spacer
spacer

PDBsum entry 3zge

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
3zge
Jmol
Contents
Protein chains
916 a.a.
Ligands
ASP ×2
SO4 ×2
EDO ×2
Waters ×198
HEADER    LYASE                                   17-DEC-12   3ZGE
TITLE     GREATER EFFICIENCY OF PHOTOSYNTHETIC CARBON FIXATION DUE TO
TITLE    2 SINGLE AMINO ACID SUBSTITUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: C4 PHOSPHOENOLPYRUVATE CARBOXYLASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: C4 PEPC, C4 PEPCASE, PPCA, PHOTOSYNTHETIC PEPCASE;
COMPND   5 EC: 4.1.1.31;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: FLAVERIA TRINERVIA;
SOURCE   3 ORGANISM_TAXID: 4227;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PETEV16B
KEYWDS    LYASE, C4 PHOTOSYNTHETIC PATHWAY, CARBON FIXATION, PEP CARBOXYLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.K.PAULUS,D.SCHLIEPER,G.GROTH
REVDAT   2   13-MAR-13 3ZGE    1       JRNL
REVDAT   1   27-FEB-13 3ZGE    0
JRNL        AUTH   J.K.PAULUS,D.SCHLIEPER,G.GROTH
JRNL        TITL   GREATER EFFICIENCY OF PHOTOSYNTHETIC CARBON FIXATION DUE TO
JRNL        TITL 2 SINGLE AMINO ACID SUBSTITUTION
JRNL        REF    NAT.COMMUN.                   V.   4  1518 2013
JRNL        REFN                   ISSN 2041-1723
JRNL        PMID   23443546
JRNL        DOI    10.1038/NCOMMS2504
REMARK   2
REMARK   2 RESOLUTION.    2.49 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) : 2.49
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.63
REMARK   3   NUMBER OF REFLECTIONS             : 90203
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) : 0.20425
REMARK   3   R VALUE            (WORKING SET) : 0.20358
REMARK   3   FREE R VALUE                     : 0.23719
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1845
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) : 2.490
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.554
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6235
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK   3   BIN R VALUE           (WORKING SET) : 0.241
REMARK   3   BIN FREE R VALUE SET COUNT          : 112
REMARK   3   BIN FREE R VALUE                    : 0.292
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 14710
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 36
REMARK   3   SOLVENT ATOMS            : 198
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 45.2
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.521
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.37
REMARK   3    B22 (A**2) : -0.09
REMARK   3    B33 (A**2) : -0.27
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.358
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.242
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.171
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.145
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15045 ; 0.017 ; 0.019
REMARK   3   BOND LENGTHS OTHERS               (A): 10500 ; 0.005 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20334 ; 1.794 ; 1.972
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 25494 ; 1.204 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1815 ; 5.902 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   729 ;34.370 ;23.717
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2710 ;16.890 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   127 ;17.039 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2241 ; 0.098 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16551 ; 0.009 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  3080 ; 0.004 ; 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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : 1
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 5
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     8        A   223
REMARK   3    ORIGIN FOR THE GROUP (A):  97.6503  10.8188 102.5361
REMARK   3    T TENSOR
REMARK   3      T11:   0.1047 T22:   0.2066
REMARK   3      T33:   0.1503 T12:  -0.0745
REMARK   3      T13:   0.0110 T23:  -0.0091
REMARK   3    L TENSOR
REMARK   3      L11:   1.5302 L22:   1.6533
REMARK   3      L33:   0.6156 L12:  -0.5153
REMARK   3      L13:   0.0500 L23:  -0.0186
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0928 S12:  -0.1094 S13:  -0.2824
REMARK   3      S21:   0.2223 S22:   0.1015 S23:  -0.1334
REMARK   3      S31:   0.0287 S32:   0.1210 S33:  -0.0087
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 :   A   224        A   704
REMARK   3    ORIGIN FOR THE GROUP (A):  83.7128  27.2863  79.3709
REMARK   3    T TENSOR
REMARK   3      T11:   0.1038 T22:   0.1526
REMARK   3      T33:   0.0668 T12:  -0.0468
REMARK   3      T13:  -0.0546 T23:   0.0226
REMARK   3    L TENSOR
REMARK   3      L11:   0.4994 L22:   1.1930
REMARK   3      L33:   0.9885 L12:   0.0781
REMARK   3      L13:   0.0281 L23:  -0.6096
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0077 S12:   0.1074 S13:  -0.0701
REMARK   3      S21:  -0.2412 S22:   0.0131 S23:   0.1384
REMARK   3      S31:   0.0436 S32:  -0.0356 S33:  -0.0054
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 :   A   705        A   966
REMARK   3    ORIGIN FOR THE GROUP (A): 111.0884  30.6068 100.9383
REMARK   3    T TENSOR
REMARK   3      T11:   0.1058 T22:   0.2268
REMARK   3      T33:   0.0775 T12:  -0.1444
REMARK   3      T13:  -0.0395 T23:   0.0304
REMARK   3    L TENSOR
REMARK   3      L11:   2.0955 L22:   2.1835
REMARK   3      L33:   1.1589 L12:  -0.3623
REMARK   3      L13:  -0.0081 L23:  -0.0830
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0707 S12:   0.0558 S13:   0.0087
REMARK   3      S21:   0.0197 S22:  -0.0310 S23:  -0.2967
REMARK   3      S31:  -0.1756 S32:   0.2258 S33:   0.1017
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 :   B     8        B   223
REMARK   3    ORIGIN FOR THE GROUP (A):  69.0347  15.9442 135.3563
REMARK   3    T TENSOR
REMARK   3      T11:   0.0894 T22:   0.1081
REMARK   3      T33:   0.1430 T12:   0.0429
REMARK   3      T13:   0.0407 T23:  -0.0019
REMARK   3    L TENSOR
REMARK   3      L11:   1.5914 L22:   1.0818
REMARK   3      L33:   0.5890 L12:   0.4622
REMARK   3      L13:   0.0293 L23:   0.0169
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0749 S12:   0.2244 S13:  -0.1561
REMARK   3      S21:  -0.1209 S22:   0.0546 S23:   0.1939
REMARK   3      S31:   0.0043 S32:  -0.1262 S33:   0.0203
REMARK   3
REMARK   3   TLS GROUP :     5
REMARK   3    NUMBER OF COMPONENTS GROUP :    1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   224        B   704
REMARK   3    ORIGIN FOR THE GROUP (A):  88.2266  26.7190 158.2517
REMARK   3    T TENSOR
REMARK   3      T11:   0.0726 T22:   0.0433
REMARK   3      T33:   0.1025 T12:  -0.0044
REMARK   3      T13:  -0.0202 T23:   0.0330
REMARK   3    L TENSOR
REMARK   3      L11:   0.3219 L22:   1.4517
REMARK   3      L33:   0.6698 L12:   0.0051
REMARK   3      L13:   0.1819 L23:   0.6245
REMARK   3    S TENSOR
REMARK   3      S11:   0.0356 S12:  -0.0592 S13:  -0.1490
REMARK   3      S21:   0.2552 S22:   0.0376 S23:  -0.1010
REMARK   3      S31:   0.0955 S32:   0.0034 S33:  -0.0733
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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
REMARK   3   RIDING POSITIONS. U VALUES WITH TLS ADDED
REMARK   4
REMARK   4 3ZGE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-12.
REMARK 100 THE PDBE ID CODE IS EBI-55163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : BM14
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (MX-225)
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90203
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.49
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.83
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 26.2
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.097
REMARK 200   FOR THE DATA SET  : 5.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.62
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 24
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.389
REMARK 200   FOR SHELL         : 5.90
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 1JQO
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M
REMARK 280  TRI-SODIUM CITRATE/HCL PH 5.6, 15 % PEG 4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-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        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       81.26000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.05500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       81.26000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.05500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 167740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY:  19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      162.52000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       -0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.6 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   BIOMT1   2 -1.000000  0.000000  0.000000      162.52000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000       -0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.9 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   BIOMT1   2 -1.000000  0.000000  0.000000      162.52000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A   -23
REMARK 465     GLY A   -22
REMARK 465     HIS A   -21
REMARK 465     HIS A   -20
REMARK 465     HIS 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     HIS A   -12
REMARK 465     SER A   -11
REMARK 465     SER A   -10
REMARK 465     GLY A    -9
REMARK 465     HIS A    -8
REMARK 465     GLU A    -7
REMARK 465     ASN A    -6
REMARK 465     LEU A    -5
REMARK 465     TYR A    -4
REMARK 465     PHE A    -3
REMARK 465     GLN A    -2
REMARK 465     GLY A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     ASN A     3
REMARK 465     ARG A     4
REMARK 465     ASN A     5
REMARK 465     VAL A     6
REMARK 465     GLU A     7
REMARK 465     LYS A   198
REMARK 465     ALA A   345
REMARK 465     ARG A   346
REMARK 465     LYS A   347
REMARK 465     ASP A   348
REMARK 465     VAL A   349
REMARK 465     LYS A   350
REMARK 465     MET A   748
REMARK 465     ASN A   749
REMARK 465     ILE A   750
REMARK 465     GLY A   751
REMARK 465     SER A   752
REMARK 465     ARG A   753
REMARK 465     PRO A   754
REMARK 465     SER A   755
REMARK 465     LYS A   756
REMARK 465     ARG A   757
REMARK 465     LYS A   758
REMARK 465     PRO A   759
REMARK 465     SER A   760
REMARK 465     TYR A   923
REMARK 465     ALA A   924
REMARK 465     ALA A   925
REMARK 465     GLU A   926
REMARK 465     PRO A   927
REMARK 465     SER A   928
REMARK 465     LYS A   929
REMARK 465     PRO A   930
REMARK 465     ALA A   931
REMARK 465     ASP A   932
REMARK 465     GLU A   933
REMARK 465     LEU A   934
REMARK 465     ILE A   935
REMARK 465     HIS A   936
REMARK 465     LEU A   937
REMARK 465     ASN A   938
REMARK 465     PRO A   939
REMARK 465     THR A   940
REMARK 465     SER A   941
REMARK 465     GLU A   942
REMARK 465     TYR A   943
REMARK 465     ALA A   944
REMARK 465     PRO A   945
REMARK 465     MET B   -23
REMARK 465     GLY B   -22
REMARK 465     HIS B   -21
REMARK 465     HIS B   -20
REMARK 465     HIS 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     HIS B   -12
REMARK 465     SER B   -11
REMARK 465     SER B   -10
REMARK 465     GLY B    -9
REMARK 465     HIS B    -8
REMARK 465     GLU B    -7
REMARK 465     ASN B    -6
REMARK 465     LEU B    -5
REMARK 465     TYR B    -4
REMARK 465     PHE B    -3
REMARK 465     GLN B    -2
REMARK 465     GLY B    -1
REMARK 465     HIS B     0
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     ASN B     3
REMARK 465     ARG B     4
REMARK 465     ASN B     5
REMARK 465     VAL B     6
REMARK 465     GLU B     7
REMARK 465     LYS B   198
REMARK 465     ASP B   199
REMARK 465     ILE B   225
REMARK 465     ARG B   226
REMARK 465     ARG B   227
REMARK 465     CYS B   330
REMARK 465     ARG B   343
REMARK 465     THR B   344
REMARK 465     ALA B   345
REMARK 465     ARG B   346
REMARK 465     LYS B   347
REMARK 465     ASP B   348
REMARK 465     VAL B   349
REMARK 465     MET B   748
REMARK 465     ASN B   749
REMARK 465     ILE B   750
REMARK 465     GLY B   751
REMARK 465     SER B   752
REMARK 465     ARG B   753
REMARK 465     PRO B   754
REMARK 465     SER B   755
REMARK 465     LYS B   756
REMARK 465     ARG B   757
REMARK 465     LYS B   758
REMARK 465     PRO B   759
REMARK 465     SER B   760
REMARK 465     GLU B   922
REMARK 465     TYR B   923
REMARK 465     ALA B   924
REMARK 465     ALA B   925
REMARK 465     GLU B   926
REMARK 465     PRO B   927
REMARK 465     SER B   928
REMARK 465     LYS B   929
REMARK 465     PRO B   930
REMARK 465     ALA B   931
REMARK 465     ASP B   932
REMARK 465     GLU B   933
REMARK 465     LEU B   934
REMARK 465     ILE B   935
REMARK 465     HIS B   936
REMARK 465     LEU B   937
REMARK 465     ASN B   938
REMARK 465     PRO B   939
REMARK 465     THR B   940
REMARK 465     SER B   941
REMARK 465     GLU B   942
REMARK 465     TYR B   943
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    GLU B 859   CD    GLU B 859   OE1     0.072
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    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 288   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 288   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 584   CG  -  CD  -  NE  ANGL. DEV. = -13.0 DEGREES
REMARK 500    ARG A 635   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 663   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A 663   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    MET A 711   CG  -  SD  -  CE  ANGL. DEV. = -12.4 DEGREES
REMARK 500    ARG A 817   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ASP B  28   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG B 144   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG B 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG B 288   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES
REMARK 500    ARG B 288   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    CYS B 420   CA  -  CB  -  SG  ANGL. DEV. =   7.2 DEGREES
REMARK 500    LEU B 444   CB  -  CG  -  CD1 ANGL. DEV. = -16.8 DEGREES
REMARK 500    ARG B 584   CG  -  CD  -  NE  ANGL. DEV. = -14.2 DEGREES
REMARK 500    ARG B 663   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES
REMARK 500    ARG B 663   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    MET B 711   CG  -  SD  -  CE  ANGL. DEV. = -18.3 DEGREES
REMARK 500    PRO B 945   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    LYS A  23       70.25    -69.90
REMARK 500    VAL A  24       81.22    -65.06
REMARK 500    GLN A 175       95.25    177.47
REMARK 500    ASP A 223       33.42   -143.74
REMARK 500    THR A 246      -40.05   -138.22
REMARK 500    ASN A 268       43.78   -109.91
REMARK 500    GLN A 363       65.18   -115.33
REMARK 500    LEU A 444      -50.99    -29.46
REMARK 500    ASN A 698       69.70   -150.47
REMARK 500    ASP A 799      117.24   -160.78
REMARK 500    PRO A 909       16.51    -69.69
REMARK 500    HIS A 918      126.43    -35.46
REMARK 500    GLN A 963     -132.18     49.42
REMARK 500    THR A 965      -94.73   -135.06
REMARK 500    VAL B  24       79.91    -64.96
REMARK 500    GLN B 175       93.03    177.53
REMARK 500    ASP B 223       33.32   -140.69
REMARK 500    THR B 246      -39.12   -143.69
REMARK 500    ASN B 268       41.26   -109.78
REMARK 500    ASN B 291       83.95   -150.82
REMARK 500    HIS B 351       38.01    -83.52
REMARK 500    GLN B 363       65.94   -117.22
REMARK 500    LEU B 444      -51.37    -29.36
REMARK 500    ASN B 698       69.36   -152.34
REMARK 500    ASP B 799      115.86   -162.67
REMARK 500    HIS B 918      127.21    -33.67
REMARK 500    GLN B 963     -132.86     48.98
REMARK 500    THR B 965      -97.08   -136.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP A1967
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1968
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1969
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP B1967
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1968
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1969
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZGB   RELATED DB: PDB
REMARK 900  GREATER EFFICIENCY OF PHOTOSYNTHETIC CARBON FIXATION DUE
REMARK 900  TO SINGLE AMINO ACID SUBSTITUTION
DBREF  3ZGE A    1   966  UNP    P30694   CAPPA_FLATR      1    966
DBREF  3ZGE B    1   966  UNP    P30694   CAPPA_FLATR      1    966
SEQADV 3ZGE MET A  -23  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLY A  -22  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -21  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -20  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -19  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -18  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -17  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -16  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -15  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -14  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -13  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A  -12  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE SER A  -11  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE SER A  -10  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLY A   -9  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A   -8  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLU A   -7  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE ASN A   -6  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE LEU A   -5  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE TYR A   -4  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE PHE A   -3  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLN A   -2  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLY A   -1  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS A    0  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE MET B  -23  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLY B  -22  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -21  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -20  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -19  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -18  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -17  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -16  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -15  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -14  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -13  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B  -12  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE SER B  -11  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE SER B  -10  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLY B   -9  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B   -8  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLU B   -7  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE ASN B   -6  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE LEU B   -5  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE TYR B   -4  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE PHE B   -3  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLN B   -2  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE GLY B   -1  UNP  P30694              EXPRESSION TAG
SEQADV 3ZGE HIS B    0  UNP  P30694              EXPRESSION TAG
SEQRES   1 A  990  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 A  990  SER GLY HIS GLU ASN LEU TYR PHE GLN GLY HIS MET ALA
SEQRES   3 A  990  ASN ARG ASN VAL GLU LYS LEU ALA SER ILE ASP ALA GLN
SEQRES   4 A  990  LEU ARG LEU LEU VAL PRO GLY LYS VAL SER GLU ASP ASP
SEQRES   5 A  990  LYS LEU VAL GLU TYR ASP ALA LEU LEU LEU ASP LYS PHE
SEQRES   6 A  990  LEU ASP ILE LEU GLN ASP LEU HIS GLY GLU ASP LEU LYS
SEQRES   7 A  990  GLU ALA VAL GLN GLN CYS TYR GLU LEU SER ALA GLU TYR
SEQRES   8 A  990  GLU GLY LYS HIS ASP PRO LYS LYS LEU GLU GLU LEU GLY
SEQRES   9 A  990  SER LEU LEU THR SER LEU ASP THR GLY ASP SER ILE VAL
SEQRES  10 A  990  ILE ALA LYS ALA PHE SER HIS MET LEU ASN LEU ALA ASN
SEQRES  11 A  990  LEU ALA GLU GLU LEU GLN ILE ALA TYR ARG ARG ARG ILE
SEQRES  12 A  990  LYS LEU LYS SER GLY ASP PHE ALA ASP GLU ALA ASN ALA
SEQRES  13 A  990  THR THR GLU SER ASP ILE GLU GLU THR PHE LYS ARG LEU
SEQRES  14 A  990  VAL HIS LYS LEU ASN LYS SER PRO GLU GLU VAL PHE ASP
SEQRES  15 A  990  ALA LEU LYS ASN GLN THR VAL GLU LEU VAL LEU THR ALA
SEQRES  16 A  990  HIS PRO THR GLN SER VAL ARG ARG SER LEU LEU GLN LYS
SEQRES  17 A  990  HIS GLY ARG ILE ARG ASN CYS LEU ALA GLN LEU TYR ALA
SEQRES  18 A  990  LYS ASP ILE THR PRO ASP ASP LYS GLN GLU LEU ASP GLU
SEQRES  19 A  990  ALA LEU HIS ARG GLU ILE GLN ALA ALA PHE ARG THR ASP
SEQRES  20 A  990  GLU ILE ARG ARG THR PRO PRO THR PRO GLN ASP GLU MET
SEQRES  21 A  990  ARG ALA GLY MET SER TYR PHE HIS GLU THR ILE TRP LYS
SEQRES  22 A  990  GLY VAL PRO LYS PHE LEU ARG ARG VAL ASP THR ALA LEU
SEQRES  23 A  990  LYS ASN ILE GLY ILE ASN GLU ARG PHE PRO TYR ASN ALA
SEQRES  24 A  990  PRO LEU ILE GLN PHE SER SER TRP MET GLY GLY ASP ARG
SEQRES  25 A  990  ASP GLY ASN PRO ARG VAL THR PRO GLU VAL THR ARG ASP
SEQRES  26 A  990  VAL CYS LEU LEU ALA ARG MET MET THR SER ASN MET TYR
SEQRES  27 A  990  PHE SER GLN ILE GLU ASP LEU MET ILE GLU MET SER MET
SEQRES  28 A  990  TRP ARG CYS ASN SER GLU LEU ARG VAL ARG ALA GLU GLU
SEQRES  29 A  990  LEU TYR ARG THR ALA ARG LYS ASP VAL LYS HIS TYR ILE
SEQRES  30 A  990  GLU PHE TRP LYS ARG ILE PRO PRO ASN GLN PRO TYR ARG
SEQRES  31 A  990  VAL ILE LEU GLY ASP VAL ARG ASP LYS LEU TYR ASN THR
SEQRES  32 A  990  ARG GLU ARG SER ARG HIS LEU LEU VAL ASP GLY LYS SER
SEQRES  33 A  990  ASP ILE PRO ASP GLU ALA VAL TYR THR ASN VAL GLU GLN
SEQRES  34 A  990  LEU LEU GLU PRO LEU GLU LEU CYS TYR ARG SER LEU CYS
SEQRES  35 A  990  ASP CYS GLY ASP HIS VAL ILE ALA ASP GLY SER LEU LEU
SEQRES  36 A  990  ASP PHE LEU ARG GLN VAL SER THR PHE GLY LEU SER LEU
SEQRES  37 A  990  VAL LYS LEU ASP ILE ARG GLN GLU SER ASP ARG HIS THR
SEQRES  38 A  990  GLU VAL LEU ASP ALA ILE THR GLN HIS LEU GLY ILE GLY
SEQRES  39 A  990  SER TYR ARG GLU TRP SER GLU GLU LYS ARG GLN GLU TRP
SEQRES  40 A  990  LEU LEU ALA GLU LEU SER GLY LYS ARG PRO LEU ILE GLY
SEQRES  41 A  990  PRO ASP LEU PRO LYS THR GLU GLU VAL LYS ASP CYS LEU
SEQRES  42 A  990  ASP THR PHE LYS VAL LEU ALA GLU LEU PRO SER ASP CYS
SEQRES  43 A  990  PHE GLY ALA TYR ILE ILE SER MET ALA THR SER THR SER
SEQRES  44 A  990  ASP VAL LEU ALA VAL GLU LEU LEU GLN ARG GLU TYR HIS
SEQRES  45 A  990  ILE LYS HIS PRO LEU ARG VAL VAL PRO LEU PHE GLU LYS
SEQRES  46 A  990  LEU ALA ASP LEU GLU ALA ALA PRO ALA ALA MET THR ARG
SEQRES  47 A  990  LEU PHE SER MET ASP TRP TYR ARG ASN ARG ILE ASP GLY
SEQRES  48 A  990  LYS GLN GLU VAL MET ILE GLY TYR SER ASP SER GLY LYS
SEQRES  49 A  990  ASP ALA GLY ARG PHE SER ALA ALA TRP GLN LEU TYR LYS
SEQRES  50 A  990  THR GLN GLU GLN ILE VAL LYS ILE ALA LYS GLU PHE GLY
SEQRES  51 A  990  VAL LYS LEU VAL ILE PHE HIS GLY ARG GLY GLY THR VAL
SEQRES  52 A  990  GLY ARG GLY GLY GLY PRO THR HIS LEU ALA LEU LEU SER
SEQRES  53 A  990  GLN PRO PRO ASP THR ILE ASN GLY SER LEU ARG VAL THR
SEQRES  54 A  990  VAL GLN GLY GLU VAL ILE GLU GLN SER PHE GLY GLU GLU
SEQRES  55 A  990  HIS LEU CYS PHE ARG THR LEU GLN ARG PHE CYS ALA ALA
SEQRES  56 A  990  THR LEU GLU HIS GLY MET ASN PRO PRO ILE SER PRO ARG
SEQRES  57 A  990  PRO GLU TRP ARG GLU LEU MET ASP GLN MET ALA VAL VAL
SEQRES  58 A  990  ALA THR GLU GLU TYR ARG SER VAL VAL PHE LYS GLU PRO
SEQRES  59 A  990  ARG PHE VAL GLU TYR PHE ARG LEU ALA THR PRO GLU LEU
SEQRES  60 A  990  GLU PHE GLY ARG MET ASN ILE GLY SER ARG PRO SER LYS
SEQRES  61 A  990  ARG LYS PRO SER GLY GLY ILE GLU SER LEU ARG ALA ILE
SEQRES  62 A  990  PRO TRP ILE PHE SER TRP THR GLN THR ARG PHE HIS LEU
SEQRES  63 A  990  PRO VAL TRP LEU GLY PHE GLY ALA ALA PHE LYS HIS ALA
SEQRES  64 A  990  ILE GLN LYS ASP SER LYS ASN LEU GLN MET LEU GLN GLU
SEQRES  65 A  990  MET TYR LYS THR TRP PRO PHE PHE ARG VAL THR ILE ASP
SEQRES  66 A  990  LEU VAL GLU MET VAL PHE ALA LYS GLY ASN PRO GLY ILE
SEQRES  67 A  990  ALA ALA LEU ASN ASP LYS LEU LEU VAL SER GLU ASP LEU
SEQRES  68 A  990  ARG PRO PHE GLY GLU SER LEU ARG ALA ASN TYR GLU GLU
SEQRES  69 A  990  THR LYS ASN TYR LEU LEU LYS ILE ALA GLY HIS LYS ASP
SEQRES  70 A  990  LEU LEU GLU GLY ASP PRO TYR LEU LYS GLN GLY ILE ARG
SEQRES  71 A  990  LEU ARG ASP PRO TYR ILE THR THR LEU ASN VAL CYS GLN
SEQRES  72 A  990  ALA TYR THR LEU LYS ARG ILE ARG ASP PRO ASN TYR HIS
SEQRES  73 A  990  VAL THR LEU ARG PRO HIS ILE SER LYS GLU TYR ALA ALA
SEQRES  74 A  990  GLU PRO SER LYS PRO ALA ASP GLU LEU ILE HIS LEU ASN
SEQRES  75 A  990  PRO THR SER GLU TYR ALA PRO GLY LEU GLU ASP THR LEU
SEQRES  76 A  990  ILE LEU THR MET LYS GLY ILE ALA ALA GLY MET GLN ASN
SEQRES  77 A  990  THR GLY
SEQRES   1 B  990  MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES   2 B  990  SER GLY HIS GLU ASN LEU TYR PHE GLN GLY HIS MET ALA
SEQRES   3 B  990  ASN ARG ASN VAL GLU LYS LEU ALA SER ILE ASP ALA GLN
SEQRES   4 B  990  LEU ARG LEU LEU VAL PRO GLY LYS VAL SER GLU ASP ASP
SEQRES   5 B  990  LYS LEU VAL GLU TYR ASP ALA LEU LEU LEU ASP LYS PHE
SEQRES   6 B  990  LEU ASP ILE LEU GLN ASP LEU HIS GLY GLU ASP LEU LYS
SEQRES   7 B  990  GLU ALA VAL GLN GLN CYS TYR GLU LEU SER ALA GLU TYR
SEQRES   8 B  990  GLU GLY LYS HIS ASP PRO LYS LYS LEU GLU GLU LEU GLY
SEQRES   9 B  990  SER LEU LEU THR SER LEU ASP THR GLY ASP SER ILE VAL
SEQRES  10 B  990  ILE ALA LYS ALA PHE SER HIS MET LEU ASN LEU ALA ASN
SEQRES  11 B  990  LEU ALA GLU GLU LEU GLN ILE ALA TYR ARG ARG ARG ILE
SEQRES  12 B  990  LYS LEU LYS SER GLY ASP PHE ALA ASP GLU ALA ASN ALA
SEQRES  13 B  990  THR THR GLU SER ASP ILE GLU GLU THR PHE LYS ARG LEU
SEQRES  14 B  990  VAL HIS LYS LEU ASN LYS SER PRO GLU GLU VAL PHE ASP
SEQRES  15 B  990  ALA LEU LYS ASN GLN THR VAL GLU LEU VAL LEU THR ALA
SEQRES  16 B  990  HIS PRO THR GLN SER VAL ARG ARG SER LEU LEU GLN LYS
SEQRES  17 B  990  HIS GLY ARG ILE ARG ASN CYS LEU ALA GLN LEU TYR ALA
SEQRES  18 B  990  LYS ASP ILE THR PRO ASP ASP LYS GLN GLU LEU ASP GLU
SEQRES  19 B  990  ALA LEU HIS ARG GLU ILE GLN ALA ALA PHE ARG THR ASP
SEQRES  20 B  990  GLU ILE ARG ARG THR PRO PRO THR PRO GLN ASP GLU MET
SEQRES  21 B  990  ARG ALA GLY MET SER TYR PHE HIS GLU THR ILE TRP LYS
SEQRES  22 B  990  GLY VAL PRO LYS PHE LEU ARG ARG VAL ASP THR ALA LEU
SEQRES  23 B  990  LYS ASN ILE GLY ILE ASN GLU ARG PHE PRO TYR ASN ALA
SEQRES  24 B  990  PRO LEU ILE GLN PHE SER SER TRP MET GLY GLY ASP ARG
SEQRES  25 B  990  ASP GLY ASN PRO ARG VAL THR PRO GLU VAL THR ARG ASP
SEQRES  26 B  990  VAL CYS LEU LEU ALA ARG MET MET THR SER ASN MET TYR
SEQRES  27 B  990  PHE SER GLN ILE GLU ASP LEU MET ILE GLU MET SER MET
SEQRES  28 B  990  TRP ARG CYS ASN SER GLU LEU ARG VAL ARG ALA GLU GLU
SEQRES  29 B  990  LEU TYR ARG THR ALA ARG LYS ASP VAL LYS HIS TYR ILE
SEQRES  30 B  990  GLU PHE TRP LYS ARG ILE PRO PRO ASN GLN PRO TYR ARG
SEQRES  31 B  990  VAL ILE LEU GLY ASP VAL ARG ASP LYS LEU TYR ASN THR
SEQRES  32 B  990  ARG GLU ARG SER ARG HIS LEU LEU VAL ASP GLY LYS SER
SEQRES  33 B  990  ASP ILE PRO ASP GLU ALA VAL TYR THR ASN VAL GLU GLN
SEQRES  34 B  990  LEU LEU GLU PRO LEU GLU LEU CYS TYR ARG SER LEU CYS
SEQRES  35 B  990  ASP CYS GLY ASP HIS VAL ILE ALA ASP GLY SER LEU LEU
SEQRES  36 B  990  ASP PHE LEU ARG GLN VAL SER THR PHE GLY LEU SER LEU
SEQRES  37 B  990  VAL LYS LEU ASP ILE ARG GLN GLU SER ASP ARG HIS THR
SEQRES  38 B  990  GLU VAL LEU ASP ALA ILE THR GLN HIS LEU GLY ILE GLY
SEQRES  39 B  990  SER TYR ARG GLU TRP SER GLU GLU LYS ARG GLN GLU TRP
SEQRES  40 B  990  LEU LEU ALA GLU LEU SER GLY LYS ARG PRO LEU ILE GLY
SEQRES  41 B  990  PRO ASP LEU PRO LYS THR GLU GLU VAL LYS ASP CYS LEU
SEQRES  42 B  990  ASP THR PHE LYS VAL LEU ALA GLU LEU PRO SER ASP CYS
SEQRES  43 B  990  PHE GLY ALA TYR ILE ILE SER MET ALA THR SER THR SER
SEQRES  44 B  990  ASP VAL LEU ALA VAL GLU LEU LEU GLN ARG GLU TYR HIS
SEQRES  45 B  990  ILE LYS HIS PRO LEU ARG VAL VAL PRO LEU PHE GLU LYS
SEQRES  46 B  990  LEU ALA ASP LEU GLU ALA ALA PRO ALA ALA MET THR ARG
SEQRES  47 B  990  LEU PHE SER MET ASP TRP TYR ARG ASN ARG ILE ASP GLY
SEQRES  48 B  990  LYS GLN GLU VAL MET ILE GLY TYR SER ASP SER GLY LYS
SEQRES  49 B  990  ASP ALA GLY ARG PHE SER ALA ALA TRP GLN LEU TYR LYS
SEQRES  50 B  990  THR GLN GLU GLN ILE VAL LYS ILE ALA LYS GLU PHE GLY
SEQRES  51 B  990  VAL LYS LEU VAL ILE PHE HIS GLY ARG GLY GLY THR VAL
SEQRES  52 B  990  GLY ARG GLY GLY GLY PRO THR HIS LEU ALA LEU LEU SER
SEQRES  53 B  990  GLN PRO PRO ASP THR ILE ASN GLY SER LEU ARG VAL THR
SEQRES  54 B  990  VAL GLN GLY GLU VAL ILE GLU GLN SER PHE GLY GLU GLU
SEQRES  55 B  990  HIS LEU CYS PHE ARG THR LEU GLN ARG PHE CYS ALA ALA
SEQRES  56 B  990  THR LEU GLU HIS GLY MET ASN PRO PRO ILE SER PRO ARG
SEQRES  57 B  990  PRO GLU TRP ARG GLU LEU MET ASP GLN MET ALA VAL VAL
SEQRES  58 B  990  ALA THR GLU GLU TYR ARG SER VAL VAL PHE LYS GLU PRO
SEQRES  59 B  990  ARG PHE VAL GLU TYR PHE ARG LEU ALA THR PRO GLU LEU
SEQRES  60 B  990  GLU PHE GLY ARG MET ASN ILE GLY SER ARG PRO SER LYS
SEQRES  61 B  990  ARG LYS PRO SER GLY GLY ILE GLU SER LEU ARG ALA ILE
SEQRES  62 B  990  PRO TRP ILE PHE SER TRP THR GLN THR ARG PHE HIS LEU
SEQRES  63 B  990  PRO VAL TRP LEU GLY PHE GLY ALA ALA PHE LYS HIS ALA
SEQRES  64 B  990  ILE GLN LYS ASP SER LYS ASN LEU GLN MET LEU GLN GLU
SEQRES  65 B  990  MET TYR LYS THR TRP PRO PHE PHE ARG VAL THR ILE ASP
SEQRES  66 B  990  LEU VAL GLU MET VAL PHE ALA LYS GLY ASN PRO GLY ILE
SEQRES  67 B  990  ALA ALA LEU ASN ASP LYS LEU LEU VAL SER GLU ASP LEU
SEQRES  68 B  990  ARG PRO PHE GLY GLU SER LEU ARG ALA ASN TYR GLU GLU
SEQRES  69 B  990  THR LYS ASN TYR LEU LEU LYS ILE ALA GLY HIS LYS ASP
SEQRES  70 B  990  LEU LEU GLU GLY ASP PRO TYR LEU LYS GLN GLY ILE ARG
SEQRES  71 B  990  LEU ARG ASP PRO TYR ILE THR THR LEU ASN VAL CYS GLN
SEQRES  72 B  990  ALA TYR THR LEU LYS ARG ILE ARG ASP PRO ASN TYR HIS
SEQRES  73 B  990  VAL THR LEU ARG PRO HIS ILE SER LYS GLU TYR ALA ALA
SEQRES  74 B  990  GLU PRO SER LYS PRO ALA ASP GLU LEU ILE HIS LEU ASN
SEQRES  75 B  990  PRO THR SER GLU TYR ALA PRO GLY LEU GLU ASP THR LEU
SEQRES  76 B  990  ILE LEU THR MET LYS GLY ILE ALA ALA GLY MET GLN ASN
SEQRES  77 B  990  THR GLY
HET    ASP  A1967       9
HET    SO4  A1968       5
HET    EDO  A1969       4
HET    ASP  B1967       9
HET    SO4  B1968       5
HET    EDO  B1969       4
HETNAM     ASP ASPARTIC ACID
HETNAM     SO4 SULFATE ION
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   3  ASP    2(C4 H7 N O4)
FORMUL   4  SO4    2(O4 S 2-)
FORMUL   5  EDO    2(C2 H6 O2)
FORMUL   9  HOH   *198(H2 O)
HELIX    1   1 LYS A    8  VAL A   20  1                                  13
HELIX    2   2 LYS A   29  GLY A   50  1                                  22
HELIX    3   3 GLY A   50  HIS A   71  1                                  22
HELIX    4   4 ASP A   72  SER A   85  1                                  14
HELIX    5   5 ASP A   87  ARG A  116  1                                  30
HELIX    6   6 ASP A  125  ASN A  131  5                                   7
HELIX    7   7 ASP A  137  LYS A  148  1                                  12
HELIX    8   8 SER A  152  GLN A  163  1                                  12
HELIX    9   9 ARG A  178  TYR A  196  1                                  19
HELIX   10  10 THR A  201  ARG A  221  1                                  21
HELIX   11  11 THR A  231  ASN A  264  1                                  34
HELIX   12  12 THR A  295  MET A  325  1                                  31
HELIX   13  13 ASN A  331  THR A  344  1                                  14
HELIX   14  14 GLN A  363  ASP A  389  1                                  27
HELIX   15  15 PRO A  395  VAL A  399  5                                   5
HELIX   16  16 ASN A  402  CYS A  420  1                                  19
HELIX   17  17 ASP A  422  ASP A  427  1                                   6
HELIX   18  18 GLY A  428  GLY A  441  1                                  14
HELIX   19  19 SER A  453  LEU A  467  1                                  15
HELIX   20  20 SER A  471  TRP A  475  5                                   5
HELIX   21  21 SER A  476  SER A  489  1                                  14
HELIX   22  22 THR A  502  LEU A  518  1                                  17
HELIX   23  23 PRO A  519  ASP A  521  5                                   3
HELIX   24  24 SER A  533  TYR A  547  1                                  15
HELIX   25  25 LYS A  561  ASP A  586  1                                  26
HELIX   26  26 GLY A  594  GLY A  603  1                                  10
HELIX   27  27 GLY A  603  PHE A  625  1                                  23
HELIX   28  28 GLY A  637  ARG A  641  5                                   5
HELIX   29  29 GLY A  643  GLN A  653  1                                  11
HELIX   30  30 VAL A  670  GLY A  676  1                                   7
HELIX   31  31 GLU A  677  ASN A  698  1                                  22
HELIX   32  32 ARG A  704  PHE A  727  1                                  24
HELIX   33  33 ARG A  731  THR A  740  1                                  10
HELIX   34  34 PRO A  741  GLY A  746  1                                   6
HELIX   35  35 GLY A  762  LEU A  766  5                                   5
HELIX   36  36 ARG A  767  GLN A  777  1                                  11
HELIX   37  37 HIS A  781  LEU A  786  1                                   6
HELIX   38  38 GLY A  787  ASP A  799  1                                  13
HELIX   39  39 LYS A  801  TRP A  813  1                                  13
HELIX   40  40 TRP A  813  LYS A  829  1                                  17
HELIX   41  41 ASN A  831  VAL A  843  1                                  13
HELIX   42  42 LEU A  847  GLY A  870  1                                  24
HELIX   43  43 ASP A  878  ASP A  908  1                                  31
HELIX   44  44 GLY A  946  GLN A  963  1                                  18
HELIX   45  45 LYS B    8  VAL B   20  1                                  13
HELIX   46  46 LYS B   29  GLY B   50  1                                  22
HELIX   47  47 GLY B   50  HIS B   71  1                                  22
HELIX   48  48 ASP B   72  SER B   85  1                                  14
HELIX   49  49 ASP B   87  ARG B  116  1                                  30
HELIX   50  50 ASP B  125  ASN B  131  5                                   7
HELIX   51  51 ASP B  137  LYS B  148  1                                  12
HELIX   52  52 SER B  152  ASN B  162  1                                  11
HELIX   53  53 ARG B  178  TYR B  196  1                                  19
HELIX   54  54 THR B  201  ARG B  221  1                                  21
HELIX   55  55 THR B  231  ILE B  265  1                                  35
HELIX   56  56 THR B  295  MET B  325  1                                  31
HELIX   57  57 ASN B  331  TYR B  342  1                                  12
HELIX   58  58 GLN B  363  ASP B  389  1                                  27
HELIX   59  59 PRO B  395  VAL B  399  5                                   5
HELIX   60  60 ASN B  402  CYS B  420  1                                  19
HELIX   61  61 ASP B  422  ASP B  427  1                                   6
HELIX   62  62 GLY B  428  GLY B  441  1                                  14
HELIX   63  63 SER B  453  LEU B  467  1                                  15
HELIX   64  64 SER B  471  TRP B  475  5                                   5
HELIX   65  65 SER B  476  SER B  489  1                                  14
HELIX   66  66 THR B  502  LEU B  518  1                                  17
HELIX   67  67 PRO B  519  ASP B  521  5                                   3
HELIX   68  68 SER B  533  TYR B  547  1                                  15
HELIX   69  69 LYS B  561  ASP B  586  1                                  26
HELIX   70  70 GLY B  594  GLY B  603  1                                  10
HELIX   71  71 GLY B  603  PHE B  625  1                                  23
HELIX   72  72 GLY B  637  ARG B  641  5                                   5
HELIX   73  73 GLY B  643  GLN B  653  1                                  11
HELIX   74  74 VAL B  670  GLY B  676  1                                   7
HELIX   75  75 GLU B  677  ASN B  698  1                                  22
HELIX   76  76 ARG B  704  PHE B  727  1                                  24
HELIX   77  77 ARG B  731  THR B  740  1                                  10
HELIX   78  78 PRO B  741  GLY B  746  1                                   6
HELIX   79  79 ARG B  767  GLN B  777  1                                  11
HELIX   80  80 HIS B  781  LEU B  786  1                                   6
HELIX   81  81 GLY B  787  ASP B  799  1                                  13
HELIX   82  82 LYS B  801  TRP B  813  1                                  13
HELIX   83  83 TRP B  813  LYS B  829  1                                  17
HELIX   84  84 ASN B  831  VAL B  843  1                                  13
HELIX   85  85 LEU B  847  GLY B  870  1                                  24
HELIX   86  86 ASP B  878  ASP B  908  1                                  31
HELIX   87  87 GLY B  946  GLN B  963  1                                  18
SHEET    1  AA 8 ARG A 554  PRO A 557  0
SHEET    2  AA 8 PHE A 523  SER A 529  1  O  GLY A 524   N  ARG A 554
SHEET    3  AA 8 LYS A 446  GLU A 452  1  O  LEU A 447   N  GLY A 524
SHEET    4  AA 8 ILE A 278  SER A 282  1  O  PHE A 280   N  LYS A 446
SHEET    5  AA 8 THR A 164  LEU A 169  1  O  VAL A 165   N  GLN A 279
SHEET    6  AA 8 SER A 661  VAL A 666  1  O  LEU A 662   N  GLU A 166
SHEET    7  AA 8 LYS A 628  HIS A 633  1  O  ILE A 631   N  ARG A 663
SHEET    8  AA 8 LYS A 588  ILE A 593  1  O  GLN A 589   N  VAL A 630
SHEET    1  BA 8 ARG B 554  PRO B 557  0
SHEET    2  BA 8 PHE B 523  SER B 529  1  O  GLY B 524   N  ARG B 554
SHEET    3  BA 8 LYS B 446  GLU B 452  1  O  LEU B 447   N  GLY B 524
SHEET    4  BA 8 ILE B 278  SER B 282  1  O  PHE B 280   N  LYS B 446
SHEET    5  BA 8 THR B 164  LEU B 169  1  O  VAL B 165   N  GLN B 279
SHEET    6  BA 8 SER B 661  VAL B 666  1  O  LEU B 662   N  GLU B 166
SHEET    7  BA 8 LYS B 628  HIS B 633  1  O  ILE B 631   N  ARG B 663
SHEET    8  BA 8 LYS B 588  ILE B 593  1  O  GLN B 589   N  VAL B 630
SITE     1 AC1 11 ARG A 641  GLN A 673  MET A 825  LYS A 829
SITE     2 AC1 11 LEU A 881  ARG A 888  GLN A 963  ASN A 964
SITE     3 AC1 11 HOH A2010  HOH A2078  HOH A2116
SITE     1 AC2  4 ARG A 178  ARG A 179  SER A 180  ARG A 366
SITE     1 AC3  6 GLY A 636  GLY A 637  GLN A 667  ASN A 964
SITE     2 AC3  6 THR A 965  GLY A 966
SITE     1 AC4 11 ARG B 641  GLN B 673  MET B 825  LYS B 829
SITE     2 AC4 11 LEU B 881  ARG B 888  GLN B 963  ASN B 964
SITE     3 AC4 11 HOH B2006  HOH B2059  HOH B2082
SITE     1 AC5  4 ARG B 178  ARG B 179  SER B 180  ARG B 366
SITE     1 AC6  6 GLY B 636  GLY B 637  GLN B 667  ASN B 964
SITE     2 AC6  6 THR B 965  GLY B 966
CRYST1  162.520  122.110  131.910  90.00  90.00  90.00 P 21 21 2     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      0.006153  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008189  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007581        0.00000
      
PROCHECK
Go to PROCHECK summary
 References