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PDBsum entry 3qbp

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Top Page protein Protein-protein interface(s) links
Lyase PDB id
3qbp
Jmol
Contents
Protein chains
441 a.a.
Waters ×1684
HEADER    LYASE                                   13-JAN-11   3QBP
TITLE     CRYSTAL STRUCTURE OF FUMARASE FUM FROM MYCOBACTERIUM MARINUM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FUMARASE FUM;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM MARINUM;
SOURCE   3 ORGANISM_TAXID: 216594;
SOURCE   4 STRAIN: ATCC BAA-535 / M;
SOURCE   5 GENE: FUM, MMAR_4368;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS   2 INFECTIOUS DISEASE, SSGCID, FUMARASE, MYCOBACTERIUM, TUBERCULOSIS,
KEYWDS   3 NON-PATHOGENIC SPECIES, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT   1   26-JAN-11 3QBP    0
JRNL        AUTH   T.E.EDWARDS,A.S.GARDBERG,B.SANKARAN
JRNL        TITL   CRYSTAL STRUCTURE OF FUMARASE FUM FROM MYCOBACTERIUM MARINUM
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 176519
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157
REMARK   3   R VALUE            (WORKING SET) : 0.155
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 8834
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12411
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150
REMARK   3   BIN FREE R VALUE SET COUNT          : 672
REMARK   3   BIN FREE R VALUE                    : 0.2630
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 12804
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 1684
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 22.30
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.28
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.34000
REMARK   3    B22 (A**2) : -0.75000
REMARK   3    B33 (A**2) : 1.55000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.79000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.067
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.905
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13296 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18180 ; 1.314 ; 1.965
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1848 ; 5.079 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   527 ;36.664 ;24.934
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2159 ;12.559 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    87 ;17.533 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2212 ; 0.092 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10019 ; 0.007 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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):  8878 ; 0.689 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14201 ; 1.203 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4418 ; 2.000 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3933 ; 3.357 ; 4.500
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 : NULL
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 : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   -10        A  9999
REMARK   3    ORIGIN FOR THE GROUP (A): -36.7949 -18.5342 -11.5332
REMARK   3    T TENSOR
REMARK   3      T11:   0.0285 T22:   0.0415
REMARK   3      T33:   0.0078 T12:  -0.0118
REMARK   3      T13:   0.0109 T23:  -0.0070
REMARK   3    L TENSOR
REMARK   3      L11:   0.0311 L22:   0.3641
REMARK   3      L33:   0.2419 L12:   0.0667
REMARK   3      L13:   0.0624 L23:   0.1891
REMARK   3    S TENSOR
REMARK   3      S11:   0.0185 S12:  -0.0270 S13:   0.0072
REMARK   3      S21:   0.0453 S22:  -0.0151 S23:   0.0043
REMARK   3      S31:   0.0334 S32:  -0.0644 S33:  -0.0034
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   -10        B  9999
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3901 -18.9778 -42.4560
REMARK   3    T TENSOR
REMARK   3      T11:   0.0282 T22:   0.0318
REMARK   3      T33:   0.0108 T12:   0.0037
REMARK   3      T13:   0.0103 T23:   0.0018
REMARK   3    L TENSOR
REMARK   3      L11:   0.3148 L22:   0.1284
REMARK   3      L33:   0.0397 L12:   0.0656
REMARK   3      L13:   0.0393 L23:   0.0355
REMARK   3    S TENSOR
REMARK   3      S11:   0.0024 S12:   0.0353 S13:   0.0089
REMARK   3      S21:  -0.0234 S22:  -0.0056 S23:  -0.0105
REMARK   3      S31:   0.0195 S32:   0.0052 S33:   0.0033
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   -10        C  9999
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4131 -21.9570 -13.7955
REMARK   3    T TENSOR
REMARK   3      T11:   0.0275 T22:   0.0086
REMARK   3      T33:   0.0505 T12:   0.0068
REMARK   3      T13:  -0.0065 T23:   0.0094
REMARK   3    L TENSOR
REMARK   3      L11:   0.3316 L22:   0.6508
REMARK   3      L33:   0.2086 L12:   0.3743
REMARK   3      L13:   0.1541 L23:   0.2995
REMARK   3    S TENSOR
REMARK   3      S11:   0.0277 S12:  -0.0316 S13:  -0.0711
REMARK   3      S21:   0.0348 S22:  -0.0164 S23:  -0.1176
REMARK   3      S31:   0.0309 S32:   0.0087 S33:  -0.0112
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   -10        D  9999
REMARK   3    ORIGIN FOR THE GROUP (A): -27.8140   3.1923 -30.7345
REMARK   3    T TENSOR
REMARK   3      T11:   0.0090 T22:   0.0131
REMARK   3      T33:   0.0422 T12:   0.0101
REMARK   3      T13:   0.0027 T23:   0.0043
REMARK   3    L TENSOR
REMARK   3      L11:   0.4170 L22:   0.1162
REMARK   3      L33:   0.0802 L12:   0.0707
REMARK   3      L13:   0.0828 L23:  -0.0124
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0052 S12:   0.0071 S13:   0.0926
REMARK   3      S21:   0.0029 S22:  -0.0049 S23:   0.0280
REMARK   3      S31:  -0.0128 S32:  -0.0077 S33:   0.0101
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3QBP COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 5.0.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 176663
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850
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     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.50500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.100
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 3NO9, MOLECULE A RESIDUES 43 TO 393
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MYMAA.01507.A.A1 PS00842 AT 51.1 MG/ML
REMARK 280  AGAINST PACT SCREEN CONDITION A7, 0.2 M NACL, 0.1 M NAOAC PH 5.0,
REMARK 280  20% PEG 6000 SOAKED INTO PACT A7 WITH 25% EG AS CRYO-PROTECTANT,
REMARK 280  CRYSTAL TRACKING ID 218662A7, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 289K
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       57.04000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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    -3
REMARK 465     PRO A    -2
REMARK 465     GLY A    -1
REMARK 465     SER A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     HIS A     3
REMARK 465     SER A     4
REMARK 465     ALA A     5
REMARK 465     HIS A     6
REMARK 465     ASP A     7
REMARK 465     ASP A     8
REMARK 465     ALA A     9
REMARK 465     ASP A    10
REMARK 465     ASN A    11
REMARK 465     ASP A    12
REMARK 465     THR A    13
REMARK 465     GLU A    14
REMARK 465     TYR A    15
REMARK 465     ARG A    16
REMARK 465     ILE A    17
REMARK 465     GLU A    18
REMARK 465     HIS A    19
REMARK 465     ASP A    20
REMARK 465     THR A    21
REMARK 465     MET A    22
REMARK 465     GLY A    23
REMARK 465     GLU A    24
REMARK 465     VAL A    25
REMARK 465     GLN A   320
REMARK 465     PRO A   321
REMARK 465     GLY A   322
REMARK 465     SER A   323
REMARK 465     SER A   324
REMARK 465     ILE A   325
REMARK 465     ALA A   473
REMARK 465     THR A   474
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     ALA B     2
REMARK 465     HIS B     3
REMARK 465     SER B     4
REMARK 465     ALA B     5
REMARK 465     HIS B     6
REMARK 465     ASP B     7
REMARK 465     ASP B     8
REMARK 465     ALA B     9
REMARK 465     ASP B    10
REMARK 465     ASN B    11
REMARK 465     ASP B    12
REMARK 465     THR B    13
REMARK 465     GLU B    14
REMARK 465     TYR B    15
REMARK 465     ARG B    16
REMARK 465     ILE B    17
REMARK 465     GLU B    18
REMARK 465     HIS B    19
REMARK 465     ASP B    20
REMARK 465     THR B    21
REMARK 465     MET B    22
REMARK 465     GLY B    23
REMARK 465     GLU B    24
REMARK 465     VAL B    25
REMARK 465     ALA B   473
REMARK 465     THR B   474
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     ALA C     2
REMARK 465     HIS C     3
REMARK 465     SER C     4
REMARK 465     ALA C     5
REMARK 465     HIS C     6
REMARK 465     ASP C     7
REMARK 465     ASP C     8
REMARK 465     ALA C     9
REMARK 465     ASP C    10
REMARK 465     ASN C    11
REMARK 465     ASP C    12
REMARK 465     THR C    13
REMARK 465     GLU C    14
REMARK 465     TYR C    15
REMARK 465     ARG C    16
REMARK 465     ILE C    17
REMARK 465     GLU C    18
REMARK 465     HIS C    19
REMARK 465     ASP C    20
REMARK 465     THR C    21
REMARK 465     MET C    22
REMARK 465     GLY C    23
REMARK 465     GLU C    24
REMARK 465     VAL C    25
REMARK 465     ARG C    26
REMARK 465     VAL C    27
REMARK 465     PRO C    28
REMARK 465     ALA C    29
REMARK 465     LYS C    30
REMARK 465     GLN C   320
REMARK 465     PRO C   321
REMARK 465     GLY C   322
REMARK 465     SER C   323
REMARK 465     SER C   324
REMARK 465     ALA C   473
REMARK 465     THR C   474
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     ALA D     2
REMARK 465     HIS D     3
REMARK 465     SER D     4
REMARK 465     ALA D     5
REMARK 465     HIS D     6
REMARK 465     ASP D     7
REMARK 465     ASP D     8
REMARK 465     ALA D     9
REMARK 465     ASP D    10
REMARK 465     ASN D    11
REMARK 465     ASP D    12
REMARK 465     THR D    13
REMARK 465     GLU D    14
REMARK 465     TYR D    15
REMARK 465     ARG D    16
REMARK 465     ILE D    17
REMARK 465     GLU D    18
REMARK 465     HIS D    19
REMARK 465     ASP D    20
REMARK 465     THR D    21
REMARK 465     MET D    22
REMARK 465     GLY D    23
REMARK 465     GLU D    24
REMARK 465     VAL D    25
REMARK 465     ARG D    26
REMARK 465     GLN D   320
REMARK 465     PRO D   321
REMARK 465     GLY D   322
REMARK 465     SER D   323
REMARK 465     SER D   324
REMARK 465     ILE D   325
REMARK 465     MET D   326
REMARK 465     PRO D   327
REMARK 465     GLY D   328
REMARK 465     ALA D   473
REMARK 465     THR D   474
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  26    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A  30    CG   CD   CE   NZ
REMARK 470     ARG A  39    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 435    CG   CD   CE   NZ
REMARK 470     ARG A 437    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A 452    CG   OD1  OD2
REMARK 470     LYS A 453    CG   CD   CE   NZ
REMARK 470     GLU A 457    CG   CD   OE1  OE2
REMARK 470     GLU A 472    CG   CD   OE1  OE2
REMARK 470     ARG B  26    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B  30    CG   CD   CE   NZ
REMARK 470     ARG B  39    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  49    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B 315    CG   CD   OE1  NE2
REMARK 470     GLU B 401    CG   CD   OE1  OE2
REMARK 470     GLU B 405    CG   CD   OE1  OE2
REMARK 470     LYS B 435    CG   CD   CE   NZ
REMARK 470     ARG B 437    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B 452    CG   OD1  OD2
REMARK 470     LYS B 453    CG   CD   CE   NZ
REMARK 470     GLU B 472    CG   CD   OE1  OE2
REMARK 470     ARG C  49    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C 244    CG   CD   OE1  OE2
REMARK 470     ILE C 325    CG1  CG2  CD1
REMARK 470     GLU C 401    CG   CD   OE1  OE2
REMARK 470     TYR C 423    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     GLU C 424    CG   CD   OE1  OE2
REMARK 470     LYS C 431    CG   CD   CE   NZ
REMARK 470     LYS C 435    CG   CD   CE   NZ
REMARK 470     ARG C 461    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C 472    CG   CD   OE1  OE2
REMARK 470     LYS D  30    CG   CD   CE   NZ
REMARK 470     ARG D  39    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D  49    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG D  53    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU D 244    CG   CD   OE1  OE2
REMARK 470     GLU D 401    CG   CD   OE1  OE2
REMARK 470     LYS D 431    CG   CD   CE   NZ
REMARK 470     LYS D 435    CG   CD   CE   NZ
REMARK 470     ARG D 437    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP D 452    CG   OD1  OD2
REMARK 470     GLU D 457    CG   CD   OE1  OE2
REMARK 470     GLU D 472    CG   CD   OE1  OE2
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   NE2  GLN B   257     O    HOH B  1214              2.13
REMARK 500   O    HOH B   960     O    HOH D  1223              2.14
REMARK 500   OE1  GLN A   257     O    HOH A  1213              2.16
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    PRO A  28      153.69    -46.01
REMARK 500    ARG A  34     -154.11   -130.24
REMARK 500    PHE A  44       55.71   -119.30
REMARK 500    HIS A  96       36.51   -143.45
REMARK 500    HIS A 163      -58.89   -121.23
REMARK 500    THR A 234     -143.43     52.12
REMARK 500    PHE A 361     -123.33     52.64
REMARK 500    VAL A 365       45.90   -108.14
REMARK 500    CYS A 392      -66.05   -131.41
REMARK 500    LEU A 454      106.28   -161.20
REMARK 500    ARG B  34     -151.90   -128.90
REMARK 500    HIS B 163      -57.46   -121.68
REMARK 500    THR B 234     -142.91     51.38
REMARK 500    PHE B 361     -119.62     52.06
REMARK 500    VAL B 365       47.79   -107.38
REMARK 500    CYS B 392      -66.01   -126.51
REMARK 500    ARG C  34     -156.92   -122.65
REMARK 500    HIS C 163      -62.35   -120.61
REMARK 500    THR C 234     -143.75     49.68
REMARK 500    PHE C 361     -120.63     52.68
REMARK 500    VAL C 365       47.92   -109.72
REMARK 500    CYS C 392      -66.63   -132.37
REMARK 500    LEU C 454      102.13   -164.15
REMARK 500    ARG D  34     -150.85   -129.10
REMARK 500    ASP D 137      -60.93   -102.16
REMARK 500    HIS D 163      -58.49   -122.35
REMARK 500    THR D 234     -139.43     50.56
REMARK 500    PHE D 361     -120.30     52.93
REMARK 500    VAL D 365       46.45   -107.96
REMARK 500    CYS D 392      -65.86   -126.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYMAA.01507.A   RELATED DB: TARGETDB
DBREF  3QBP A    1   474  UNP    B2HT54   B2HT54_MYCMM     1    474
DBREF  3QBP B    1   474  UNP    B2HT54   B2HT54_MYCMM     1    474
DBREF  3QBP C    1   474  UNP    B2HT54   B2HT54_MYCMM     1    474
DBREF  3QBP D    1   474  UNP    B2HT54   B2HT54_MYCMM     1    474
SEQADV 3QBP GLY A   -3  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP PRO A   -2  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY A   -1  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP SER A    0  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY B   -3  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP PRO B   -2  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY B   -1  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP SER B    0  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY C   -3  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP PRO C   -2  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY C   -1  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP SER C    0  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY D   -3  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP PRO D   -2  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP GLY D   -1  UNP  B2HT54              EXPRESSION TAG
SEQADV 3QBP SER D    0  UNP  B2HT54              EXPRESSION TAG
SEQRES   1 A  478  GLY PRO GLY SER MET ALA HIS SER ALA HIS ASP ASP ALA
SEQRES   2 A  478  ASP ASN ASP THR GLU TYR ARG ILE GLU HIS ASP THR MET
SEQRES   3 A  478  GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES   4 A  478  GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES   5 A  478  ARG GLY LEU GLU ARG ALA GLN ILE ARG ALA LEU GLY LEU
SEQRES   6 A  478  LEU LYS GLY ALA CYS ALA GLN VAL ASN MET ASP LEU GLY
SEQRES   7 A  478  LEU LEU ALA PRO GLU LYS ALA GLU ALA ILE ILE ALA ALA
SEQRES   8 A  478  ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES   9 A  478  PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES  10 A  478  ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA GLY
SEQRES  11 A  478  ALA ASN GLY VAL ALA VAL HIS PRO ASN ASP ASP VAL ASN
SEQRES  12 A  478  MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES  13 A  478  HIS ILE ALA ALA THR GLU ALA ALA VAL SER HIS LEU ILE
SEQRES  14 A  478  PRO ALA LEU GLU ILE LEU GLN ASP ALA LEU ALA THR LYS
SEQRES  15 A  478  ALA LEU GLU TRP GLN SER VAL VAL LYS SER GLY ARG THR
SEQRES  16 A  478  HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES  17 A  478  PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES  18 A  478  ARG VAL ARG ALA THR LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES  19 A  478  ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES  20 A  478  GLU GLY PHE GLY VAL LYS VAL VAL SER VAL LEU VAL SER
SEQRES  21 A  478  GLN THR GLY LEU PRO GLN LEU ARG THR ALA ALA ASN SER
SEQRES  22 A  478  PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES  23 A  478  SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES  24 A  478  ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES  25 A  478  THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES  26 A  478  GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES  27 A  478  PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES  28 A  478  ASN ASP ALA ALA VAL ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES  29 A  478  PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES  30 A  478  ILE LEU GLU SER PHE THR LEU LEU THR ASN VAL SER LYS
SEQRES  31 A  478  LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES  32 A  478  ALA GLU HIS LEU ARG GLU LEU ALA GLU SER SER PRO SER
SEQRES  33 A  478  ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES  34 A  478  ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES  35 A  478  THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES  36 A  478  ASP LYS LEU SER LEU GLU GLU LEU ASP ARG ARG LEU ASP
SEQRES  37 A  478  VAL LEU ALA MET ALA LYS VAL GLU ALA THR
SEQRES   1 B  478  GLY PRO GLY SER MET ALA HIS SER ALA HIS ASP ASP ALA
SEQRES   2 B  478  ASP ASN ASP THR GLU TYR ARG ILE GLU HIS ASP THR MET
SEQRES   3 B  478  GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES   4 B  478  GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES   5 B  478  ARG GLY LEU GLU ARG ALA GLN ILE ARG ALA LEU GLY LEU
SEQRES   6 B  478  LEU LYS GLY ALA CYS ALA GLN VAL ASN MET ASP LEU GLY
SEQRES   7 B  478  LEU LEU ALA PRO GLU LYS ALA GLU ALA ILE ILE ALA ALA
SEQRES   8 B  478  ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES   9 B  478  PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES  10 B  478  ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA GLY
SEQRES  11 B  478  ALA ASN GLY VAL ALA VAL HIS PRO ASN ASP ASP VAL ASN
SEQRES  12 B  478  MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES  13 B  478  HIS ILE ALA ALA THR GLU ALA ALA VAL SER HIS LEU ILE
SEQRES  14 B  478  PRO ALA LEU GLU ILE LEU GLN ASP ALA LEU ALA THR LYS
SEQRES  15 B  478  ALA LEU GLU TRP GLN SER VAL VAL LYS SER GLY ARG THR
SEQRES  16 B  478  HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES  17 B  478  PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES  18 B  478  ARG VAL ARG ALA THR LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES  19 B  478  ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES  20 B  478  GLU GLY PHE GLY VAL LYS VAL VAL SER VAL LEU VAL SER
SEQRES  21 B  478  GLN THR GLY LEU PRO GLN LEU ARG THR ALA ALA ASN SER
SEQRES  22 B  478  PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES  23 B  478  SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES  24 B  478  ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES  25 B  478  THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES  26 B  478  GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES  27 B  478  PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES  28 B  478  ASN ASP ALA ALA VAL ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES  29 B  478  PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES  30 B  478  ILE LEU GLU SER PHE THR LEU LEU THR ASN VAL SER LYS
SEQRES  31 B  478  LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES  32 B  478  ALA GLU HIS LEU ARG GLU LEU ALA GLU SER SER PRO SER
SEQRES  33 B  478  ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES  34 B  478  ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES  35 B  478  THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES  36 B  478  ASP LYS LEU SER LEU GLU GLU LEU ASP ARG ARG LEU ASP
SEQRES  37 B  478  VAL LEU ALA MET ALA LYS VAL GLU ALA THR
SEQRES   1 C  478  GLY PRO GLY SER MET ALA HIS SER ALA HIS ASP ASP ALA
SEQRES   2 C  478  ASP ASN ASP THR GLU TYR ARG ILE GLU HIS ASP THR MET
SEQRES   3 C  478  GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES   4 C  478  GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES   5 C  478  ARG GLY LEU GLU ARG ALA GLN ILE ARG ALA LEU GLY LEU
SEQRES   6 C  478  LEU LYS GLY ALA CYS ALA GLN VAL ASN MET ASP LEU GLY
SEQRES   7 C  478  LEU LEU ALA PRO GLU LYS ALA GLU ALA ILE ILE ALA ALA
SEQRES   8 C  478  ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES   9 C  478  PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES  10 C  478  ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA GLY
SEQRES  11 C  478  ALA ASN GLY VAL ALA VAL HIS PRO ASN ASP ASP VAL ASN
SEQRES  12 C  478  MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES  13 C  478  HIS ILE ALA ALA THR GLU ALA ALA VAL SER HIS LEU ILE
SEQRES  14 C  478  PRO ALA LEU GLU ILE LEU GLN ASP ALA LEU ALA THR LYS
SEQRES  15 C  478  ALA LEU GLU TRP GLN SER VAL VAL LYS SER GLY ARG THR
SEQRES  16 C  478  HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES  17 C  478  PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES  18 C  478  ARG VAL ARG ALA THR LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES  19 C  478  ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES  20 C  478  GLU GLY PHE GLY VAL LYS VAL VAL SER VAL LEU VAL SER
SEQRES  21 C  478  GLN THR GLY LEU PRO GLN LEU ARG THR ALA ALA ASN SER
SEQRES  22 C  478  PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES  23 C  478  SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES  24 C  478  ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES  25 C  478  THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES  26 C  478  GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES  27 C  478  PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES  28 C  478  ASN ASP ALA ALA VAL ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES  29 C  478  PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES  30 C  478  ILE LEU GLU SER PHE THR LEU LEU THR ASN VAL SER LYS
SEQRES  31 C  478  LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES  32 C  478  ALA GLU HIS LEU ARG GLU LEU ALA GLU SER SER PRO SER
SEQRES  33 C  478  ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES  34 C  478  ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES  35 C  478  THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES  36 C  478  ASP LYS LEU SER LEU GLU GLU LEU ASP ARG ARG LEU ASP
SEQRES  37 C  478  VAL LEU ALA MET ALA LYS VAL GLU ALA THR
SEQRES   1 D  478  GLY PRO GLY SER MET ALA HIS SER ALA HIS ASP ASP ALA
SEQRES   2 D  478  ASP ASN ASP THR GLU TYR ARG ILE GLU HIS ASP THR MET
SEQRES   3 D  478  GLY GLU VAL ARG VAL PRO ALA LYS ALA LEU TRP ARG ALA
SEQRES   4 D  478  GLN THR GLN ARG ALA VAL GLU ASN PHE PRO ILE SER GLY
SEQRES   5 D  478  ARG GLY LEU GLU ARG ALA GLN ILE ARG ALA LEU GLY LEU
SEQRES   6 D  478  LEU LYS GLY ALA CYS ALA GLN VAL ASN MET ASP LEU GLY
SEQRES   7 D  478  LEU LEU ALA PRO GLU LYS ALA GLU ALA ILE ILE ALA ALA
SEQRES   8 D  478  ALA ALA GLU ILE ALA ASP GLY GLN HIS ASP ASP GLN PHE
SEQRES   9 D  478  PRO ILE ASP VAL PHE GLN THR GLY SER GLY THR SER SER
SEQRES  10 D  478  ASN MET ASN THR ASN GLU VAL ILE ALA SER ILE ALA GLY
SEQRES  11 D  478  ALA ASN GLY VAL ALA VAL HIS PRO ASN ASP ASP VAL ASN
SEQRES  12 D  478  MET SER GLN SER SER ASN ASP THR PHE PRO THR ALA THR
SEQRES  13 D  478  HIS ILE ALA ALA THR GLU ALA ALA VAL SER HIS LEU ILE
SEQRES  14 D  478  PRO ALA LEU GLU ILE LEU GLN ASP ALA LEU ALA THR LYS
SEQRES  15 D  478  ALA LEU GLU TRP GLN SER VAL VAL LYS SER GLY ARG THR
SEQRES  16 D  478  HIS LEU MET ASP ALA VAL PRO VAL THR LEU GLY GLN GLU
SEQRES  17 D  478  PHE SER GLY TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU
SEQRES  18 D  478  ARG VAL ARG ALA THR LEU PRO ARG LEU GLY GLU LEU ALA
SEQRES  19 D  478  ILE GLY GLY THR ALA VAL GLY THR GLY LEU ASN ALA PRO
SEQRES  20 D  478  GLU GLY PHE GLY VAL LYS VAL VAL SER VAL LEU VAL SER
SEQRES  21 D  478  GLN THR GLY LEU PRO GLN LEU ARG THR ALA ALA ASN SER
SEQRES  22 D  478  PHE GLU ALA GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA
SEQRES  23 D  478  SER GLY ALA LEU ARG THR ILE ALA VAL SER LEU THR LYS
SEQRES  24 D  478  ILE ALA ASN ASP ILE ARG TRP MET GLY SER GLY PRO LEU
SEQRES  25 D  478  THR GLY LEU ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO
SEQRES  26 D  478  GLY SER SER ILE MET PRO GLY LYS VAL ASN PRO VAL LEU
SEQRES  27 D  478  PRO GLU ALA VAL THR GLN VAL ALA ALA GLN VAL ILE GLY
SEQRES  28 D  478  ASN ASP ALA ALA VAL ALA TRP GLY GLY ALA ASN GLY ALA
SEQRES  29 D  478  PHE GLU LEU ASN VAL TYR ILE PRO MET MET ALA ARG ASN
SEQRES  30 D  478  ILE LEU GLU SER PHE THR LEU LEU THR ASN VAL SER LYS
SEQRES  31 D  478  LEU PHE ALA GLN ARG CYS ILE ALA GLY LEU THR ALA ASN
SEQRES  32 D  478  ALA GLU HIS LEU ARG GLU LEU ALA GLU SER SER PRO SER
SEQRES  33 D  478  ILE VAL THR PRO LEU ASN SER ALA ILE GLY TYR GLU GLU
SEQRES  34 D  478  ALA ALA ALA VAL ALA LYS GLN ALA LEU LYS GLU ARG LYS
SEQRES  35 D  478  THR ILE ARG GLN THR VAL ILE ASP ARG GLY LEU ILE GLY
SEQRES  36 D  478  ASP LYS LEU SER LEU GLU GLU LEU ASP ARG ARG LEU ASP
SEQRES  37 D  478  VAL LEU ALA MET ALA LYS VAL GLU ALA THR
FORMUL   5  HOH   *1684(H2 O)
HELIX    1   1 ARG A   34  PHE A   44  1                                  11
HELIX    2   2 GLU A   52  LEU A   73  1                                  22
HELIX    3   3 ALA A   77  ASP A   93  1                                  17
HELIX    4   4 GLY A  110  ASN A  128  1                                  19
HELIX    5   5 ASP A  146  HIS A  163  1                                  18
HELIX    6   6 HIS A  163  TRP A  182  1                                  20
HELIX    7   7 LEU A  201  GLY A  227  1                                  27
HELIX    8   8 GLY A  245  GLY A  259  1                                  15
HELIX    9   9 PHE A  270  ALA A  275  1                                   6
HELIX   10  10 ARG A  276  GLY A  304  1                                  29
HELIX   11  11 PRO A  332  ASN A  358  1                                  27
HELIX   12  12 TYR A  366  CYS A  392  1                                  27
HELIX   13  13 ASN A  399  GLU A  408  1                                  10
HELIX   14  14 SER A  409  PRO A  416  5                                   8
HELIX   15  15 LEU A  417  ARG A  437  1                                  21
HELIX   16  16 THR A  439  ARG A  447  1                                   9
HELIX   17  17 SER A  455  LEU A  463  1                                   9
HELIX   18  18 ASP A  464  ALA A  469  1                                   6
HELIX   19  19 ARG B   34  PHE B   44  1                                  11
HELIX   20  20 GLU B   52  LEU B   73  1                                  22
HELIX   21  21 ALA B   77  ASP B   93  1                                  17
HELIX   22  22 HIS B   96  PHE B  100  5                                   5
HELIX   23  23 GLY B  110  ASN B  128  1                                  19
HELIX   24  24 SER B  143  HIS B  163  1                                  21
HELIX   25  25 HIS B  163  TRP B  182  1                                  20
HELIX   26  26 LEU B  201  GLY B  227  1                                  27
HELIX   27  27 GLY B  245  GLY B  259  1                                  15
HELIX   28  28 PHE B  270  ALA B  275  1                                   6
HELIX   29  29 ARG B  276  GLY B  304  1                                  29
HELIX   30  30 PRO B  332  ASN B  358  1                                  27
HELIX   31  31 TYR B  366  CYS B  392  1                                  27
HELIX   32  32 ASN B  399  GLU B  408  1                                  10
HELIX   33  33 SER B  409  PRO B  416  5                                   8
HELIX   34  34 LEU B  417  GLY B  422  1                                   6
HELIX   35  35 GLY B  422  GLU B  436  1                                  15
HELIX   36  36 THR B  439  ARG B  447  1                                   9
HELIX   37  37 SER B  455  LEU B  463  1                                   9
HELIX   38  38 ASP B  464  LYS B  470  1                                   7
HELIX   39  39 ARG C   34  PHE C   44  1                                  11
HELIX   40  40 GLU C   52  LEU C   73  1                                  22
HELIX   41  41 ALA C   77  ASP C   93  1                                  17
HELIX   42  42 HIS C   96  PHE C  100  5                                   5
HELIX   43  43 GLY C  110  ASN C  128  1                                  19
HELIX   44  44 SER C  143  HIS C  163  1                                  21
HELIX   45  45 HIS C  163  TRP C  182  1                                  20
HELIX   46  46 LEU C  201  GLY C  227  1                                  27
HELIX   47  47 GLY C  245  GLY C  259  1                                  15
HELIX   48  48 PHE C  270  ALA C  275  1                                   6
HELIX   49  49 ARG C  276  SER C  305  1                                  30
HELIX   50  50 PRO C  332  ASN C  358  1                                  27
HELIX   51  51 TYR C  366  CYS C  392  1                                  27
HELIX   52  52 ASN C  399  GLU C  408  1                                  10
HELIX   53  53 SER C  409  PRO C  416  5                                   8
HELIX   54  54 LEU C  417  ARG C  437  1                                  21
HELIX   55  55 THR C  439  ARG C  447  1                                   9
HELIX   56  56 SER C  455  LEU C  463  1                                   9
HELIX   57  57 ASP C  464  ALA C  469  1                                   6
HELIX   58  58 ARG D   34  PHE D   44  1                                  11
HELIX   59  59 GLU D   52  LEU D   73  1                                  22
HELIX   60  60 ALA D   77  ASP D   93  1                                  17
HELIX   61  61 GLY D  110  ASN D  128  1                                  19
HELIX   62  62 SER D  143  HIS D  163  1                                  21
HELIX   63  63 HIS D  163  TRP D  182  1                                  20
HELIX   64  64 LEU D  201  GLY D  227  1                                  27
HELIX   65  65 GLY D  245  GLY D  259  1                                  15
HELIX   66  66 PHE D  270  ALA D  275  1                                   6
HELIX   67  67 ARG D  276  GLY D  304  1                                  29
HELIX   68  68 PRO D  332  ASN D  358  1                                  27
HELIX   69  69 TYR D  366  CYS D  392  1                                  27
HELIX   70  70 ASN D  399  GLU D  408  1                                  10
HELIX   71  71 SER D  409  PRO D  416  5                                   8
HELIX   72  72 LEU D  417  GLY D  422  1                                   6
HELIX   73  73 GLY D  422  ARG D  437  1                                  16
HELIX   74  74 THR D  439  ARG D  447  1                                   9
HELIX   75  75 SER D  455  LEU D  463  1                                   9
HELIX   76  76 ASP D  464  LYS D  470  1                                   7
SHEET    1   A 2 VAL A 186  THR A 191  0
SHEET    2   A 2 MET A 194  THR A 200 -1  O  VAL A 199   N  LYS A 187
SHEET    1   B 2 GLU A 228  LEU A 229  0
SHEET    2   B 2 ARG A 264  THR A 265  1  O  ARG A 264   N  LEU A 229
SHEET    1   C 2 ILE A 314  GLN A 315  0
SHEET    2   C 2 THR A 397  ALA A 398 -1  O  THR A 397   N  GLN A 315
SHEET    1   D 2 VAL B 186  THR B 191  0
SHEET    2   D 2 MET B 194  THR B 200 -1  O  VAL B 199   N  LYS B 187
SHEET    1   E 2 GLU B 228  LEU B 229  0
SHEET    2   E 2 ARG B 264  THR B 265  1  O  ARG B 264   N  LEU B 229
SHEET    1   F 2 ILE B 314  GLN B 315  0
SHEET    2   F 2 THR B 397  ALA B 398 -1  O  THR B 397   N  GLN B 315
SHEET    1   G 2 VAL C 186  THR C 191  0
SHEET    2   G 2 MET C 194  THR C 200 -1  O  VAL C 199   N  LYS C 187
SHEET    1   H 2 GLU C 228  LEU C 229  0
SHEET    2   H 2 ARG C 264  THR C 265  1  O  ARG C 264   N  LEU C 229
SHEET    1   I 2 ILE C 314  GLN C 315  0
SHEET    2   I 2 THR C 397  ALA C 398 -1  O  THR C 397   N  GLN C 315
SHEET    1   J 2 VAL D 186  THR D 191  0
SHEET    2   J 2 MET D 194  THR D 200 -1  O  VAL D 199   N  LYS D 187
SHEET    1   K 2 GLU D 228  LEU D 229  0
SHEET    2   K 2 ARG D 264  THR D 265  1  O  ARG D 264   N  LEU D 229
SHEET    1   L 2 ILE D 314  GLN D 315  0
SHEET    2   L 2 THR D 397  ALA D 398 -1  O  THR D 397   N  GLN D 315
CISPEP   1 GLY A  306    PRO A  307          0         4.46
CISPEP   2 GLY B  306    PRO B  307          0         6.96
CISPEP   3 GLY C  306    PRO C  307          0         3.35
CISPEP   4 GLY D  306    PRO D  307          0         3.12
CRYST1   97.880  114.080   98.840  90.00 107.01  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      0.010217  0.000000  0.003125        0.00000
SCALE2      0.000000  0.008766  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010580        0.00000
      
PROCHECK
Go to PROCHECK summary
 References