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PDBsum entry 4egj

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Ligase PDB id
4egj
Jmol
Contents
Protein chains
285 a.a.
246 a.a.
Waters ×358
HEADER    LIGASE                                  31-MAR-12   4EGJ
TITLE     CRYSTAL STRUCTURE OF D-ALANINE-D-ALANINE LIGASE FROM BURKHOLDERIA
TITLE    2 XENOVORANS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;
COMPND   5 EC: 6.3.2.4;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE   3 ORGANISM_TAXID: 266265;
SOURCE   4 STRAIN: LB400;
SOURCE   5 GENE: BXENO_A3907, BXE_A0488, DDL;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS    SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS   2 INFECTIOUS DISEASE, D-ALANINE-D-ALANINE LIGASE, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    SSGCID,SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
AUTHOR   2 (SSGCID)
REVDAT   2   30-OCT-13 4EGJ    1       JRNL
REVDAT   1   18-JUL-12 4EGJ    0
JRNL        AUTH   L.BAUGH,L.A.GALLAGHER,R.PATRAPUVICH,M.C.CLIFTON,
JRNL        AUTH 2 A.S.GARDBERG,T.E.EDWARDS,B.ARMOUR,D.W.BEGLEY,S.H.DIETERICH,
JRNL        AUTH 3 D.M.DRANOW,J.ABENDROTH,J.W.FAIRMAN,D.FOX,B.L.STAKER,I.PHAN,
JRNL        AUTH 4 A.GILLESPIE,R.CHOI,S.NAKAZAWA-HEWITT,M.T.NGUYEN,A.NAPULI,
JRNL        AUTH 5 L.BARRETT,G.W.BUCHKO,R.STACY,P.J.MYLER,L.J.STEWART,C.MANOIL,
JRNL        AUTH 6 W.C.VAN VOORHIS
JRNL        TITL   COMBINING FUNCTIONAL AND STRUCTURAL GENOMICS TO SAMPLE THE
JRNL        TITL 2 ESSENTIAL BURKHOLDERIA STRUCTOME.
JRNL        REF    PLOS ONE                      V.   8 53851 2013
JRNL        REFN                   ESSN 1932-6203
JRNL        PMID   23382856
JRNL        DOI    10.1371/JOURNAL.PONE.0053851
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.6.0117
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8
REMARK   3   NUMBER OF REFLECTIONS             : 59384
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.260
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3006
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4111
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.25
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3320
REMARK   3   BIN FREE R VALUE SET COUNT          : 255
REMARK   3   BIN FREE R VALUE                    : 0.3820
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8047
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 358
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 36.88
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.45000
REMARK   3    B22 (A**2) : 0.45000
REMARK   3    B33 (A**2) : -0.90000
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  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.322
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.237
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.166
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.316
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8230 ; 0.015 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A):  5445 ; 0.008 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11205 ; 1.698 ; 1.982
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13270 ; 1.473 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1095 ; 5.940 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   331 ;32.944 ;23.686
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1211 ;13.747 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;19.567 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1285 ; 0.095 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9403 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  1670 ; 0.006 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 6
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           0     A      4       A     311      0
REMARK   3           0     B      4       B     311      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : A C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           0     A      4       A     311      0
REMARK   3           0     C      4       C     311      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : A D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           0     A      4       A     311      0
REMARK   3           0     D      4       D     311      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : B C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           0     B      4       B     311      0
REMARK   3           0     C      4       C     311      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 5
REMARK   3     CHAIN NAMES                    : B D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           0     B      4       B     311      0
REMARK   3           0     D      4       D     311      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 6
REMARK   3     CHAIN NAMES                    : C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           0     C      4       C     312      0
REMARK   3           0     D      4       D     312      0
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     4        A   311
REMARK   3    RESIDUE RANGE :   A   401        A   513
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1440  59.0040   3.4770
REMARK   3    T TENSOR
REMARK   3      T11:   0.2470 T22:   0.1857
REMARK   3      T33:   0.0333 T12:  -0.0321
REMARK   3      T13:   0.0445 T23:   0.0408
REMARK   3    L TENSOR
REMARK   3      L11:   0.6211 L22:   1.2909
REMARK   3      L33:   0.7487 L12:  -0.4647
REMARK   3      L13:   0.1883 L23:  -0.4197
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0344 S12:   0.0702 S13:  -0.0492
REMARK   3      S21:   0.1383 S22:  -0.0204 S23:   0.0405
REMARK   3      S31:   0.0200 S32:   0.0188 S33:   0.0548
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     4        B   311
REMARK   3    RESIDUE RANGE :   B   401        B   498
REMARK   3    ORIGIN FOR THE GROUP (A):  16.4040  58.4920 115.0980
REMARK   3    T TENSOR
REMARK   3      T11:   0.2251 T22:   0.1952
REMARK   3      T33:   0.0204 T12:  -0.0330
REMARK   3      T13:   0.0332 T23:   0.0312
REMARK   3    L TENSOR
REMARK   3      L11:   0.7679 L22:   1.6402
REMARK   3      L33:   0.8753 L12:  -0.7561
REMARK   3      L13:  -0.1295 L23:  -0.0844
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0225 S12:   0.0135 S13:  -0.0758
REMARK   3      S21:   0.1067 S22:  -0.0275 S23:   0.0798
REMARK   3      S31:   0.0119 S32:   0.0068 S33:   0.0500
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     4        C   312
REMARK   3    RESIDUE RANGE :   C   401        C   469
REMARK   3    ORIGIN FOR THE GROUP (A):  68.2510  50.9640  32.9030
REMARK   3    T TENSOR
REMARK   3      T11:   0.3192 T22:   0.1540
REMARK   3      T33:   0.0221 T12:   0.0677
REMARK   3      T13:   0.0549 T23:  -0.0222
REMARK   3    L TENSOR
REMARK   3      L11:   1.2716 L22:   0.9167
REMARK   3      L33:   1.4681 L12:   0.6405
REMARK   3      L13:   0.1437 L23:   0.3652
REMARK   3    S TENSOR
REMARK   3      S11:   0.0013 S12:  -0.0789 S13:  -0.0404
REMARK   3      S21:  -0.0454 S22:  -0.0276 S23:  -0.0230
REMARK   3      S31:  -0.0205 S32:   0.0351 S33:   0.0264
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 2
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D     3        D   312
REMARK   3    RESIDUE RANGE :   D   401        D   478
REMARK   3    ORIGIN FOR THE GROUP (A):  67.3230  52.3800 143.8740
REMARK   3    T TENSOR
REMARK   3      T11:   0.2744 T22:   0.1561
REMARK   3      T33:   0.0184 T12:   0.0357
REMARK   3      T13:   0.0456 T23:  -0.0249
REMARK   3    L TENSOR
REMARK   3      L11:   0.9457 L22:   0.8710
REMARK   3      L33:   1.1244 L12:   0.7332
REMARK   3      L13:   0.1221 L23:   0.4045
REMARK   3    S TENSOR
REMARK   3      S11:   0.0264 S12:  -0.0558 S13:  -0.0097
REMARK   3      S21:  -0.0625 S22:  -0.1012 S23:   0.0129
REMARK   3      S31:   0.0699 S32:  -0.0047 S33:   0.0747
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED
REMARK   4
REMARK   4 4EGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071589.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-FEB-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : RIGAKU VARIMAX HF
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59426
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.1100
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) : 2.36
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.47800
REMARK 200  R SYM FOR SHELL            (I) : 0.47800
REMARK 200   FOR SHELL         : 2.090
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 3EG0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: QIAGEN JCSG CORE1 SCREEN D5: 20% PEG
REMARK 280  3350, 200MM LICL; BUXEA.00119.A.A1 PS01358 AT 23.2MG/ML, PH 7.5,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y,X,Z+3/4
REMARK 290       4555   Y,-X,Z+1/4
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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.37000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      168.55500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       56.18500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 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 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 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 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       78.93000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -56.18500
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       78.93000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -56.18500
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   -20
REMARK 465     ALA A   -19
REMARK 465     HIS A   -18
REMARK 465     HIS A   -17
REMARK 465     HIS A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     MET A   -12
REMARK 465     GLY A   -11
REMARK 465     THR A   -10
REMARK 465     LEU A    -9
REMARK 465     GLU A    -8
REMARK 465     ALA A    -7
REMARK 465     GLN A    -6
REMARK 465     THR A    -5
REMARK 465     GLN A    -4
REMARK 465     GLY A    -3
REMARK 465     PRO A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     SER A     2
REMARK 465     SER A     3
REMARK 465     GLU A   152
REMARK 465     GLY A   153
REMARK 465     SER A   154
REMARK 465     SER A   155
REMARK 465     VAL A   156
REMARK 465     ALA A   157
REMARK 465     VAL A   158
REMARK 465     ALA A   211
REMARK 465     GLY A   212
REMARK 465     GLU A   213
REMARK 465     PHE A   214
REMARK 465     TYR A   215
REMARK 465     ASP A   216
REMARK 465     TYR A   217
REMARK 465     HIS A   218
REMARK 465     ALA A   219
REMARK 465     LYS A   220
REMARK 465     TYR A   221
REMARK 465     ILE A   222
REMARK 465     ALA A   223
REMARK 465     ASN A   224
REMARK 465     ASP A   225
REMARK 465     THR A   226
REMARK 465     LYS A   312
REMARK 465     ASP A   313
REMARK 465     MET B   -20
REMARK 465     ALA B   -19
REMARK 465     HIS B   -18
REMARK 465     HIS B   -17
REMARK 465     HIS B   -16
REMARK 465     HIS B   -15
REMARK 465     HIS B   -14
REMARK 465     HIS B   -13
REMARK 465     MET B   -12
REMARK 465     GLY B   -11
REMARK 465     THR B   -10
REMARK 465     LEU B    -9
REMARK 465     GLU B    -8
REMARK 465     ALA B    -7
REMARK 465     GLN B    -6
REMARK 465     THR B    -5
REMARK 465     GLN B    -4
REMARK 465     GLY B    -3
REMARK 465     PRO B    -2
REMARK 465     GLY B    -1
REMARK 465     SER B     0
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     SER B     3
REMARK 465     GLY B   153
REMARK 465     SER B   154
REMARK 465     SER B   155
REMARK 465     VAL B   156
REMARK 465     ALA B   157
REMARK 465     VAL B   158
REMARK 465     PRO B   210
REMARK 465     ALA B   211
REMARK 465     GLY B   212
REMARK 465     GLU B   213
REMARK 465     PHE B   214
REMARK 465     TYR B   215
REMARK 465     ASP B   216
REMARK 465     TYR B   217
REMARK 465     HIS B   218
REMARK 465     ALA B   219
REMARK 465     LYS B   220
REMARK 465     TYR B   221
REMARK 465     ILE B   222
REMARK 465     ALA B   223
REMARK 465     ASN B   224
REMARK 465     ASP B   225
REMARK 465     THR B   226
REMARK 465     LYS B   312
REMARK 465     ASP B   313
REMARK 465     MET C   -20
REMARK 465     ALA C   -19
REMARK 465     HIS C   -18
REMARK 465     HIS C   -17
REMARK 465     HIS C   -16
REMARK 465     HIS C   -15
REMARK 465     HIS C   -14
REMARK 465     HIS C   -13
REMARK 465     MET C   -12
REMARK 465     GLY C   -11
REMARK 465     THR C   -10
REMARK 465     LEU C    -9
REMARK 465     GLU C    -8
REMARK 465     ALA C    -7
REMARK 465     GLN C    -6
REMARK 465     THR C    -5
REMARK 465     GLN C    -4
REMARK 465     GLY C    -3
REMARK 465     PRO C    -2
REMARK 465     GLY C    -1
REMARK 465     SER C     0
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     SER C     3
REMARK 465     LYS C   135
REMARK 465     GLU C   136
REMARK 465     ILE C   137
REMARK 465     VAL C   138
REMARK 465     ALA C   139
REMARK 465     LYS C   140
REMARK 465     PRO C   149
REMARK 465     ALA C   150
REMARK 465     SER C   151
REMARK 465     GLU C   152
REMARK 465     GLY C   153
REMARK 465     SER C   154
REMARK 465     SER C   155
REMARK 465     VAL C   156
REMARK 465     ALA C   157
REMARK 465     VAL C   158
REMARK 465     PHE C   214
REMARK 465     TYR C   215
REMARK 465     ASP C   216
REMARK 465     TYR C   217
REMARK 465     HIS C   218
REMARK 465     ALA C   219
REMARK 465     LYS C   220
REMARK 465     TYR C   221
REMARK 465     ILE C   222
REMARK 465     ALA C   223
REMARK 465     ASP C   313
REMARK 465     MET D   -20
REMARK 465     ALA D   -19
REMARK 465     HIS D   -18
REMARK 465     HIS D   -17
REMARK 465     HIS D   -16
REMARK 465     HIS D   -15
REMARK 465     HIS D   -14
REMARK 465     HIS D   -13
REMARK 465     MET D   -12
REMARK 465     GLY D   -11
REMARK 465     THR D   -10
REMARK 465     LEU D    -9
REMARK 465     GLU D    -8
REMARK 465     ALA D    -7
REMARK 465     GLN D    -6
REMARK 465     THR D    -5
REMARK 465     GLN D    -4
REMARK 465     GLY D    -3
REMARK 465     PRO D    -2
REMARK 465     GLY D    -1
REMARK 465     SER D     0
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     VAL D   124
REMARK 465     LEU D   125
REMARK 465     ARG D   126
REMARK 465     GLY D   127
REMARK 465     ASP D   128
REMARK 465     ASP D   129
REMARK 465     TYR D   130
REMARK 465     GLU D   131
REMARK 465     ALA D   132
REMARK 465     ARG D   133
REMARK 465     ALA D   134
REMARK 465     LYS D   135
REMARK 465     GLU D   136
REMARK 465     ILE D   137
REMARK 465     VAL D   138
REMARK 465     ALA D   139
REMARK 465     LYS D   140
REMARK 465     LEU D   141
REMARK 465     PRO D   149
REMARK 465     ALA D   150
REMARK 465     SER D   151
REMARK 465     GLU D   152
REMARK 465     GLY D   153
REMARK 465     SER D   154
REMARK 465     SER D   155
REMARK 465     VAL D   156
REMARK 465     ALA D   157
REMARK 465     VAL D   158
REMARK 465     ILE D   159
REMARK 465     LYS D   160
REMARK 465     VAL D   161
REMARK 465     LYS D   162
REMARK 465     SER D   163
REMARK 465     ALA D   164
REMARK 465     ASP D   165
REMARK 465     ALA D   166
REMARK 465     LEU D   167
REMARK 465     PRO D   168
REMARK 465     ALA D   169
REMARK 465     ALA D   170
REMARK 465     LEU D   171
REMARK 465     ILE D   172
REMARK 465     GLU D   173
REMARK 465     ALA D   174
REMARK 465     VAL D   175
REMARK 465     LYS D   176
REMARK 465     PHE D   177
REMARK 465     ASP D   178
REMARK 465     ARG D   179
REMARK 465     ILE D   180
REMARK 465     GLY D   212
REMARK 465     GLU D   213
REMARK 465     PHE D   214
REMARK 465     TYR D   215
REMARK 465     ASP D   216
REMARK 465     TYR D   217
REMARK 465     HIS D   218
REMARK 465     ALA D   219
REMARK 465     LYS D   220
REMARK 465     TYR D   221
REMARK 465     ILE D   222
REMARK 465     ALA D   223
REMARK 465     ASN D   224
REMARK 465     ASP D   225
REMARK 465     ASP D   313
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  58    CG   CD   CE   NZ
REMARK 470     ASP A 129    CG   OD1  OD2
REMARK 470     GLU A 131    CG   CD   OE1  OE2
REMARK 470     LYS A 135    CG   CD   CE   NZ
REMARK 470     GLU A 136    CG   CD   OE1  OE2
REMARK 470     LYS A 140    CG   CD   CE   NZ
REMARK 470     ILE A 159    CG1  CG2  CD1
REMARK 470     LYS A 162    CG   CD   CE   NZ
REMARK 470     SER A 163    OG
REMARK 470     LYS A 176    CG   CD   CE   NZ
REMARK 470     PHE A 177    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG A 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 227    CG   CD   OE1  NE2
REMARK 470     LYS B   7    CG   CD   CE   NZ
REMARK 470     ASP B 128    CG   OD1  OD2
REMARK 470     ASP B 129    CG   OD1  OD2
REMARK 470     GLU B 131    CG   CD   OE1  OE2
REMARK 470     LYS B 135    CG   CD   CE   NZ
REMARK 470     GLU B 136    CG   CD   OE1  OE2
REMARK 470     LYS B 140    CG   CD   CE   NZ
REMARK 470     GLU B 152    CG   CD   OE1  OE2
REMARK 470     ILE B 159    CG1  CG2  CD1
REMARK 470     LYS B 162    CG   CD   CE   NZ
REMARK 470     GLU B 173    CG   CD   OE1  OE2
REMARK 470     LYS B 176    CG   CD   CE   NZ
REMARK 470     PHE B 177    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG B 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL B 209    CG1  CG2
REMARK 470     GLN B 227    CG   CD   OE1  NE2
REMARK 470     ILE C   4    CG1  CG2  CD1
REMARK 470     LYS C  58    CG   CD   CE   NZ
REMARK 470     LYS C 104    CG   CD   CE   NZ
REMARK 470     LEU C 125    CG   CD1  CD2
REMARK 470     ARG C 126    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP C 128    CG   OD1  OD2
REMARK 470     ASP C 129    CG   OD1  OD2
REMARK 470     GLU C 131    CG   CD   OE1  OE2
REMARK 470     ARG C 133    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU C 141    CG   CD1  CD2
REMARK 470     LEU C 143    CG   CD1  CD2
REMARK 470     LYS C 148    CG   CD   CE   NZ
REMARK 470     ILE C 159    CG1  CG2  CD1
REMARK 470     LYS C 160    CG   CD   CE   NZ
REMARK 470     VAL C 161    CG1  CG2
REMARK 470     ASP C 165    CG   OD1  OD2
REMARK 470     LEU C 167    CG   CD1  CD2
REMARK 470     LEU C 171    CG   CD1  CD2
REMARK 470     ILE C 172    CG1  CG2  CD1
REMARK 470     GLU C 173    CG   CD   OE1  OE2
REMARK 470     VAL C 175    CG1  CG2
REMARK 470     LYS C 176    CG   CD   CE   NZ
REMARK 470     PHE C 177    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ASP C 178    CG   OD1  OD2
REMARK 470     ARG C 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE C 180    CG1  CG2  CD1
REMARK 470     VAL C 182    CG1  CG2
REMARK 470     ASN C 224    CG   OD1  ND2
REMARK 470     LYS C 312    CG   CD   CE   NZ
REMARK 470     ILE D   4    CG1  CG2  CD1
REMARK 470     LYS D   7    CG   CD   CE   NZ
REMARK 470     LYS D 104    CG   CD   CE   NZ
REMARK 470     GLU D 122    CG   CD   OE1  OE2
REMARK 470     LEU D 143    CG   CD1  CD2
REMARK 470     LYS D 148    CG   CD   CE   NZ
REMARK 470     VAL D 181    CG1  CG2
REMARK 470     VAL D 182    CG1  CG2
REMARK 470     LYS D 312    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH B   401     O    HOH B   441              2.15
REMARK 500
REMARK 500 REMARK: NULL
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    HIS B  70   CG    HIS B  70   CD2     0.063
REMARK 500    HIS B 285   CG    HIS B 285   CD2     0.063
REMARK 500    HIS D  45   CG    HIS D  45   CD2     0.062
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    GLU B 301   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ARG C  31   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG C  31   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG D 106   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    ARG A 126      113.16    -36.57
REMARK 500    ASP A 257      -41.09     82.24
REMARK 500    ARG B 126      114.00    -37.70
REMARK 500    ASP B 257      -39.23     84.18
REMARK 500    ARG C 126      112.66    -38.82
REMARK 500    ASP C 257      -42.53     81.31
REMARK 500    ASP D 257      -43.11     85.61
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  256     ASP B  257                  147.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BUXEA.00119.A   RELATED DB: TARGETTRACK
DBREF  4EGJ A    1   313  UNP    Q13TZ4   DDL_BURXL        1    313
DBREF  4EGJ B    1   313  UNP    Q13TZ4   DDL_BURXL        1    313
DBREF  4EGJ C    1   313  UNP    Q13TZ4   DDL_BURXL        1    313
DBREF  4EGJ D    1   313  UNP    Q13TZ4   DDL_BURXL        1    313
SEQADV 4EGJ MET A  -20  UNP  Q13TZ4              INITIATING METHIONINE
SEQADV 4EGJ ALA A  -19  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS A  -18  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS A  -17  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS A  -16  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS A  -15  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS A  -14  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS A  -13  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET A  -12  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY A  -11  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR A  -10  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ LEU A   -9  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLU A   -8  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ ALA A   -7  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN A   -6  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR A   -5  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN A   -4  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY A   -3  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ PRO A   -2  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY A   -1  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ SER A    0  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET B  -20  UNP  Q13TZ4              INITIATING METHIONINE
SEQADV 4EGJ ALA B  -19  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS B  -18  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS B  -17  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS B  -16  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS B  -15  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS B  -14  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS B  -13  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET B  -12  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY B  -11  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR B  -10  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ LEU B   -9  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLU B   -8  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ ALA B   -7  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN B   -6  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR B   -5  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN B   -4  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY B   -3  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ PRO B   -2  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY B   -1  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ SER B    0  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET C  -20  UNP  Q13TZ4              INITIATING METHIONINE
SEQADV 4EGJ ALA C  -19  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS C  -18  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS C  -17  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS C  -16  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS C  -15  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS C  -14  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS C  -13  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET C  -12  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY C  -11  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR C  -10  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ LEU C   -9  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLU C   -8  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ ALA C   -7  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN C   -6  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR C   -5  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN C   -4  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY C   -3  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ PRO C   -2  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY C   -1  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ SER C    0  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET D  -20  UNP  Q13TZ4              INITIATING METHIONINE
SEQADV 4EGJ ALA D  -19  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS D  -18  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS D  -17  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS D  -16  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS D  -15  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS D  -14  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ HIS D  -13  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ MET D  -12  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY D  -11  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR D  -10  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ LEU D   -9  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLU D   -8  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ ALA D   -7  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN D   -6  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ THR D   -5  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLN D   -4  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY D   -3  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ PRO D   -2  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ GLY D   -1  UNP  Q13TZ4              EXPRESSION TAG
SEQADV 4EGJ SER D    0  UNP  Q13TZ4              EXPRESSION TAG
SEQRES   1 A  334  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES   2 A  334  ALA GLN THR GLN GLY PRO GLY SER MET SER SER ILE ASP
SEQRES   3 A  334  PRO LYS GLN PHE GLY LYS VAL ALA VAL LEU LEU GLY GLY
SEQRES   4 A  334  ASN SER ALA GLU ARG GLU VAL SER LEU ASN SER GLY ARG
SEQRES   5 A  334  LEU VAL LEU GLN GLY LEU ARG ASP ALA GLY ILE ASP ALA
SEQRES   6 A  334  HIS PRO PHE ASP PRO ALA GLU ARG PRO LEU ALA ALA LEU
SEQRES   7 A  334  LYS GLU GLU GLY PHE VAL ARG ALA PHE ASN ALA LEU HIS
SEQRES   8 A  334  GLY GLY TYR GLY GLU ASN GLY GLN ILE GLN GLY ALA LEU
SEQRES   9 A  334  ASP PHE TYR GLY ILE ARG TYR THR GLY SER GLY VAL LEU
SEQRES  10 A  334  GLY SER ALA LEU GLY LEU ASP LYS PHE ARG THR LYS LEU
SEQRES  11 A  334  VAL TRP GLN GLN LEU GLY ILE PRO THR PRO PRO PHE GLU
SEQRES  12 A  334  ALA VAL LEU ARG GLY ASP ASP TYR GLU ALA ARG ALA LYS
SEQRES  13 A  334  GLU ILE VAL ALA LYS LEU GLY LEU PRO LEU PHE VAL LYS
SEQRES  14 A  334  PRO ALA SER GLU GLY SER SER VAL ALA VAL ILE LYS VAL
SEQRES  15 A  334  LYS SER ALA ASP ALA LEU PRO ALA ALA LEU ILE GLU ALA
SEQRES  16 A  334  VAL LYS PHE ASP ARG ILE VAL VAL VAL GLU LYS SER ILE
SEQRES  17 A  334  GLU GLY GLY GLY GLU TYR THR ALA CYS ILE ALA GLY ASN
SEQRES  18 A  334  LEU ASP LEU PRO VAL ILE ARG ILE VAL PRO ALA GLY GLU
SEQRES  19 A  334  PHE TYR ASP TYR HIS ALA LYS TYR ILE ALA ASN ASP THR
SEQRES  20 A  334  GLN TYR LEU ILE PRO CYS GLY LEU THR ALA ASP GLU GLU
SEQRES  21 A  334  ALA ARG LEU LYS VAL LEU ALA ARG ARG ALA PHE ASP VAL
SEQRES  22 A  334  LEU GLY CYS THR ASP TRP GLY ARG ALA ASP PHE MET LEU
SEQRES  23 A  334  ASP ALA ASP GLY ASN PRO TYR PHE LEU GLU VAL ASN THR
SEQRES  24 A  334  ALA PRO GLY MET THR ASP HIS SER LEU PRO PRO LYS ALA
SEQRES  25 A  334  ALA ARG ALA VAL GLY ILE SER TYR GLN GLU LEU VAL VAL
SEQRES  26 A  334  ALA VAL LEU ALA LEU THR LEU LYS ASP
SEQRES   1 B  334  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES   2 B  334  ALA GLN THR GLN GLY PRO GLY SER MET SER SER ILE ASP
SEQRES   3 B  334  PRO LYS GLN PHE GLY LYS VAL ALA VAL LEU LEU GLY GLY
SEQRES   4 B  334  ASN SER ALA GLU ARG GLU VAL SER LEU ASN SER GLY ARG
SEQRES   5 B  334  LEU VAL LEU GLN GLY LEU ARG ASP ALA GLY ILE ASP ALA
SEQRES   6 B  334  HIS PRO PHE ASP PRO ALA GLU ARG PRO LEU ALA ALA LEU
SEQRES   7 B  334  LYS GLU GLU GLY PHE VAL ARG ALA PHE ASN ALA LEU HIS
SEQRES   8 B  334  GLY GLY TYR GLY GLU ASN GLY GLN ILE GLN GLY ALA LEU
SEQRES   9 B  334  ASP PHE TYR GLY ILE ARG TYR THR GLY SER GLY VAL LEU
SEQRES  10 B  334  GLY SER ALA LEU GLY LEU ASP LYS PHE ARG THR LYS LEU
SEQRES  11 B  334  VAL TRP GLN GLN LEU GLY ILE PRO THR PRO PRO PHE GLU
SEQRES  12 B  334  ALA VAL LEU ARG GLY ASP ASP TYR GLU ALA ARG ALA LYS
SEQRES  13 B  334  GLU ILE VAL ALA LYS LEU GLY LEU PRO LEU PHE VAL LYS
SEQRES  14 B  334  PRO ALA SER GLU GLY SER SER VAL ALA VAL ILE LYS VAL
SEQRES  15 B  334  LYS SER ALA ASP ALA LEU PRO ALA ALA LEU ILE GLU ALA
SEQRES  16 B  334  VAL LYS PHE ASP ARG ILE VAL VAL VAL GLU LYS SER ILE
SEQRES  17 B  334  GLU GLY GLY GLY GLU TYR THR ALA CYS ILE ALA GLY ASN
SEQRES  18 B  334  LEU ASP LEU PRO VAL ILE ARG ILE VAL PRO ALA GLY GLU
SEQRES  19 B  334  PHE TYR ASP TYR HIS ALA LYS TYR ILE ALA ASN ASP THR
SEQRES  20 B  334  GLN TYR LEU ILE PRO CYS GLY LEU THR ALA ASP GLU GLU
SEQRES  21 B  334  ALA ARG LEU LYS VAL LEU ALA ARG ARG ALA PHE ASP VAL
SEQRES  22 B  334  LEU GLY CYS THR ASP TRP GLY ARG ALA ASP PHE MET LEU
SEQRES  23 B  334  ASP ALA ASP GLY ASN PRO TYR PHE LEU GLU VAL ASN THR
SEQRES  24 B  334  ALA PRO GLY MET THR ASP HIS SER LEU PRO PRO LYS ALA
SEQRES  25 B  334  ALA ARG ALA VAL GLY ILE SER TYR GLN GLU LEU VAL VAL
SEQRES  26 B  334  ALA VAL LEU ALA LEU THR LEU LYS ASP
SEQRES   1 C  334  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES   2 C  334  ALA GLN THR GLN GLY PRO GLY SER MET SER SER ILE ASP
SEQRES   3 C  334  PRO LYS GLN PHE GLY LYS VAL ALA VAL LEU LEU GLY GLY
SEQRES   4 C  334  ASN SER ALA GLU ARG GLU VAL SER LEU ASN SER GLY ARG
SEQRES   5 C  334  LEU VAL LEU GLN GLY LEU ARG ASP ALA GLY ILE ASP ALA
SEQRES   6 C  334  HIS PRO PHE ASP PRO ALA GLU ARG PRO LEU ALA ALA LEU
SEQRES   7 C  334  LYS GLU GLU GLY PHE VAL ARG ALA PHE ASN ALA LEU HIS
SEQRES   8 C  334  GLY GLY TYR GLY GLU ASN GLY GLN ILE GLN GLY ALA LEU
SEQRES   9 C  334  ASP PHE TYR GLY ILE ARG TYR THR GLY SER GLY VAL LEU
SEQRES  10 C  334  GLY SER ALA LEU GLY LEU ASP LYS PHE ARG THR LYS LEU
SEQRES  11 C  334  VAL TRP GLN GLN LEU GLY ILE PRO THR PRO PRO PHE GLU
SEQRES  12 C  334  ALA VAL LEU ARG GLY ASP ASP TYR GLU ALA ARG ALA LYS
SEQRES  13 C  334  GLU ILE VAL ALA LYS LEU GLY LEU PRO LEU PHE VAL LYS
SEQRES  14 C  334  PRO ALA SER GLU GLY SER SER VAL ALA VAL ILE LYS VAL
SEQRES  15 C  334  LYS SER ALA ASP ALA LEU PRO ALA ALA LEU ILE GLU ALA
SEQRES  16 C  334  VAL LYS PHE ASP ARG ILE VAL VAL VAL GLU LYS SER ILE
SEQRES  17 C  334  GLU GLY GLY GLY GLU TYR THR ALA CYS ILE ALA GLY ASN
SEQRES  18 C  334  LEU ASP LEU PRO VAL ILE ARG ILE VAL PRO ALA GLY GLU
SEQRES  19 C  334  PHE TYR ASP TYR HIS ALA LYS TYR ILE ALA ASN ASP THR
SEQRES  20 C  334  GLN TYR LEU ILE PRO CYS GLY LEU THR ALA ASP GLU GLU
SEQRES  21 C  334  ALA ARG LEU LYS VAL LEU ALA ARG ARG ALA PHE ASP VAL
SEQRES  22 C  334  LEU GLY CYS THR ASP TRP GLY ARG ALA ASP PHE MET LEU
SEQRES  23 C  334  ASP ALA ASP GLY ASN PRO TYR PHE LEU GLU VAL ASN THR
SEQRES  24 C  334  ALA PRO GLY MET THR ASP HIS SER LEU PRO PRO LYS ALA
SEQRES  25 C  334  ALA ARG ALA VAL GLY ILE SER TYR GLN GLU LEU VAL VAL
SEQRES  26 C  334  ALA VAL LEU ALA LEU THR LEU LYS ASP
SEQRES   1 D  334  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES   2 D  334  ALA GLN THR GLN GLY PRO GLY SER MET SER SER ILE ASP
SEQRES   3 D  334  PRO LYS GLN PHE GLY LYS VAL ALA VAL LEU LEU GLY GLY
SEQRES   4 D  334  ASN SER ALA GLU ARG GLU VAL SER LEU ASN SER GLY ARG
SEQRES   5 D  334  LEU VAL LEU GLN GLY LEU ARG ASP ALA GLY ILE ASP ALA
SEQRES   6 D  334  HIS PRO PHE ASP PRO ALA GLU ARG PRO LEU ALA ALA LEU
SEQRES   7 D  334  LYS GLU GLU GLY PHE VAL ARG ALA PHE ASN ALA LEU HIS
SEQRES   8 D  334  GLY GLY TYR GLY GLU ASN GLY GLN ILE GLN GLY ALA LEU
SEQRES   9 D  334  ASP PHE TYR GLY ILE ARG TYR THR GLY SER GLY VAL LEU
SEQRES  10 D  334  GLY SER ALA LEU GLY LEU ASP LYS PHE ARG THR LYS LEU
SEQRES  11 D  334  VAL TRP GLN GLN LEU GLY ILE PRO THR PRO PRO PHE GLU
SEQRES  12 D  334  ALA VAL LEU ARG GLY ASP ASP TYR GLU ALA ARG ALA LYS
SEQRES  13 D  334  GLU ILE VAL ALA LYS LEU GLY LEU PRO LEU PHE VAL LYS
SEQRES  14 D  334  PRO ALA SER GLU GLY SER SER VAL ALA VAL ILE LYS VAL
SEQRES  15 D  334  LYS SER ALA ASP ALA LEU PRO ALA ALA LEU ILE GLU ALA
SEQRES  16 D  334  VAL LYS PHE ASP ARG ILE VAL VAL VAL GLU LYS SER ILE
SEQRES  17 D  334  GLU GLY GLY GLY GLU TYR THR ALA CYS ILE ALA GLY ASN
SEQRES  18 D  334  LEU ASP LEU PRO VAL ILE ARG ILE VAL PRO ALA GLY GLU
SEQRES  19 D  334  PHE TYR ASP TYR HIS ALA LYS TYR ILE ALA ASN ASP THR
SEQRES  20 D  334  GLN TYR LEU ILE PRO CYS GLY LEU THR ALA ASP GLU GLU
SEQRES  21 D  334  ALA ARG LEU LYS VAL LEU ALA ARG ARG ALA PHE ASP VAL
SEQRES  22 D  334  LEU GLY CYS THR ASP TRP GLY ARG ALA ASP PHE MET LEU
SEQRES  23 D  334  ASP ALA ASP GLY ASN PRO TYR PHE LEU GLU VAL ASN THR
SEQRES  24 D  334  ALA PRO GLY MET THR ASP HIS SER LEU PRO PRO LYS ALA
SEQRES  25 D  334  ALA ARG ALA VAL GLY ILE SER TYR GLN GLU LEU VAL VAL
SEQRES  26 D  334  ALA VAL LEU ALA LEU THR LEU LYS ASP
FORMUL   5  HOH   *358(H2 O)
HELIX    1   1 ASP A    5  PHE A    9  5                                   5
HELIX    2   2 GLU A   22  ALA A   40  1                                  19
HELIX    3   3 ALA A   55  GLU A   60  1                                   6
HELIX    4   4 GLY A   71  GLU A   75  5                                   5
HELIX    5   5 GLY A   77  GLY A   87  1                                  11
HELIX    6   6 GLY A   94  LEU A  102  1                                   9
HELIX    7   7 ASP A  103  LEU A  114  1                                  12
HELIX    8   8 ASP A  129  GLY A  142  1                                  14
HELIX    9   9 SER A  163  ASP A  165  5                                   3
HELIX   10  10 ALA A  166  VAL A  175  1                                  10
HELIX   11  11 THR A  235  VAL A  252  1                                  18
HELIX   12  12 SER A  286  VAL A  295  1                                  10
HELIX   13  13 SER A  298  LEU A  309  1                                  12
HELIX   14  14 ASP B    5  PHE B    9  5                                   5
HELIX   15  15 GLU B   22  ALA B   40  1                                  19
HELIX   16  16 LEU B   54  GLU B   60  1                                   7
HELIX   17  17 GLY B   71  GLU B   75  5                                   5
HELIX   18  18 GLY B   77  GLY B   87  1                                  11
HELIX   19  19 GLY B   94  LEU B  102  1                                   9
HELIX   20  20 ASP B  103  LEU B  114  1                                  12
HELIX   21  21 ASP B  129  GLY B  142  1                                  14
HELIX   22  22 SER B  163  ASP B  165  5                                   3
HELIX   23  23 ALA B  166  VAL B  175  1                                  10
HELIX   24  24 THR B  235  VAL B  252  1                                  18
HELIX   25  25 SER B  286  VAL B  295  1                                  10
HELIX   26  26 SER B  298  LEU B  309  1                                  12
HELIX   27  27 ASP C    5  PHE C    9  5                                   5
HELIX   28  28 GLU C   22  ALA C   40  1                                  19
HELIX   29  29 ALA C   55  GLU C   60  1                                   6
HELIX   30  30 GLY C   71  GLU C   75  5                                   5
HELIX   31  31 GLY C   77  GLY C   87  1                                  11
HELIX   32  32 GLY C   94  LEU C  102  1                                   9
HELIX   33  33 ASP C  103  LEU C  114  1                                  12
HELIX   34  34 ASP C  129  ALA C  134  1                                   6
HELIX   35  35 SER C  163  ASP C  165  5                                   3
HELIX   36  36 ALA C  166  VAL C  175  1                                  10
HELIX   37  37 THR C  235  VAL C  252  1                                  18
HELIX   38  38 SER C  286  VAL C  295  1                                  10
HELIX   39  39 SER C  298  LEU C  309  1                                  12
HELIX   40  40 THR C  310  LYS C  312  5                                   3
HELIX   41  41 ASP D    5  PHE D    9  5                                   5
HELIX   42  42 GLU D   22  ALA D   40  1                                  19
HELIX   43  43 LEU D   54  GLU D   60  1                                   7
HELIX   44  44 GLY D   71  GLU D   75  5                                   5
HELIX   45  45 GLY D   77  GLY D   87  1                                  11
HELIX   46  46 GLY D   94  LEU D  102  1                                   9
HELIX   47  47 ASP D  103  LEU D  114  1                                  12
HELIX   48  48 THR D  235  VAL D  252  1                                  18
HELIX   49  49 SER D  286  VAL D  295  1                                  10
HELIX   50  50 SER D  298  LEU D  309  1                                  12
HELIX   51  51 THR D  310  LYS D  312  5                                   3
SHEET    1   A 4 ASP A  43  PHE A  47  0
SHEET    2   A 4 LYS A  11  LEU A  15  1  N  VAL A  14   O  HIS A  45
SHEET    3   A 4 ARG A  64  ASN A  67  1  O  ARG A  64   N  ALA A  13
SHEET    4   A 4 ARG A  89  TYR A  90  1  O  ARG A  89   N  ALA A  65
SHEET    1   B 4 PHE A 121  LEU A 125  0
SHEET    2   B 4 ILE A 180  LYS A 185 -1  O  VAL A 181   N  VAL A 124
SHEET    3   B 4 LEU A 145  PRO A 149 -1  N  PHE A 146   O  GLU A 184
SHEET    4   B 4 LYS A 160  VAL A 161 -1  O  VAL A 161   N  LEU A 145
SHEET    1   C 5 TYR A 228  LEU A 229  0
SHEET    2   C 5 ILE A 206  ILE A 208 -1  N  ARG A 207   O  LEU A 229
SHEET    3   C 5 GLY A 189  ALA A 198 -1  N  THR A 194   O  ILE A 206
SHEET    4   C 5 TRP A 258  ASP A 266 -1  O  PHE A 263   N  TYR A 193
SHEET    5   C 5 PRO A 271  ASN A 277 -1  O  TYR A 272   N  MET A 264
SHEET    1   D 4 ASP B  43  PHE B  47  0
SHEET    2   D 4 LYS B  11  LEU B  15  1  N  VAL B  14   O  HIS B  45
SHEET    3   D 4 ARG B  64  ASN B  67  1  O  ARG B  64   N  ALA B  13
SHEET    4   D 4 ARG B  89  TYR B  90  1  O  ARG B  89   N  ALA B  65
SHEET    1   E 4 PHE B 121  LEU B 125  0
SHEET    2   E 4 ILE B 180  LYS B 185 -1  O  VAL B 181   N  VAL B 124
SHEET    3   E 4 LEU B 145  PRO B 149 -1  N  PHE B 146   O  GLU B 184
SHEET    4   E 4 LYS B 160  VAL B 161 -1  O  VAL B 161   N  LEU B 145
SHEET    1   F 4 ILE B 206  ILE B 208  0
SHEET    2   F 4 GLY B 189  ALA B 198 -1  N  THR B 194   O  ILE B 206
SHEET    3   F 4 TRP B 258  ASP B 266 -1  O  PHE B 263   N  TYR B 193
SHEET    4   F 4 PRO B 271  ASN B 277 -1  O  TYR B 272   N  MET B 264
SHEET    1   G 4 ASP C  43  PHE C  47  0
SHEET    2   G 4 LYS C  11  LEU C  15  1  N  VAL C  14   O  HIS C  45
SHEET    3   G 4 ARG C  64  ASN C  67  1  O  ARG C  64   N  ALA C  13
SHEET    4   G 4 ARG C  89  TYR C  90  1  O  ARG C  89   N  ALA C  65
SHEET    1   H 4 PHE C 121  LEU C 125  0
SHEET    2   H 4 ILE C 180  LYS C 185 -1  O  VAL C 181   N  VAL C 124
SHEET    3   H 4 LEU C 145  LYS C 148 -1  N  PHE C 146   O  GLU C 184
SHEET    4   H 4 LYS C 160  VAL C 161 -1  O  VAL C 161   N  LEU C 145
SHEET    1   I 5 GLN C 227  LEU C 229  0
SHEET    2   I 5 ILE C 206  VAL C 209 -1  N  ARG C 207   O  LEU C 229
SHEET    3   I 5 GLY C 189  ALA C 198 -1  N  THR C 194   O  ILE C 206
SHEET    4   I 5 TRP C 258  ASP C 266 -1  O  PHE C 263   N  TYR C 193
SHEET    5   I 5 PRO C 271  ASN C 277 -1  O  TYR C 272   N  MET C 264
SHEET    1   J 4 ASP D  43  PHE D  47  0
SHEET    2   J 4 LYS D  11  LEU D  15  1  N  VAL D  14   O  HIS D  45
SHEET    3   J 4 ARG D  64  ASN D  67  1  O  ARG D  64   N  ALA D  13
SHEET    4   J 4 ARG D  89  TYR D  90  1  O  ARG D  89   N  ALA D  65
SHEET    1   K 3 PHE D 121  GLU D 122  0
SHEET    2   K 3 VAL D 183  LYS D 185 -1  O  VAL D 183   N  GLU D 122
SHEET    3   K 3 LEU D 145  VAL D 147 -1  N  PHE D 146   O  GLU D 184
SHEET    1   L 5 GLN D 227  LEU D 229  0
SHEET    2   L 5 ILE D 206  VAL D 209 -1  N  ARG D 207   O  LEU D 229
SHEET    3   L 5 GLY D 189  ALA D 198 -1  N  THR D 194   O  ILE D 206
SHEET    4   L 5 TRP D 258  ASP D 266 -1  O  PHE D 263   N  TYR D 193
SHEET    5   L 5 PRO D 271  ASN D 277 -1  O  TYR D 272   N  MET D 264
CISPEP   1 LEU A  143    PRO A  144          0        -7.59
CISPEP   2 ILE A  230    PRO A  231          0         1.15
CISPEP   3 LEU B  143    PRO B  144          0        -3.20
CISPEP   4 ILE B  230    PRO B  231          0        -0.57
CISPEP   5 LEU C  143    PRO C  144          0        -4.20
CISPEP   6 ILE C  230    PRO C  231          0        -0.26
CISPEP   7 LEU D  143    PRO D  144          0        -6.71
CISPEP   8 ILE D  230    PRO D  231          0        -6.14
CRYST1   78.930   78.930  224.740  90.00  90.00  90.00 P 43         16
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      0.012669  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012669  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004450        0.00000
      
PROCHECK
Go to PROCHECK summary
 References