMARK 465     ALA B   103
REMARK 465     GLY B   104
REMARK 465     GLU B   105
REMARK 465     GLY B   119
REMARK 465     PRO B   120
REMARK 465     TYR B   121
REMARK 465     GLY B   122
REMARK 465     GLU B   123
REMARK 465     ASP B   124
REMARK 465     GLY B   125
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     ARG A   7    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A   8    CG   OD1  OD2
REMARK 470     ARG A   9    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE A  26    CG1  CG2  CD1
REMARK 470     VAL A  97    CB   CG1  CG2
REMARK 470     SER A  98    CB   OG
REMARK 470     LEU A  99    CG   CD1  CD2
REMARK 470     MET A 150    CG   SD   CE
REMARK 470     HIS A 180    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 182    CG   CD   OE1  NE2
REMARK 470     GLU A 185    CG   CD   OE1  OE2
REMARK 470     VAL A 263    CG1  CG2
REMARK 470     ARG A 266    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  10    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  12    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL B  15    CG1  CG2
REMARK 470     VAL B  16    CG1  CG2
REMARK 470     HIS B  24    CG   ND1  CD2  CE1  NE2
REMARK 470     ILE B  26    CG1  CG2  CD1
REMARK 470     SER B  27    OG
REMARK 470     VAL B  29    CG1  CG2
REMARK 470     SER B  33    OG
REMARK 470     ARG B  36    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  41    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE B  46    CG1  CG2  CD1
REMARK 470     ILE B  50    CG1  CG2  CD1
REMARK 470     PRO B  52    CG   CD
REMARK 470     VAL B 106    CG1  CG2
REMARK 470     LEU B 107    CG   CD1  CD2
REMARK 470     VAL B 116    CG1  CG2
REMARK 470     LEU B 117    CG   CD1  CD2
REMARK 470     HIS B 118    CG   ND1  CD2  CE1  NE2
REMARK 470     THR B 126    OG1  CG2
REMARK 470     ILE B 127    CG1  CG2  CD1
REMARK 470     GLN B 182    CG   CD   OE1  NE2
REMARK 470     VAL B 263    CG1  CG2
REMARK 470     ARG B 264    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 266    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B 280    CG   OD1  OD2
REMARK 470     GLN B 293    CG   CD   OE1  NE2
REMARK 470     VAL B 370    CG1  CG2
REMARK 470     HIS B 373    CG   ND1  CD2  CE1  NE2
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    ASN A  62   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES
REMARK 500    PRO B  52   N   -  CA  -  CB  ANGL. DEV. =   9.8 DEGREES
REMARK 500    PRO B  52   N   -  CA  -  C   ANGL. DEV. = -21.5 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    ASP B  39      101.63    -47.37
REMARK 500    THR B  51      158.03    -44.06
REMARK 500    LEU B 107      158.85     73.79
REMARK 500    GLU B 108     -179.95     74.45
REMARK 500    SER B 109       -5.22     58.08
REMARK 500    VAL B 143      -78.39    -41.96
REMARK 500    SER B 200       74.25   -106.56
REMARK 500    SER B 201      -51.24   -147.07
REMARK 500    ALA B 261      150.93     70.46
REMARK 500    VAL B 263     -171.40    165.81
REMARK 500    ARG B 264      -70.10   -101.37
REMARK 500    ARG B 266        3.73     51.62
REMARK 500    ARG B 368      -60.83    -95.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR B   51     PRO B   52                 -135.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASN A  62        45.9      L          L   OUTSIDE RANGE
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 A 605        DISTANCE =  5.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 374
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 374
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV2981C   RELATED DB: TARGETDB
DBREF  3LWB A    1   373  UNP    P95114   DDL_MYCTU        1    373
DBREF  3LWB B    1   373  UNP    P95114   DDL_MYCTU        1    373
SEQRES   1 A  373  MET SER ALA ASN ASP ARG ARG ASP ARG ARG VAL ARG VAL
SEQRES   2 A  373  ALA VAL VAL PHE GLY GLY ARG SER ASN GLU HIS ALA ILE
SEQRES   3 A  373  SER CYS VAL SER ALA GLY SER ILE LEU ARG ASN LEU ASP
SEQRES   4 A  373  SER ARG ARG PHE ASP VAL ILE ALA VAL GLY ILE THR PRO
SEQRES   5 A  373  ALA GLY SER TRP VAL LEU THR ASP ALA ASN PRO ASP ALA
SEQRES   6 A  373  LEU THR ILE THR ASN ARG GLU LEU PRO GLN VAL LYS SER
SEQRES   7 A  373  GLY SER GLY THR GLU LEU ALA LEU PRO ALA ASP PRO ARG
SEQRES   8 A  373  ARG GLY GLY GLN LEU VAL SER LEU PRO PRO GLY ALA GLY
SEQRES   9 A  373  GLU VAL LEU GLU SER VAL ASP VAL VAL PHE PRO VAL LEU
SEQRES  10 A  373  HIS GLY PRO TYR GLY GLU ASP GLY THR ILE GLN GLY LEU
SEQRES  11 A  373  LEU GLU LEU ALA GLY VAL PRO TYR VAL GLY ALA GLY VAL
SEQRES  12 A  373  LEU ALA SER ALA VAL GLY MET ASP LYS GLU PHE THR LYS
SEQRES  13 A  373  LYS LEU LEU ALA ALA ASP GLY LEU PRO VAL GLY ALA TYR
SEQRES  14 A  373  ALA VAL LEU ARG PRO PRO ARG SER THR LEU HIS ARG GLN
SEQRES  15 A  373  GLU CYS GLU ARG LEU GLY LEU PRO VAL PHE VAL LYS PRO
SEQRES  16 A  373  ALA ARG GLY GLY SER SER ILE GLY VAL SER ARG VAL SER
SEQRES  17 A  373  SER TRP ASP GLN LEU PRO ALA ALA VAL ALA ARG ALA ARG
SEQRES  18 A  373  ARG HIS ASP PRO LYS VAL ILE VAL GLU ALA ALA ILE SER
SEQRES  19 A  373  GLY ARG GLU LEU GLU CYS GLY VAL LEU GLU MET PRO ASP
SEQRES  20 A  373  GLY THR LEU GLU ALA SER THR LEU GLY GLU ILE ARG VAL
SEQRES  21 A  373  ALA GLY VAL ARG GLY ARG GLU ASP SER PHE TYR ASP PHE
SEQRES  22 A  373  ALA THR LYS TYR LEU ASP ASP ALA ALA GLU LEU ASP VAL
SEQRES  23 A  373  PRO ALA LYS VAL ASP ASP GLN VAL ALA GLU ALA ILE ARG
SEQRES  24 A  373  GLN LEU ALA ILE ARG ALA PHE ALA ALA ILE ASP CYS ARG
SEQRES  25 A  373  GLY LEU ALA ARG VAL ASP PHE PHE LEU THR ASP ASP GLY
SEQRES  26 A  373  PRO VAL ILE ASN GLU ILE ASN THR MET PRO GLY PHE THR
SEQRES  27 A  373  THR ILE SER MET TYR PRO ARG MET TRP ALA ALA SER GLY
SEQRES  28 A  373  VAL ASP TYR PRO THR LEU LEU ALA THR MET ILE GLU THR
SEQRES  29 A  373  THR LEU ALA ARG GLY VAL GLY LEU HIS
SEQRES   1 B  373  MET SER ALA ASN ASP ARG ARG ASP ARG ARG VAL ARG VAL
SEQRES   2 B  373  ALA VAL VAL PHE GLY GLY ARG SER ASN GLU HIS ALA ILE
SEQRES   3 B  373  SER CYS VAL SER ALA GLY SER ILE LEU ARG ASN LEU ASP
SEQRES   4 B  373  SER ARG ARG PHE ASP VAL ILE ALA VAL GLY ILE THR PRO
SEQRES   5 B  373  ALA GLY SER TRP VAL LEU THR ASP ALA ASN PRO ASP ALA
SEQRES   6 B  373  LEU THR ILE THR ASN ARG GLU LEU PRO GLN VAL LYS SER
SEQRES   7 B  373  GLY SER GLY THR GLU LEU ALA LEU PRO ALA ASP PRO ARG
SEQRES   8 B  373  ARG GLY GLY GLN LEU VAL SER LEU PRO PRO GLY ALA GLY
SEQRES   9 B  373  GLU VAL LEU GLU SER VAL ASP VAL VAL PHE PRO VAL LEU
SEQRES  10 B  373  HIS GLY PRO TYR GLY GLU ASP GLY THR ILE GLN GLY LEU
SEQRES  11 B  373  LEU GLU LEU ALA GLY VAL PRO TYR VAL GLY ALA GLY VAL
SEQRES  12 B  373  LEU ALA SER ALA VAL GLY MET ASP LYS GLU PHE THR LYS
SEQRES  13 B  373  LYS LEU LEU ALA ALA ASP GLY LEU PRO VAL GLY ALA TYR
SEQRES  14 B  373  ALA VAL LEU ARG PRO PRO ARG SER THR LEU HIS ARG GLN
SEQRES  15 B  373  GLU CYS GLU ARG LEU GLY LEU PRO VAL PHE VAL LYS PRO
SEQRES  16 B  373  ALA ARG GLY GLY SER SER ILE GLY VAL SER ARG VAL SER
SEQRES  17 B  373  SER TRP ASP GLN LEU PRO ALA ALA VAL ALA ARG ALA ARG
SEQRES  18 B  373  ARG HIS ASP PRO LYS VAL ILE VAL GLU ALA ALA ILE SER
SEQRES  19 B  373  GLY ARG GLU LEU GLU CYS GLY VAL LEU GLU MET PRO ASP
SEQRES  20 B  373  GLY THR LEU GLU ALA SER THR LEU GLY GLU ILE ARG VAL
SEQRES  21 B  373  ALA GLY VAL ARG GLY ARG GLU ASP SER PHE TYR ASP PHE
SEQRES  22 B  373  ALA THR LYS TYR LEU ASP ASP ALA ALA GLU LEU ASP VAL
SEQRES  23 B  373  PRO ALA LYS VAL ASP ASP GLN VAL ALA GLU ALA ILE ARG
SEQRES  24 B  373  GLN LEU ALA ILE ARG ALA PHE ALA ALA ILE ASP CYS ARG
SEQRES  25 B  373  GLY LEU ALA ARG VAL ASP PHE PHE LEU THR ASP ASP GLY
SEQRES  26 B  373  PRO VAL ILE ASN GLU ILE ASN THR MET PRO GLY PHE THR
SEQRES  27 B  373  THR ILE SER MET TYR PRO ARG MET TRP ALA ALA SER GLY
SEQRES  28 B  373  VAL ASP TYR PRO THR LEU LEU ALA THR MET ILE GLU THR
SEQRES  29 B  373  THR LEU ALA ARG GLY VAL GLY LEU HIS
HET    NO3  A 374       4
HET    NO3  B 374       4
HETNAM     NO3 NITRATE ION
FORMUL   3  NO3    2(N O3 1-)
FORMUL   5  HOH   *383(H2 O)
HELIX    1   1 ALA A   25  LEU A   38  1                                  14
HELIX    2   2 GLY A  102  SER A  109  1                                   8
HELIX    3   3 GLY A  125  GLY A  135  1                                  11
HELIX    4   4 GLY A  142  ASP A  151  1                                  10
HELIX    5   5 ASP A  151  ASP A  162  1                                  12
HELIX    6   6 HIS A  180  GLY A  188  1                                   9
HELIX    7   7 SER A  209  ASP A  211  5                                   3
HELIX    8   8 GLN A  212  ARG A  222  1                                  11
HELIX    9   9 ASP A  272  LEU A  278  1                                   7
HELIX   10  10 ASP A  291  ILE A  309  1                                  19
HELIX   11  11 SER A  341  SER A  350  1                                  10
HELIX   12  12 ASP A  353  ARG A  368  1                                  16
HELIX   13  13 ALA B   25  LEU B   38  1                                  14
HELIX   14  14 THR B  126  LEU B  133  1                                   8
HELIX   15  15 GLY B  142  ASP B  151  1                                  10
HELIX   16  16 ASP B  151  ASP B  162  1                                  12
HELIX   17  17 HIS B  180  GLY B  188  1                                   9
HELIX   18  18 SER B  209  ASP B  211  5                                   3
HELIX   19  19 GLN B  212  ARG B  222  1                                  11
HELIX   20  20 ASP B  272  ASP B  279  1                                   8
HELIX   21  21 ASP B  291  ILE B  309  1                                  19
HELIX   22  22 SER B  341  ALA B  349  1                                   9
HELIX   23  23 ASP B  353  GLY B  369  1                                  17
SHEET    1   A 4 TRP A  56  THR A  59  0
SHEET    2   A 4 PHE A  43  ILE A  50 -1  N  GLY A  49   O  VAL A  57
SHEET    3   A 4 VAL A  11  GLY A  18  1  N  VAL A  11   O  ASP A  44
SHEET    4   A 4 VAL A 112  PRO A 115  1  O  PHE A 114   N  ALA A  14
SHEET    1   B 2 HIS A 118  GLY A 119  0
SHEET    2   B 2 GLY A 122  GLU A 123 -1  O  GLY A 122   N  GLY A 119
SHEET    1   C 4 TYR A 169  LEU A 172  0
SHEET    2   C 4 VAL A 227  ALA A 231 -1  O  VAL A 227   N  LEU A 172
SHEET    3   C 4 VAL A 191  PRO A 195 -1  N  LYS A 194   O  ILE A 228
SHEET    4   C 4 SER A 205  VAL A 207 -1  O  VAL A 207   N  VAL A 191
SHEET    1   D 4 LEU A 250  ALA A 252  0
SHEET    2   D 4 SER A 234  GLU A 244 -1  N  LEU A 243   O  GLU A 251
SHEET    3   D 4 GLY A 256  ARG A 259 -1  O  GLY A 256   N  GLU A 239
SHEET    4   D 4 GLU A 283  ASP A 285 -1  O  ASP A 285   N  GLU A 257
SHEET    1   E 4 GLU A 267  ASP A 268  0
SHEET    2   E 4 SER A 234  GLU A 244 -1  N  GLY A 235   O  GLU A 267
SHEET    3   E 4 LEU A 314  THR A 322 -1  O  PHE A 319   N  LEU A 238
SHEET    4   E 4 GLY A 325  ASN A 332 -1  O  ASN A 332   N  ARG A 316
SHEET    1   F 3 PHE B  43  VAL B  48  0
SHEET    2   F 3 VAL B  11  VAL B  16  1  N  VAL B  13   O  ASP B  44
SHEET    3   F 3 VAL B 112  PRO B 115  1  O  PHE B 114   N  ALA B  14
SHEET    1   G 4 TYR B 169  LEU B 172  0
SHEET    2   G 4 VAL B 227  ALA B 231 -1  O  VAL B 227   N  LEU B 172
SHEET    3   G 4 VAL B 191  PRO B 195 -1  N  PHE B 192   O  GLU B 230
SHEET    4   G 4 SER B 205  VAL B 207 -1  O  VAL B 207   N  VAL B 191
SHEET    1   H 4 LEU B 250  ALA B 252  0
SHEET    2   H 4 SER B 234  GLU B 244 -1  N  LEU B 243   O  GLU B 251
SHEET    3   H 4 GLY B 256  ARG B 259 -1  O  GLY B 256   N  GLU B 239
SHEET    4   H 4 GLU B 283  ASP B 285 -1  O  ASP B 285   N  GLU B 257
SHEET    1   I 4 GLU B 267  ASP B 268  0
SHEET    2   I 4 SER B 234  GLU B 244 -1  N  GLY B 235   O  GLU B 267
SHEET    3   I 4 LEU B 314  THR B 322 -1  O  PHE B 319   N  LEU B 238
SHEET    4   I 4 GLY B 325  ASN B 332 -1  O  ASN B 332   N  ARG B 316
CISPEP   1 PRO A  174    PRO A  175          0         3.69
CISPEP   2 LEU A  189    PRO A  190          0        -1.66
CISPEP   3 VAL A  286    PRO A  287          0         6.23
CISPEP   4 LEU B  107    GLU B  108          0        10.85
CISPEP   5 PRO B  174    PRO B  175          0         4.54
CISPEP   6 LEU B  189    PRO B  190          0        -0.93
CISPEP   7 VAL B  286    PRO B  287          0         1.71
CISPEP   8 GLY B  369    VAL B  370          0         0.85
SITE     1 AC1  6 ARG A 316  PRO A 335  GLY A 336  SER A 341
SITE     2 AC1  6 MET A 342  TYR A 343
SITE     1 AC2  5 ARG B 316  PRO B 335  GLY B 336  MET B 342
SITE     2 AC2  5 TYR B 343
CRYST1   51.720  108.302   69.064  90.00  99.92  90.00 P 1 21 1      4
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.019335  0.000000  0.003382        0.00000
SCALE2      0.000000  0.009233  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014699        0.00000
      
PROCHECK
Go to PROCHECK summary
 References