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PDBsum entry 3pxj

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Hydrolase PDB id
3pxj
Jmol
Contents
Protein chains
199 a.a.
187 a.a.
Waters ×138
HEADER    HYDROLASE                               10-DEC-10   3PXJ
TITLE     TANDEM IG REPEATS OF DLAR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE LAR;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: IG DOMAINS 1 AND 2 (UNP RESIDUES 32-237);
COMPND   5 SYNONYM: PROTEIN-TYROSINE-PHOSPHATE PHOSPHOHYDROLASE, DLAR;
COMPND   6 EC: 3.1.3.48;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;
SOURCE   4 ORGANISM_TAXID: 7227;
SOURCE   5 GENE: LAR, CG10443;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI 2(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32
KEYWDS    IG DOMAINS, CELL ADHESION, RECEPTOR PROTEIN TYROSINE PHOSPHATASE,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.H.BIERSMITH,S.BOUYAIN
REVDAT   3   04-MAY-11 3PXJ    1       JRNL
REVDAT   2   20-APR-11 3PXJ    1       JRNL
REVDAT   1   23-MAR-11 3PXJ    0
JRNL        AUTH   B.H.BIERSMITH,M.HAMMEL,E.R.GEISBRECHT,S.BOUYAIN
JRNL        TITL   THE IMMUNOGLOBULIN-LIKE DOMAINS 1 AND 2 OF THE PROTEIN
JRNL        TITL 2 TYROSINE PHOSPHATASE LAR ADOPT AN UNUSUAL HORSESHOE-LIKE
JRNL        TITL 3 CONFORMATION.
JRNL        REF    J.MOL.BIOL.                   V. 408   616 2011
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   21402080
JRNL        DOI    10.1016/J.JMB.2011.03.013
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.38
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0
REMARK   3   NUMBER OF REFLECTIONS             : 37084
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225
REMARK   3   R VALUE            (WORKING SET) : 0.223
REMARK   3   FREE R VALUE                     : 0.261
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970
REMARK   3   FREE R VALUE TEST SET COUNT      : 1844
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 41.3916 -  4.9533    0.94     3666   191  0.2091 0.2243
REMARK   3     2  4.9533 -  3.9326    0.98     3721   196  0.1564 0.1807
REMARK   3     3  3.9326 -  3.4357    0.98     3730   196  0.2030 0.2531
REMARK   3     4  3.4357 -  3.1217    0.98     3686   194  0.2339 0.2439
REMARK   3     5  3.1217 -  2.8980    0.96     3646   187  0.2561 0.2938
REMARK   3     6  2.8980 -  2.7272    0.94     3561   187  0.2731 0.3524
REMARK   3     7  2.7272 -  2.5906    0.93     3513   182  0.2936 0.3317
REMARK   3     8  2.5906 -  2.4779    0.89     3356   177  0.3158 0.4006
REMARK   3     9  2.4779 -  2.3825    0.87     3304   175  0.3388 0.4508
REMARK   3    10  2.3825 -  2.3003    0.82     3057   159  0.3383 0.3881
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.90
REMARK   3   SHRINKAGE RADIUS   : 0.61
REMARK   3   K_SOL              : 0.35
REMARK   3   B_SOL              : 61.03
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.910
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.23
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.29220
REMARK   3    B22 (A**2) : -7.08390
REMARK   3    B33 (A**2) : 10.37610
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.67950
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      :  0.032           6097
REMARK   3   ANGLE     :  1.657           8262
REMARK   3   CHIRALITY :  0.135            905
REMARK   3   PLANARITY :  0.014           1096
REMARK   3   DIHEDRAL  : 21.028           2306
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 8
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A AND RESID 33:134
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1008   4.7170   5.8134
REMARK   3    T TENSOR
REMARK   3      T11:   0.1177 T22:   0.4669
REMARK   3      T33:   0.2347 T12:  -0.0361
REMARK   3      T13:  -0.0781 T23:  -0.0287
REMARK   3    L TENSOR
REMARK   3      L11:   1.1013 L22:   0.1434
REMARK   3      L33:   0.3772 L12:   0.3409
REMARK   3      L13:   0.3598 L23:  -1.0945
REMARK   3    S TENSOR
REMARK   3      S11:   0.2672 S12:  -0.2074 S13:   0.2550
REMARK   3      S21:  -0.0010 S22:  -0.1310 S23:  -0.1132
REMARK   3      S31:  -0.0768 S32:  -0.0084 S33:  -0.0530
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN A AND RESID 135:230
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9639  22.8581   0.1726
REMARK   3    T TENSOR
REMARK   3      T11:   0.1213 T22:   0.4320
REMARK   3      T33:   0.2912 T12:  -0.0333
REMARK   3      T13:  -0.0606 T23:   0.0206
REMARK   3    L TENSOR
REMARK   3      L11:   0.9805 L22:   1.4264
REMARK   3      L33:   0.8569 L12:  -1.3713
REMARK   3      L13:  -0.1977 L23:   0.7154
REMARK   3    S TENSOR
REMARK   3      S11:   0.1865 S12:   0.1397 S13:   0.2308
REMARK   3      S21:   0.0171 S22:   0.1064 S23:  -0.5143
REMARK   3      S31:  -0.0288 S32:  -0.0114 S33:  -0.2456
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN B AND RESID 32:134
REMARK   3    ORIGIN FOR THE GROUP (A):  30.1378   6.8944  45.9239
REMARK   3    T TENSOR
REMARK   3      T11:   0.1055 T22:   0.0830
REMARK   3      T33:   0.1647 T12:  -0.0235
REMARK   3      T13:  -0.0273 T23:  -0.0055
REMARK   3    L TENSOR
REMARK   3      L11:   1.1881 L22:   0.9658
REMARK   3      L33:   0.9909 L12:  -1.0354
REMARK   3      L13:  -0.1794 L23:  -0.6025
REMARK   3    S TENSOR
REMARK   3      S11:   0.0666 S12:  -0.0447 S13:   0.0507
REMARK   3      S21:   0.0104 S22:  -0.0795 S23:  -0.2333
REMARK   3      S31:   0.0960 S32:   0.0375 S33:   0.0226
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN B AND RESID 135:230
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0129  24.9454  40.1993
REMARK   3    T TENSOR
REMARK   3      T11:   0.0881 T22:  -0.0944
REMARK   3      T33:   0.1738 T12:   0.0342
REMARK   3      T13:  -0.0243 T23:  -0.0540
REMARK   3    L TENSOR
REMARK   3      L11:   0.7461 L22:   1.0191
REMARK   3      L33:   0.5024 L12:  -0.9005
REMARK   3      L13:  -0.2816 L23:   0.6788
REMARK   3    S TENSOR
REMARK   3      S11:   0.1270 S12:   0.1544 S13:   0.1198
REMARK   3      S21:  -0.1214 S22:   0.1979 S23:   0.1628
REMARK   3      S31:  -0.0197 S32:  -0.1926 S33:  -0.2593
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN C AND RESID 33:131
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1639  22.8791  45.6445
REMARK   3    T TENSOR
REMARK   3      T11:   0.1683 T22:   0.0937
REMARK   3      T33:   0.4886 T12:  -0.0070
REMARK   3      T13:  -0.1454 T23:   0.0077
REMARK   3    L TENSOR
REMARK   3      L11:   0.1363 L22:   0.2682
REMARK   3      L33:   0.6453 L12:  -0.2077
REMARK   3      L13:  -0.1619 L23:   0.0838
REMARK   3    S TENSOR
REMARK   3      S11:   0.0977 S12:   0.0134 S13:   0.2894
REMARK   3      S21:  -0.1909 S22:  -0.1216 S23:   0.4390
REMARK   3      S31:  -0.1841 S32:  -0.0134 S33:   0.0392
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: CHAIN C AND RESID 138:230
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6851   4.4413  40.4479
REMARK   3    T TENSOR
REMARK   3      T11:   0.1208 T22:   0.0405
REMARK   3      T33:   0.3827 T12:   0.0082
REMARK   3      T13:  -0.1247 T23:   0.0457
REMARK   3    L TENSOR
REMARK   3      L11:   1.6248 L22:   0.2632
REMARK   3      L33:   0.4654 L12:  -0.2980
REMARK   3      L13:   0.4399 L23:  -0.1548
REMARK   3    S TENSOR
REMARK   3      S11:   0.0871 S12:   0.0423 S13:   0.1486
REMARK   3      S21:  -0.0555 S22:  -0.0309 S23:   0.2467
REMARK   3      S31:   0.1172 S32:   0.0448 S33:  -0.0913
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: CHAIN D AND RESID 134:231
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1595   2.9022  -0.3233
REMARK   3    T TENSOR
REMARK   3      T11:   0.1368 T22:   0.4205
REMARK   3      T33:   0.2862 T12:   0.0077
REMARK   3      T13:  -0.1375 T23:  -0.0394
REMARK   3    L TENSOR
REMARK   3      L11:   1.3780 L22:   0.8522
REMARK   3      L33:   0.3778 L12:  -1.2531
REMARK   3      L13:   1.0241 L23:  -0.4005
REMARK   3    S TENSOR
REMARK   3      S11:   0.1422 S12:  -0.0512 S13:   0.0906
REMARK   3      S21:  -0.0336 S22:  -0.0268 S23:   0.1663
REMARK   3      S31:   0.0581 S32:   0.2331 S33:  -0.0554
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: CHAIN E
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3744  13.4284  24.7663
REMARK   3    T TENSOR
REMARK   3      T11:   0.1602 T22:   0.3039
REMARK   3      T33:   0.1025 T12:  -0.0253
REMARK   3      T13:   0.0589 T23:   0.0170
REMARK   3    L TENSOR
REMARK   3      L11:  -0.0009 L22:   0.0968
REMARK   3      L33:  -0.6801 L12:  -0.0869
REMARK   3      L13:   0.1668 L23:  -0.1313
REMARK   3    S TENSOR
REMARK   3      S11:   0.0319 S12:   0.1026 S13:  -0.0062
REMARK   3      S21:   0.0203 S22:  -0.0253 S23:   0.0116
REMARK   3      S31:   0.0290 S32:   0.0235 S33:  -0.0011
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 3PXJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-10.
REMARK 100 THE RCSB ID CODE IS RCSB062934.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97242
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK MONOCHROMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39287
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
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     (%) : 98.7
REMARK 200  DATA REDUNDANCY                : 2.700
REMARK 200  R MERGE                    (I) : 0.11700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.41500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3PXH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM IMIDAZOLE PH 7.0, 10 MM AMMONIUM
REMARK 280  SULFATE, 20% (W/V) PEG 2000 MME, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  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       38.75650
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: C
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: 4
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A    28
REMARK 465     PRO A    29
REMARK 465     GLY A    30
REMARK 465     SER A    31
REMARK 465     ARG A   231
REMARK 465     VAL A   232
REMARK 465     PRO A   233
REMARK 465     PRO A   234
REMARK 465     THR A   235
REMARK 465     PHE A   236
REMARK 465     SER A   237
REMARK 465     GLY B    28
REMARK 465     PRO B    29
REMARK 465     GLY B    30
REMARK 465     SER B    31
REMARK 465     ARG B   231
REMARK 465     VAL B   232
REMARK 465     PRO B   233
REMARK 465     PRO B   234
REMARK 465     THR B   235
REMARK 465     PHE B   236
REMARK 465     SER B   237
REMARK 465     GLY C    28
REMARK 465     PRO C    29
REMARK 465     GLY C    30
REMARK 465     SER C    31
REMARK 465     ALA C    32
REMARK 465     SER C    77
REMARK 465     GLY C    78
REMARK 465     THR C    79
REMARK 465     GLN C    80
REMARK 465     ASN C   115
REMARK 465     GLY C   116
REMARK 465     VAL C   117
REMARK 465     GLY C   118
REMARK 465     ASP C   119
REMARK 465     GLY C   132
REMARK 465     ASP C   133
REMARK 465     ARG C   231
REMARK 465     VAL C   232
REMARK 465     PRO C   233
REMARK 465     PRO C   234
REMARK 465     THR C   235
REMARK 465     PHE C   236
REMARK 465     SER C   237
REMARK 465     GLY D    28
REMARK 465     PRO D    29
REMARK 465     GLY D    30
REMARK 465     SER D    31
REMARK 465     ALA D    32
REMARK 465     THR D    79
REMARK 465     GLN D    80
REMARK 465     GLY D   132
REMARK 465     ASP D   133
REMARK 465     ARG D   231
REMARK 465     VAL D   232
REMARK 465     PRO D   233
REMARK 465     PRO D   234
REMARK 465     THR D   235
REMARK 465     PHE D   236
REMARK 465     SER D   237
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     GLU C 114    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS B 111   CB    CYS B 111   SG     -0.097
REMARK 500    GLU B 114   C     ASN B 115   N       0.160
REMARK 500    GLU D 208   C     CYS D 209   N       0.214
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    CYS A 161   CA  -  CB  -  SG  ANGL. DEV. =   9.3 DEGREES
REMARK 500    PRO B  89   C   -  N   -  CD  ANGL. DEV. = -19.4 DEGREES
REMARK 500    GLU B 114   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES
REMARK 500    ASN B 115   C   -  N   -  CA  ANGL. DEV. = -18.0 DEGREES
REMARK 500    CYS B 209   CA  -  CB  -  SG  ANGL. DEV. =   9.2 DEGREES
REMARK 500    CYS C 111   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES
REMARK 500    PRO D 146   C   -  N   -  CD  ANGL. DEV. = -15.1 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    LYS A 190      -89.06    -91.03
REMARK 500    ASP A 191       63.71   -111.23
REMARK 500    VAL C 229      170.72    -55.08
REMARK 500    THR D 143      -79.97    -35.22
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 B  96         0.18    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PX4   RELATED DB: PDB
DBREF  3PXJ A   32   237  UNP    P16621   LAR_DROME       32    237
DBREF  3PXJ B   32   237  UNP    P16621   LAR_DROME       32    237
DBREF  3PXJ C   32   237  UNP    P16621   LAR_DROME       32    237
DBREF  3PXJ D   32   237  UNP    P16621   LAR_DROME       32    237
SEQADV 3PXJ GLY A   28  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ PRO A   29  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY A   30  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ SER A   31  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY B   28  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ PRO B   29  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY B   30  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ SER B   31  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY C   28  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ PRO C   29  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY C   30  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ SER C   31  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY D   28  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ PRO D   29  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ GLY D   30  UNP  P16621              EXPRESSION TAG
SEQADV 3PXJ SER D   31  UNP  P16621              EXPRESSION TAG
SEQRES   1 A  210  GLY PRO GLY SER ALA ALA HIS PRO PRO GLU ILE ILE ARG
SEQRES   2 A  210  LYS PRO GLN ASN GLN GLY VAL ARG VAL GLY GLY VAL ALA
SEQRES   3 A  210  SER PHE TYR CYS ALA ALA ARG GLY ASP PRO PRO PRO SER
SEQRES   4 A  210  ILE VAL TRP ARG LYS ASN GLY LYS LYS VAL SER GLY THR
SEQRES   5 A  210  GLN SER ARG TYR THR VAL LEU GLU GLN PRO GLY GLY ILE
SEQRES   6 A  210  SER ILE LEU ARG ILE GLU PRO VAL ARG ALA GLY ARG ASP
SEQRES   7 A  210  ASP ALA PRO TYR GLU CYS VAL ALA GLU ASN GLY VAL GLY
SEQRES   8 A  210  ASP ALA VAL SER ALA ASP ALA THR LEU THR ILE TYR GLU
SEQRES   9 A  210  GLY ASP LYS THR PRO ALA GLY PHE PRO VAL ILE THR GLN
SEQRES  10 A  210  GLY PRO GLY THR ARG VAL ILE GLU VAL GLY HIS THR VAL
SEQRES  11 A  210  LEU MET THR CYS LYS ALA ILE GLY ASN PRO THR PRO ASN
SEQRES  12 A  210  ILE TYR TRP ILE LYS ASN GLN THR LYS VAL ASP MET SER
SEQRES  13 A  210  ASN PRO ARG TYR SER LEU LYS ASP GLY PHE LEU GLN ILE
SEQRES  14 A  210  GLU ASN SER ARG GLU GLU ASP GLN GLY LYS TYR GLU CYS
SEQRES  15 A  210  VAL ALA GLU ASN SER MET GLY THR GLU HIS SER LYS ALA
SEQRES  16 A  210  THR ASN LEU TYR VAL LYS VAL ARG ARG VAL PRO PRO THR
SEQRES  17 A  210  PHE SER
SEQRES   1 B  210  GLY PRO GLY SER ALA ALA HIS PRO PRO GLU ILE ILE ARG
SEQRES   2 B  210  LYS PRO GLN ASN GLN GLY VAL ARG VAL GLY GLY VAL ALA
SEQRES   3 B  210  SER PHE TYR CYS ALA ALA ARG GLY ASP PRO PRO PRO SER
SEQRES   4 B  210  ILE VAL TRP ARG LYS ASN GLY LYS LYS VAL SER GLY THR
SEQRES   5 B  210  GLN SER ARG TYR THR VAL LEU GLU GLN PRO GLY GLY ILE
SEQRES   6 B  210  SER ILE LEU ARG ILE GLU PRO VAL ARG ALA GLY ARG ASP
SEQRES   7 B  210  ASP ALA PRO TYR GLU CYS VAL ALA GLU ASN GLY VAL GLY
SEQRES   8 B  210  ASP ALA VAL SER ALA ASP ALA THR LEU THR ILE TYR GLU
SEQRES   9 B  210  GLY ASP LYS THR PRO ALA GLY PHE PRO VAL ILE THR GLN
SEQRES  10 B  210  GLY PRO GLY THR ARG VAL ILE GLU VAL GLY HIS THR VAL
SEQRES  11 B  210  LEU MET THR CYS LYS ALA ILE GLY ASN PRO THR PRO ASN
SEQRES  12 B  210  ILE TYR TRP ILE LYS ASN GLN THR LYS VAL ASP MET SER
SEQRES  13 B  210  ASN PRO ARG TYR SER LEU LYS ASP GLY PHE LEU GLN ILE
SEQRES  14 B  210  GLU ASN SER ARG GLU GLU ASP GLN GLY LYS TYR GLU CYS
SEQRES  15 B  210  VAL ALA GLU ASN SER MET GLY THR GLU HIS SER LYS ALA
SEQRES  16 B  210  THR ASN LEU TYR VAL LYS VAL ARG ARG VAL PRO PRO THR
SEQRES  17 B  210  PHE SER
SEQRES   1 C  210  GLY PRO GLY SER ALA ALA HIS PRO PRO GLU ILE ILE ARG
SEQRES   2 C  210  LYS PRO GLN ASN GLN GLY VAL ARG VAL GLY GLY VAL ALA
SEQRES   3 C  210  SER PHE TYR CYS ALA ALA ARG GLY ASP PRO PRO PRO SER
SEQRES   4 C  210  ILE VAL TRP ARG LYS ASN GLY LYS LYS VAL SER GLY THR
SEQRES   5 C  210  GLN SER ARG TYR THR VAL LEU GLU GLN PRO GLY GLY ILE
SEQRES   6 C  210  SER ILE LEU ARG ILE GLU PRO VAL ARG ALA GLY ARG ASP
SEQRES   7 C  210  ASP ALA PRO TYR GLU CYS VAL ALA GLU ASN GLY VAL GLY
SEQRES   8 C  210  ASP ALA VAL SER ALA ASP ALA THR LEU THR ILE TYR GLU
SEQRES   9 C  210  GLY ASP LYS THR PRO ALA GLY PHE PRO VAL ILE THR GLN
SEQRES  10 C  210  GLY PRO GLY THR ARG VAL ILE GLU VAL GLY HIS THR VAL
SEQRES  11 C  210  LEU MET THR CYS LYS ALA ILE GLY ASN PRO THR PRO ASN
SEQRES  12 C  210  ILE TYR TRP ILE LYS ASN GLN THR LYS VAL ASP MET SER
SEQRES  13 C  210  ASN PRO ARG TYR SER LEU LYS ASP GLY PHE LEU GLN ILE
SEQRES  14 C  210  GLU ASN SER ARG GLU GLU ASP GLN GLY LYS TYR GLU CYS
SEQRES  15 C  210  VAL ALA GLU ASN SER MET GLY THR GLU HIS SER LYS ALA
SEQRES  16 C  210  THR ASN LEU TYR VAL LYS VAL ARG ARG VAL PRO PRO THR
SEQRES  17 C  210  PHE SER
SEQRES   1 D  210  GLY PRO GLY SER ALA ALA HIS PRO PRO GLU ILE ILE ARG
SEQRES   2 D  210  LYS PRO GLN ASN GLN GLY VAL ARG VAL GLY GLY VAL ALA
SEQRES   3 D  210  SER PHE TYR CYS ALA ALA ARG GLY ASP PRO PRO PRO SER
SEQRES   4 D  210  ILE VAL TRP ARG LYS ASN GLY LYS LYS VAL SER GLY THR
SEQRES   5 D  210  GLN SER ARG TYR THR VAL LEU GLU GLN PRO GLY GLY ILE
SEQRES   6 D  210  SER ILE LEU ARG ILE GLU PRO VAL ARG ALA GLY ARG ASP
SEQRES   7 D  210  ASP ALA PRO TYR GLU CYS VAL ALA GLU ASN GLY VAL GLY
SEQRES   8 D  210  ASP ALA VAL SER ALA ASP ALA THR LEU THR ILE TYR GLU
SEQRES   9 D  210  GLY ASP LYS THR PRO ALA GLY PHE PRO VAL ILE THR GLN
SEQRES  10 D  210  GLY PRO GLY THR ARG VAL ILE GLU VAL GLY HIS THR VAL
SEQRES  11 D  210  LEU MET THR CYS LYS ALA ILE GLY ASN PRO THR PRO ASN
SEQRES  12 D  210  ILE TYR TRP ILE LYS ASN GLN THR LYS VAL ASP MET SER
SEQRES  13 D  210  ASN PRO ARG TYR SER LEU LYS ASP GLY PHE LEU GLN ILE
SEQRES  14 D  210  GLU ASN SER ARG GLU GLU ASP GLN GLY LYS TYR GLU CYS
SEQRES  15 D  210  VAL ALA GLU ASN SER MET GLY THR GLU HIS SER LYS ALA
SEQRES  16 D  210  THR ASN LEU TYR VAL LYS VAL ARG ARG VAL PRO PRO THR
SEQRES  17 D  210  PHE SER
FORMUL   5  HOH   *138(H2 O)
HELIX    1   1 ARG A  200  GLN A  204  5                                   5
HELIX    2   2 ARG B  200  GLN B  204  5                                   5
HELIX    3   3 ARG C  200  GLN C  204  5                                   5
HELIX    4   4 ARG D  200  GLN D  204  5                                   5
SHEET    1   A 4 HIS A  34  ARG A  40  0
SHEET    2   A 4 ALA A  53  ASP A  62 -1  O  ARG A  60   N  GLU A  37
SHEET    3   A 4 ILE A  92  ILE A  97 -1  O  ILE A  97   N  ALA A  53
SHEET    4   A 4 TYR A  83  GLN A  88 -1  N  LEU A  86   O  ILE A  94
SHEET    1   B 5 GLN A  45  ARG A  48  0
SHEET    2   B 5 VAL A 121  TYR A 130  1  O  THR A 128   N  GLN A  45
SHEET    3   B 5 PRO A 108  GLU A 114 -1  N  CYS A 111   O  ALA A 123
SHEET    4   B 5 SER A  66  LYS A  71 -1  N  VAL A  68   O  VAL A 112
SHEET    5   B 5 LYS A  74  LYS A  75 -1  O  LYS A  74   N  LYS A  71
SHEET    1   C 2 VAL A 141  GLN A 144  0
SHEET    2   C 2 LYS A 162  ILE A 164 -1  O  LYS A 162   N  GLN A 144
SHEET    1   D 5 ARG A 149  GLU A 152  0
SHEET    2   D 5 THR A 223  LYS A 228  1  O  TYR A 226   N  ILE A 151
SHEET    3   D 5 GLY A 205  GLU A 212 -1  N  TYR A 207   O  THR A 223
SHEET    4   D 5 ASN A 170  LYS A 175 -1  N  TYR A 172   O  VAL A 210
SHEET    5   D 5 THR A 178  LYS A 179 -1  O  THR A 178   N  LYS A 175
SHEET    1   E 4 ARG A 149  GLU A 152  0
SHEET    2   E 4 THR A 223  LYS A 228  1  O  TYR A 226   N  ILE A 151
SHEET    3   E 4 GLY A 205  GLU A 212 -1  N  TYR A 207   O  THR A 223
SHEET    4   E 4 THR A 217  HIS A 219 -1  O  GLU A 218   N  ALA A 211
SHEET    1   F 3 VAL A 157  MET A 159  0
SHEET    2   F 3 LEU A 194  ILE A 196 -1  O  LEU A 194   N  MET A 159
SHEET    3   F 3 TYR A 187  LEU A 189 -1  N  SER A 188   O  GLN A 195
SHEET    1   G 4 HIS B  34  ARG B  40  0
SHEET    2   G 4 ALA B  53  ASP B  62 -1  O  ARG B  60   N  GLU B  37
SHEET    3   G 4 ILE B  92  ILE B  97 -1  O  ILE B  97   N  ALA B  53
SHEET    4   G 4 TYR B  83  GLN B  88 -1  N  THR B  84   O  ARG B  96
SHEET    1   H 5 GLN B  45  ARG B  48  0
SHEET    2   H 5 VAL B 121  TYR B 130  1  O  TYR B 130   N  VAL B  47
SHEET    3   H 5 PRO B 108  GLU B 114 -1  N  CYS B 111   O  ALA B 123
SHEET    4   H 5 SER B  66  LYS B  71 -1  N  VAL B  68   O  VAL B 112
SHEET    5   H 5 LYS B  74  LYS B  75 -1  O  LYS B  74   N  LYS B  71
SHEET    1   I 2 VAL B 141  GLN B 144  0
SHEET    2   I 2 LYS B 162  ILE B 164 -1  O  LYS B 162   N  GLN B 144
SHEET    1   J 5 ARG B 149  GLU B 152  0
SHEET    2   J 5 THR B 223  LYS B 228  1  O  LYS B 228   N  ILE B 151
SHEET    3   J 5 GLY B 205  GLU B 212 -1  N  TYR B 207   O  THR B 223
SHEET    4   J 5 ASN B 170  LYS B 175 -1  N  ASN B 170   O  GLU B 212
SHEET    5   J 5 THR B 178  LYS B 179 -1  O  THR B 178   N  LYS B 175
SHEET    1   K 4 ARG B 149  GLU B 152  0
SHEET    2   K 4 THR B 223  LYS B 228  1  O  LYS B 228   N  ILE B 151
SHEET    3   K 4 GLY B 205  GLU B 212 -1  N  TYR B 207   O  THR B 223
SHEET    4   K 4 THR B 217  HIS B 219 -1  O  GLU B 218   N  ALA B 211
SHEET    1   L 3 VAL B 157  MET B 159  0
SHEET    2   L 3 PHE B 193  ILE B 196 -1  O  LEU B 194   N  MET B 159
SHEET    3   L 3 TYR B 187  LYS B 190 -1  N  SER B 188   O  GLN B 195
SHEET    1   M 4 HIS C  34  ARG C  40  0
SHEET    2   M 4 ALA C  53  ASP C  62 -1  O  ARG C  60   N  GLU C  37
SHEET    3   M 4 ILE C  92  ILE C  97 -1  O  ILE C  97   N  ALA C  53
SHEET    4   M 4 TYR C  83  LEU C  86 -1  N  LEU C  86   O  ILE C  94
SHEET    1   N 5 GLN C  45  ARG C  48  0
SHEET    2   N 5 VAL C 121  TYR C 130  1  O  TYR C 130   N  VAL C  47
SHEET    3   N 5 PRO C 108  GLU C 114 -1  N  TYR C 109   O  ALA C 125
SHEET    4   N 5 SER C  66  LYS C  71 -1  N  ARG C  70   O  GLU C 110
SHEET    5   N 5 LYS C  74  LYS C  75 -1  O  LYS C  74   N  LYS C  71
SHEET    1   O 2 VAL C 141  GLN C 144  0
SHEET    2   O 2 LYS C 162  ILE C 164 -1  O  LYS C 162   N  GLN C 144
SHEET    1   P 5 ARG C 149  GLU C 152  0
SHEET    2   P 5 THR C 223  LYS C 228  1  O  LYS C 228   N  ILE C 151
SHEET    3   P 5 GLY C 205  GLU C 212 -1  N  TYR C 207   O  THR C 223
SHEET    4   P 5 ASN C 170  LYS C 175 -1  N  TYR C 172   O  VAL C 210
SHEET    5   P 5 THR C 178  LYS C 179 -1  O  THR C 178   N  LYS C 175
SHEET    1   Q 4 ARG C 149  GLU C 152  0
SHEET    2   Q 4 THR C 223  LYS C 228  1  O  LYS C 228   N  ILE C 151
SHEET    3   Q 4 GLY C 205  GLU C 212 -1  N  TYR C 207   O  THR C 223
SHEET    4   Q 4 THR C 217  HIS C 219 -1  O  GLU C 218   N  ALA C 211
SHEET    1   R 3 VAL C 157  MET C 159  0
SHEET    2   R 3 PHE C 193  ILE C 196 -1  O  ILE C 196   N  VAL C 157
SHEET    3   R 3 TYR C 187  LYS C 190 -1  N  SER C 188   O  GLN C 195
SHEET    1   S 4 GLU D  37  ARG D  40  0
SHEET    2   S 4 ALA D  53  ARG D  60 -1  O  ARG D  60   N  GLU D  37
SHEET    3   S 4 ILE D  92  ILE D  97 -1  O  ILE D  97   N  ALA D  53
SHEET    4   S 4 TYR D  83  GLU D  87 -1  N  LEU D  86   O  ILE D  94
SHEET    1   T 5 GLN D  45  ARG D  48  0
SHEET    2   T 5 VAL D 121  TYR D 130  1  O  THR D 128   N  VAL D  47
SHEET    3   T 5 PRO D 108  GLU D 114 -1  N  TYR D 109   O  ALA D 125
SHEET    4   T 5 SER D  66  LYS D  71 -1  N  ARG D  70   O  GLU D 110
SHEET    5   T 5 LYS D  74  LYS D  75 -1  O  LYS D  74   N  LYS D  71
SHEET    1   U 2 VAL D 141  GLN D 144  0
SHEET    2   U 2 LYS D 162  ILE D 164 -1  O  ILE D 164   N  VAL D 141
SHEET    1   V 5 ARG D 149  GLU D 152  0
SHEET    2   V 5 THR D 223  LYS D 228  1  O  LYS D 228   N  ILE D 151
SHEET    3   V 5 GLY D 205  GLU D 212 -1  N  TYR D 207   O  THR D 223
SHEET    4   V 5 ASN D 170  LYS D 175 -1  N  ILE D 174   O  GLU D 208
SHEET    5   V 5 THR D 178  LYS D 179 -1  O  THR D 178   N  LYS D 175
SHEET    1   W 4 ARG D 149  GLU D 152  0
SHEET    2   W 4 THR D 223  LYS D 228  1  O  LYS D 228   N  ILE D 151
SHEET    3   W 4 GLY D 205  GLU D 212 -1  N  TYR D 207   O  THR D 223
SHEET    4   W 4 THR D 217  HIS D 219 -1  O  GLU D 218   N  ALA D 211
SHEET    1   X 3 VAL D 157  MET D 159  0
SHEET    2   X 3 PHE D 193  ILE D 196 -1  O  ILE D 196   N  VAL D 157
SHEET    3   X 3 TYR D 187  LYS D 190 -1  N  SER D 188   O  GLN D 195
SSBOND   1 CYS A   57    CYS A  111                          1555   1555  2.25
SSBOND   2 CYS A  161    CYS A  209                          1555   1555  2.10
SSBOND   3 CYS B   57    CYS B  111                          1555   1555  2.21
SSBOND   4 CYS B  161    CYS B  209                          1555   1555  2.17
SSBOND   5 CYS C   57    CYS C  111                          1555   1555  2.28
SSBOND   6 CYS C  161    CYS C  209                          1555   1555  2.32
SSBOND   7 CYS D   57    CYS D  111                          1555   1555  2.22
SSBOND   8 CYS D  161    CYS D  209                          1555   1555  2.20
CISPEP   1 ASP A   62    PRO A   63          0        -7.88
CISPEP   2 GLU A   98    PRO A   99          0        -7.73
CISPEP   3 ASN A  166    PRO A  167          0         5.41
CISPEP   4 ASP B   62    PRO B   63          0        -2.12
CISPEP   5 GLU B   98    PRO B   99          0       -11.45
CISPEP   6 ASN B  166    PRO B  167          0         4.84
CISPEP   7 ASP C   62    PRO C   63          0         6.91
CISPEP   8 GLU C   98    PRO C   99          0       -12.57
CISPEP   9 ASN C  166    PRO C  167          0         4.74
CISPEP  10 ASP D   62    PRO D   63          0        -1.39
CISPEP  11 GLU D   98    PRO D   99          0       -14.24
CISPEP  12 ASN D  166    PRO D  167          0         4.86
CRYST1   72.957   77.513   81.726  90.00 101.08  90.00 P 1 21 1      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      0.013707  0.000000  0.002683        0.00000
SCALE2      0.000000  0.012901  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012468        0.00000
      
PROCHECK
Go to PROCHECK summary
 References