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PDBsum entry 2uu7

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Top Page protein metals Protein-protein interface(s) links
Ligase PDB id
2uu7
Jmol
Contents
Protein chains
(+ 9 more) 370 a.a.
Metals
_CL ×15
_MG ×15
HEADER    LIGASE                                  28-FEB-07   2UU7
TITLE     CRYSTAL STRUCTURE OF APO GLUTAMINE SYNTHETASE FROM DOG (
TITLE    2 CANIS FAMILIARIS)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUTAMINE SYNTHETASE;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O;
COMPND   4 SYNONYM: GLUTAMATE--AMMONIA LIGASE, GS;
COMPND   5 EC: 6.3.1.2;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;
SOURCE   3 ORGANISM_COMMON: DOG;
SOURCE   4 ORGANISM_TAXID: 9615;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21STAR(DE3);
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS    LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.W.KRAJEWSKI,T.A.JONES,S.L.MOWBRAY
REVDAT   4   24-FEB-09 2UU7    1       VERSN
REVDAT   3   18-DEC-07 2UU7    1       JRNL
REVDAT   2   27-NOV-07 2UU7    1       JRNL
REVDAT   1   16-OCT-07 2UU7    0
JRNL        AUTH   W.W.KRAJEWSKI,R.COLLINS,L.HOLMBERG-SCHIAVONE,
JRNL        AUTH 2 T.A.JONES,T.KARLBERG,S.L.MOWBRAY
JRNL        TITL   CRYSTAL STRUCTURES OF MAMMALIAN GLUTAMINE
JRNL        TITL 2 SYNTHETASES ILLUSTRATE SUBSTRATE-INDUCED
JRNL        TITL 3 CONFORMATIONAL CHANGES AND PROVIDE OPPORTUNITIES
JRNL        TITL 4 FOR DRUG AND HERBICIDE DESIGN.
JRNL        REF    J.MOL.BIOL.                   V. 375   217 2008
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   18005987
JRNL        DOI    10.1016/J.JMB.2007.10.029
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.99
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9
REMARK   3   NUMBER OF REFLECTIONS             : 166824
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) : 0.213
REMARK   3   R VALUE            (WORKING SET) : 0.213
REMARK   3   FREE R VALUE                     : 0.230
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.200
REMARK   3   FREE R VALUE TEST SET COUNT      : 2015
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) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12053
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210
REMARK   3   BIN FREE R VALUE SET COUNT          : 156
REMARK   3   BIN FREE R VALUE                    : 0.3120
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 43995
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 30
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.43
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.42000
REMARK   3    B22 (A**2) : -1.97000
REMARK   3    B33 (A**2) : 1.55000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.357
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.267
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.164
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 45210 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 61125 ; 1.358 ; 1.940
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  5535 ; 5.899 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2280 ;38.268 ;23.684
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  7395 ;18.079 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   330 ;21.641 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  6105 ; 0.095 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 35685 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 19460 ; 0.224 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 31028 ; 0.319 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1201 ; 0.132 ; 0.200
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):   154 ; 0.539 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.543 ; 0.200
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): 27992 ; 1.338 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 44220 ; 2.487 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 19433 ; 3.320 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 16905 ; 5.900 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D E F G H I J K L M
REMARK   3                                      N O
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      3       A     500      1
REMARK   3           1     B      3       B     500      1
REMARK   3           1     C      3       C     500      1
REMARK   3           1     D      3       D     500      1
REMARK   3           1     E      3       E     500      1
REMARK   3           1     F      3       F     500      1
REMARK   3           1     G      3       G     500      1
REMARK   3           1     H      3       H     500      1
REMARK   3           1     I      3       I     500      1
REMARK   3           1     J      3       J     500      1
REMARK   3           1     K      3       K     500      1
REMARK   3           1     L      3       L     500      1
REMARK   3           1     M      3       M     500      1
REMARK   3           1     N      3       N     500      1
REMARK   3           1     O      3       O     500      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    C    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    D    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    E    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    F    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    G    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    H    (A):   2934 ;  0.05 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    I    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    J    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    K    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    L    (A):   2934 ;  0.05 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    M    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    N    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    O    (A):   2934 ;  0.04 ;  0.05
REMARK   3   TIGHT THERMAL      1    A (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    C (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    D (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    E (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    F (A**2):   2934 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      1    G (A**2):   2934 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      1    H (A**2):   2934 ;  0.09 ;  0.50
REMARK   3   TIGHT THERMAL      1    I (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    J (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    K (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    L (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    M (A**2):   2934 ;  0.08 ;  0.50
REMARK   3   TIGHT THERMAL      1    N (A**2):   2934 ;  0.10 ;  0.50
REMARK   3   TIGHT THERMAL      1    O (A**2):   2934 ;  0.09 ;  0.50
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2UU7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-07.
REMARK 100 THE PDBE ID CODE IS EBI-31648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-4
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97650
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 168869
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.00
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 3.7
REMARK 200  R MERGE                    (I) : 0.17
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.6
REMARK 200  R MERGE FOR SHELL          (I) : 0.41
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2D3A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.2 M POTASSIUM
REMARK 280  CITRATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       96.07800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       96.07800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       91.79500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      242.80100
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       91.79500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      242.80100
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       96.07800
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       91.79500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      242.80100
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       96.07800
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       91.79500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      242.80100
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 48950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 160270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -237.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, G, H, I, J, F
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE:  2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 54040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 160280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -257.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, M, N, O, K
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        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      485.60200
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      192.15600
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     ASN A   373
REMARK 465     LEU A   374
REMARK 465     GLU A   375
REMARK 465     HIS A   376
REMARK 465     HIS A   377
REMARK 465     HIS A   378
REMARK 465     HIS A   379
REMARK 465     HIS A   380
REMARK 465     HIS A   381
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     ASN B   373
REMARK 465     LEU B   374
REMARK 465     GLU B   375
REMARK 465     HIS B   376
REMARK 465     HIS B   377
REMARK 465     HIS B   378
REMARK 465     HIS B   379
REMARK 465     HIS B   380
REMARK 465     HIS B   381
REMARK 465     MET C     1
REMARK 465     ALA C     2
REMARK 465     ASN C   373
REMARK 465     LEU C   374
REMARK 465     GLU C   375
REMARK 465     HIS C   376
REMARK 465     HIS C   377
REMARK 465     HIS C   378
REMARK 465     HIS C   379
REMARK 465     HIS C   380
REMARK 465     HIS C   381
REMARK 465     MET D     1
REMARK 465     ALA D     2
REMARK 465     ASN D   373
REMARK 465     LEU D   374
REMARK 465     GLU D   375
REMARK 465     HIS D   376
REMARK 465     HIS D   377
REMARK 465     HIS D   378
REMARK 465     HIS D   379
REMARK 465     HIS D   380
REMARK 465     HIS D   381
REMARK 465     MET E     1
REMARK 465     ALA E     2
REMARK 465     ASN E   373
REMARK 465     LEU E   374
REMARK 465     GLU E   375
REMARK 465     HIS E   376
REMARK 465     HIS E   377
REMARK 465     HIS E   378
REMARK 465     HIS E   379
REMARK 465     HIS E   380
REMARK 465     HIS E   381
REMARK 465     MET F     1
REMARK 465     ALA F     2
REMARK 465     ASN F   373
REMARK 465     LEU F   374
REMARK 465     GLU F   375
REMARK 465     HIS F   376
REMARK 465     HIS F   377
REMARK 465     HIS F   378
REMARK 465     HIS F   379
REMARK 465     HIS F   380
REMARK 465     HIS F   381
REMARK 465     MET G     1
REMARK 465     ALA G     2
REMARK 465     ASN G   373
REMARK 465     LEU G   374
REMARK 465     GLU G   375
REMARK 465     HIS G   376
REMARK 465     HIS G   377
REMARK 465     HIS G   378
REMARK 465     HIS G   379
REMARK 465     HIS G   380
REMARK 465     HIS G   381
REMARK 465     MET H     1
REMARK 465     ALA H     2
REMARK 465     ASN H   373
REMARK 465     LEU H   374
REMARK 465     GLU H   375
REMARK 465     HIS H   376
REMARK 465     HIS H   377
REMARK 465     HIS H   378
REMARK 465     HIS H   379
REMARK 465     HIS H   380
REMARK 465     HIS H   381
REMARK 465     MET I     1
REMARK 465     ALA I     2
REMARK 465     ASN I   373
REMARK 465     LEU I   374
REMARK 465     GLU I   375
REMARK 465     HIS I   376
REMARK 465     HIS I   377
REMARK 465     HIS I   378
REMARK 465     HIS I   379
REMARK 465     HIS I   380
REMARK 465     HIS I   381
REMARK 465     MET J     1
REMARK 465     ALA J     2
REMARK 465     ASN J   373
REMARK 465     LEU J   374
REMARK 465     GLU J   375
REMARK 465     HIS J   376
REMARK 465     HIS J   377
REMARK 465     HIS J   378
REMARK 465     HIS J   379
REMARK 465     HIS J   380
REMARK 465     HIS J   381
REMARK 465     MET K     1
REMARK 465     ALA K     2
REMARK 465     ASN K   373
REMARK 465     LEU K   374
REMARK 465     GLU K   375
REMARK 465     HIS K   376
REMARK 465     HIS K   377
REMARK 465     HIS K   378
REMARK 465     HIS K   379
REMARK 465     HIS K   380
REMARK 465     HIS K   381
REMARK 465     MET L     1
REMARK 465     ALA L     2
REMARK 465     ASN L   373
REMARK 465     LEU L   374
REMARK 465     GLU L   375
REMARK 465     HIS L   376
REMARK 465     HIS L   377
REMARK 465     HIS L   378
REMARK 465     HIS L   379
REMARK 465     HIS L   380
REMARK 465     HIS L   381
REMARK 465     MET M     1
REMARK 465     ALA M     2
REMARK 465     ASN M   373
REMARK 465     LEU M   374
REMARK 465     GLU M   375
REMARK 465     HIS M   376
REMARK 465     HIS M   377
REMARK 465     HIS M   378
REMARK 465     HIS M   379
REMARK 465     HIS M   380
REMARK 465     HIS M   381
REMARK 465     MET N     1
REMARK 465     ALA N     2
REMARK 465     ASN N   373
REMARK 465     LEU N   374
REMARK 465     GLU N   375
REMARK 465     HIS N   376
REMARK 465     HIS N   377
REMARK 465     HIS N   378
REMARK 465     HIS N   379
REMARK 465     HIS N   380
REMARK 465     HIS N   381
REMARK 465     MET O     1
REMARK 465     ALA O     2
REMARK 465     ASN O   373
REMARK 465     LEU O   374
REMARK 465     GLU O   375
REMARK 465     HIS O   376
REMARK 465     HIS O   377
REMARK 465     HIS O   378
REMARK 465     HIS O   379
REMARK 465     HIS O   380
REMARK 465     HIS O   381
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500
REMARK 500   CB   GLU H    55     NZ   LYS L   333     3555      1.91
REMARK 500   CG   GLU H    55     NZ   LYS L   333     3555      2.08
REMARK 500   NE   ARG H   106     OE1  GLU L   263     3555      1.86
REMARK 500   CZ   ARG H   106     OE1  GLU L   263     3555      1.66
REMARK 500   NH1  ARG H   106     OE1  GLU L   263     3555      1.86
REMARK 500   NH2  ARG H   106     CB   GLU L   263     3555      1.80
REMARK 500   CE   LYS H   259     NH2  ARG K   119     3555      1.91
REMARK 500   NZ   LYS H   259     NH2  ARG K   119     3555      1.96
REMARK 500   CZ   ARG I   106     OE1  GLU M   263     1554      1.98
REMARK 500   NH2  ARG I   119     OE2  GLU M   264     1554      1.49
REMARK 500   O    GLN J   331     CG   ASN M   126     1554      1.99
REMARK 500   O    GLN J   331     ND2  ASN M   126     1554      1.85
REMARK 500   NH2  ARG K   119     CE   LYS H   259     3555      1.91
REMARK 500   NH2  ARG K   119     NZ   LYS H   259     3555      1.96
REMARK 500   CB   GLU L   263     NH2  ARG H   106     3555      1.80
REMARK 500   OE1  GLU L   263     NE   ARG H   106     3555      1.86
REMARK 500   OE1  GLU L   263     CZ   ARG H   106     3555      1.66
REMARK 500   OE1  GLU L   263     NH1  ARG H   106     3555      1.86
REMARK 500   NZ   LYS L   333     CB   GLU H    55     3555      1.91
REMARK 500   NZ   LYS L   333     CG   GLU H    55     3555      2.08
REMARK 500   CG   ASN M   126     O    GLN J   331     1556      1.99
REMARK 500   ND2  ASN M   126     O    GLN J   331     1556      1.85
REMARK 500   OE1  GLU M   263     CZ   ARG I   106     1556      1.98
REMARK 500   OE2  GLU M   264     NH2  ARG I   119     1556      1.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    THR B   3   CA    THR B   3   CB      0.178
REMARK 500    THR D   3   CA    THR D   3   CB      0.188
REMARK 500    THR E   3   CA    THR E   3   CB      0.167
REMARK 500    CYS E 252   CB    CYS E 252   SG     -0.109
REMARK 500    THR G   3   CA    THR G   3   CB      0.181
REMARK 500    THR H   3   CA    THR H   3   CB      0.158
REMARK 500    THR K   3   CA    THR K   3   CB      0.191
REMARK 500    THR L   3   CA    THR L   3   CB      0.191
REMARK 500    CYS L  42   CB    CYS L  42   SG     -0.102
REMARK 500    THR M   3   CA    THR M   3   CB      0.161
REMARK 500    CYS M  42   CB    CYS M  42   SG     -0.099
REMARK 500    CYS N 252   CB    CYS N 252   SG     -0.102
REMARK 500    THR O   3   CA    THR O   3   CB      0.158
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 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    ASN A  74       58.83   -108.03
REMARK 500    LYS A  91      171.29     72.87
REMARK 500    LYS A 103     -179.80    -69.55
REMARK 500    ARG A 106       19.12     57.55
REMARK 500    HIS A 128       70.99     44.25
REMARK 500    ASN A 362       35.61     35.87
REMARK 500    TYR A 371     -146.67   -134.62
REMARK 500    ASN B  74       58.65   -107.30
REMARK 500    LYS B  91      172.38     72.05
REMARK 500    ARG B 106       19.70     54.40
REMARK 500    HIS B 128       71.76     46.28
REMARK 500    LYS B 241       72.46   -152.08
REMARK 500    ASN B 246       48.82    -71.35
REMARK 500    ALA B 317       47.26     39.55
REMARK 500    ASN B 362       38.84     34.29
REMARK 500    TYR B 371     -148.91   -135.63
REMARK 500    ASN C  74       58.58   -107.40
REMARK 500    LYS C  91      170.91     71.47
REMARK 500    HIS C 128       71.04     44.62
REMARK 500    ASN C 246       48.77    -71.89
REMARK 500    ALA C 317       45.72     38.53
REMARK 500    ASN C 362       39.11     34.84
REMARK 500    TYR C 371     -146.32   -134.53
REMARK 500    ASN D  74       58.23   -107.49
REMARK 500    LYS D  91      169.11     73.48
REMARK 500    ARG D 106       18.39     59.36
REMARK 500    ASN D 246       47.87    -72.14
REMARK 500    ALA D 317       43.70     39.00
REMARK 500    ASN D 362       40.26     35.98
REMARK 500    TYR D 371     -146.92   -133.03
REMARK 500    ASN E  74       58.55   -107.64
REMARK 500    LYS E  91      168.36     71.61
REMARK 500    ARG E 106       19.85     56.77
REMARK 500    HIS E 128       71.69     44.97
REMARK 500    ALA E 317       47.46     38.41
REMARK 500    ASN E 362       38.88     37.44
REMARK 500    TYR E 371     -147.99   -136.20
REMARK 500    ASN F  74       56.86   -108.61
REMARK 500    LYS F  91      170.13     73.98
REMARK 500    ARG F 106       19.35     56.68
REMARK 500    HIS F 128       73.50     42.25
REMARK 500    ASN F 246       52.29    -69.75
REMARK 500    ASN F 362       37.15     35.62
REMARK 500    TYR F 371     -147.84   -133.88
REMARK 500    ASN G  74       57.10   -110.03
REMARK 500    LYS G  91      168.68     66.98
REMARK 500    ARG G 106       19.67     55.81
REMARK 500    HIS G 128       71.80     45.68
REMARK 500    ASN G 246       49.27    -72.02
REMARK 500    ASN G 362       37.35     35.91
REMARK 500    TYR G 371     -146.88   -134.62
REMARK 500    ASN H  74       56.60   -105.23
REMARK 500    LYS H  91      170.99     69.65
REMARK 500    ARG H 106       19.29     54.03
REMARK 500    HIS H 128       70.54     46.90
REMARK 500    ASN H 362       39.93     36.63
REMARK 500    TYR H 371     -148.66   -132.31
REMARK 500    ASN I  74       58.71   -108.24
REMARK 500    LYS I  91      171.56     74.90
REMARK 500    HIS I 128       70.71     44.99
REMARK 500    ASN I 246       47.77    -70.50
REMARK 500    ARG I 280       29.17   -140.84
REMARK 500    ALA I 317       44.26     38.58
REMARK 500    ASN I 362       38.78     34.21
REMARK 500    TYR I 371     -148.12   -135.32
REMARK 500    ASN J  74       59.01   -108.74
REMARK 500    LYS J  91      172.45     68.37
REMARK 500    ARG J 106       18.25     55.38
REMARK 500    HIS J 128       73.52     44.90
REMARK 500    ASP J 289      147.36   -170.01
REMARK 500    ALA J 317       47.39     39.09
REMARK 500    ASN J 362       35.75     35.57
REMARK 500    TYR J 371     -147.85   -136.30
REMARK 500    ASN K  74       59.14   -108.39
REMARK 500    ALA K  82      -51.37   -122.97
REMARK 500    LYS K  91      168.81     71.52
REMARK 500    HIS K 128       71.65     46.20
REMARK 500    ASP K 289      149.07   -170.06
REMARK 500    PRO K 290        0.08    -69.95
REMARK 500    ASN K 362       38.36     33.03
REMARK 500    TYR K 371     -145.99   -136.34
REMARK 500    ASN L  74       58.74   -108.38
REMARK 500    LYS L  91      168.86     72.26
REMARK 500    HIS L 128       73.34     45.73
REMARK 500    ASN L 246       49.48    -71.29
REMARK 500    ASP L 289      147.86   -171.54
REMARK 500    ASN L 362       37.06     37.29
REMARK 500    TYR L 371     -146.62   -134.46
REMARK 500    ASN M  74       58.17   -107.71
REMARK 500    LYS M  91      169.87     71.50
REMARK 500    ARG M 106       19.19     56.66
REMARK 500    HIS M 128       71.79     44.94
REMARK 500    LYS M 241       76.32   -150.06
REMARK 500    ALA M 317       44.13     39.83
REMARK 500    ASN M 362       37.22     36.81
REMARK 500    TYR M 371     -146.34   -136.22
REMARK 500    ASN N  74       57.84   -108.35
REMARK 500    LYS N  91      170.44     74.35
REMARK 500    HIS N 128       72.18     45.37
REMARK 500    ASN N 362       39.11     36.98
REMARK 500    TYR N 371     -148.30   -134.94
REMARK 500    ASN O  74       57.72   -109.07
REMARK 500    LYS O  91      168.73     71.87
REMARK 500    HIS O 128       71.44     44.78
REMARK 500    ALA O 317       46.81     38.55
REMARK 500    ASN O 362       40.64     34.94
REMARK 500    TYR O 371     -148.07   -136.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 196   OE2
REMARK 620 2 GLU A 136   OE1  73.8
REMARK 620 3 GLU A 203   OE1  72.7  79.1
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 196   OE2
REMARK 620 2 GLU B 203   OE1  68.4
REMARK 620 3 GLU B 136   OE1  71.3  80.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 136   OE1
REMARK 620 2 GLU C 203   OE1  77.0
REMARK 620 3 GLU C 196   OE2  73.0  68.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 196   OE2
REMARK 620 2 GLU D 136   OE1  76.9
REMARK 620 3 GLU D 203   OE1  75.2  82.4
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG E 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 203   OE1
REMARK 620 2 GLU E 136   OE1  85.3
REMARK 620 3 GLU E 196   OE2  70.5  78.3
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG F 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 136   OE1
REMARK 620 2 GLU F 196   OE2  70.9
REMARK 620 3 GLU F 203   OE1  78.4  68.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG G 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 136   OE1
REMARK 620 2 GLU G 196   OE2  72.2
REMARK 620 3 GLU G 203   OE1  78.9  71.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG H 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU H 136   OE1
REMARK 620 2 GLU H 203   OE1  80.2
REMARK 620 3 GLU H 196   OE2  76.4  75.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG I 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 136   OE1
REMARK 620 2 GLU I 196   OE2  76.8
REMARK 620 3 GLU I 203   OE1  81.5  69.6
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG J 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU J 136   OE1
REMARK 620 2 GLU J 196   OE2  71.1
REMARK 620 3 GLU J 203   OE1  76.0  69.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG K 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 136   OE1
REMARK 620 2 GLU K 203   OE1  81.9
REMARK 620 3 GLU K 196   OE2  78.2  74.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG L 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 196   OE2
REMARK 620 2 GLU L 203   OE1  69.9
REMARK 620 3 GLU L 136   OE1  73.4  80.2
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG M 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU M 196   OE2
REMARK 620 2 GLU M 136   OE1  74.7
REMARK 620 3 GLU M 203   OE1  72.8  82.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG N 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU N 203   OE1
REMARK 620 2 GLU N 196   OE2  69.9
REMARK 620 3 GLU N 136   OE1  78.7  70.1
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG O 401  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU O 136   OE1
REMARK 620 2 GLU O 196   OE2  75.5
REMARK 620 3 GLU O 203   OE1  82.8  72.7
REMARK 620 N                    1     2
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL E1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL F1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL G1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL H1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL I1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL J1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL K1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL L1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL M1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL N1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL O1373
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG I 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG J 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG K 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG L 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG M 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG N 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG O 401
DBREF  2UU7 A    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 A    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 A  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 B    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 B    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 B  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 C    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 C    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 C  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 D    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 D    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 D  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 E    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 E    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 E  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 F    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 F    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 F  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 G    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 G    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 G  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 H    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 H    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 H  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 I    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 I    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 I  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 J    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 J    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 J  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 K    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 K    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 K  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 L    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 L    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 L  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 M    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 M    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 M  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 N    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 N    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 N  374   381  PDB    2UU7     2UU7           374    381
DBREF  2UU7 O    1     1  PDB    2UU7     2UU7             1      1
DBREF  2UU7 O    2   373  UNP    Q8HZM5   GLNA_CANFA       1    372
DBREF  2UU7 O  374   381  PDB    2UU7     2UU7           374    381
SEQRES   1 A  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 A  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 A  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 A  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 A  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 A  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 A  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 A  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 A  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 A  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 A  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 A  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 A  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 A  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 A  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 A  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 A  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 A  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 A  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 A  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 A  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 A  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 A  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 A  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 A  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 A  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 A  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 A  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 A  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 A  381  HIS HIS HIS HIS
SEQRES   1 B  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 B  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 B  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 B  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 B  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 B  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 B  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 B  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 B  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 B  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 B  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 B  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 B  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 B  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 B  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 B  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 B  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 B  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 B  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 B  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 B  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 B  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 B  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 B  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 B  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 B  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 B  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 B  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 B  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 B  381  HIS HIS HIS HIS
SEQRES   1 C  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 C  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 C  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 C  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 C  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 C  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 C  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 C  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 C  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 C  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 C  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 C  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 C  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 C  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 C  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 C  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 C  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 C  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 C  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 C  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 C  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 C  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 C  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 C  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 C  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 C  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 C  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 C  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 C  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 C  381  HIS HIS HIS HIS
SEQRES   1 D  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 D  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 D  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 D  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 D  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 D  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 D  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 D  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 D  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 D  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 D  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 D  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 D  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 D  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 D  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 D  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 D  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 D  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 D  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 D  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 D  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 D  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 D  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 D  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 D  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 D  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 D  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 D  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 D  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 D  381  HIS HIS HIS HIS
SEQRES   1 E  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 E  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 E  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 E  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 E  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 E  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 E  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 E  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 E  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 E  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 E  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 E  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 E  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 E  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 E  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 E  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 E  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 E  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 E  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 E  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 E  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 E  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 E  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 E  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 E  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 E  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 E  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 E  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 E  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 E  381  HIS HIS HIS HIS
SEQRES   1 F  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 F  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 F  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 F  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 F  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 F  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 F  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 F  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 F  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 F  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 F  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 F  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 F  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 F  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 F  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 F  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 F  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 F  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 F  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 F  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 F  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 F  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 F  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 F  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 F  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 F  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 F  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 F  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 F  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 F  381  HIS HIS HIS HIS
SEQRES   1 G  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 G  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 G  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 G  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 G  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 G  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 G  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 G  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 G  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 G  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 G  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 G  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 G  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 G  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 G  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 G  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 G  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 G  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 G  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 G  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 G  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 G  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 G  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 G  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 G  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 G  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 G  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 G  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 G  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 G  381  HIS HIS HIS HIS
SEQRES   1 H  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 H  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 H  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 H  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 H  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 H  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 H  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 H  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 H  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 H  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 H  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 H  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 H  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 H  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 H  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 H  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 H  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 H  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 H  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 H  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 H  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 H  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 H  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 H  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 H  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 H  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 H  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 H  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 H  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 H  381  HIS HIS HIS HIS
SEQRES   1 I  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 I  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 I  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 I  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 I  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 I  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 I  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 I  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 I  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 I  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 I  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 I  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 I  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 I  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 I  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 I  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 I  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 I  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 I  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 I  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 I  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 I  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 I  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 I  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 I  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 I  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 I  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 I  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 I  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 I  381  HIS HIS HIS HIS
SEQRES   1 J  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 J  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 J  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 J  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 J  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 J  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 J  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 J  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 J  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 J  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 J  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 J  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 J  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 J  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 J  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 J  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 J  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 J  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 J  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 J  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 J  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 J  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 J  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 J  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 J  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 J  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 J  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 J  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 J  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 J  381  HIS HIS HIS HIS
SEQRES   1 K  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 K  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 K  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 K  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 K  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 K  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 K  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 K  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 K  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 K  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 K  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 K  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 K  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 K  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 K  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 K  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 K  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 K  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 K  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 K  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 K  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 K  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 K  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 K  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 K  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 K  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 K  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 K  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 K  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 K  381  HIS HIS HIS HIS
SEQRES   1 L  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 L  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 L  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 L  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 L  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 L  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 L  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 L  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 L  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 L  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 L  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 L  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 L  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 L  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 L  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 L  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 L  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 L  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 L  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 L  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 L  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 L  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 L  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 L  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 L  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 L  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 L  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 L  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 L  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 L  381  HIS HIS HIS HIS
SEQRES   1 M  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 M  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 M  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 M  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 M  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 M  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 M  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 M  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 M  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 M  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 M  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 M  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 M  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 M  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 M  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 M  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 M  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 M  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 M  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 M  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 M  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 M  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 M  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 M  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 M  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 M  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 M  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 M  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 M  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 M  381  HIS HIS HIS HIS
SEQRES   1 N  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 N  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 N  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 N  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 N  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 N  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 N  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 N  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 N  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 N  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 N  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 N  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 N  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 N  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 N  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 N  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 N  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 N  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 N  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 N  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 N  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 N  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 N  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 N  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 N  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 N  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 N  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 N  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 N  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 N  381  HIS HIS HIS HIS
SEQRES   1 O  381  MET ALA THR SER ALA SER SER HIS LEU ASN LYS GLY ILE
SEQRES   2 O  381  LYS GLN VAL TYR MET SER LEU PRO GLN GLY GLU LYS VAL
SEQRES   3 O  381  GLN ALA MET TYR ILE TRP ILE ASP GLY THR GLY GLU GLY
SEQRES   4 O  381  LEU ARG CYS LYS THR ARG THR LEU ASP SER GLU PRO LYS
SEQRES   5 O  381  GLY VAL GLU GLU LEU PRO GLU TRP ASN PHE ASP GLY SER
SEQRES   6 O  381  SER THR PHE GLN SER GLU GLY SER ASN SER ASP MET TYR
SEQRES   7 O  381  LEU VAL PRO ALA ALA MET PHE ARG ASP PRO PHE ARG LYS
SEQRES   8 O  381  ASP PRO ASN LYS LEU VAL PHE CYS GLU VAL PHE LYS TYR
SEQRES   9 O  381  ASN ARG LYS PRO ALA GLU THR ASN LEU ARG HIS THR CYS
SEQRES  10 O  381  LYS ARG ILE MET ASP MET VAL SER ASN GLN HIS PRO TRP
SEQRES  11 O  381  PHE GLY MET GLU GLN GLU TYR THR LEU MET GLY THR ASP
SEQRES  12 O  381  GLY HIS PRO PHE GLY TRP PRO SER ASN GLY PHE PRO GLY
SEQRES  13 O  381  PRO GLN GLY PRO TYR TYR CYS GLY VAL GLY ALA ASP LYS
SEQRES  14 O  381  ALA TYR GLY ARG ASP ILE VAL GLU ALA HIS TYR ARG ALA
SEQRES  15 O  381  CYS LEU TYR ALA GLY ILE LYS ILE ALA GLY THR ASN ALA
SEQRES  16 O  381  GLU VAL MET PRO ALA GLN TRP GLU PHE GLN ILE GLY PRO
SEQRES  17 O  381  CYS GLU GLY ILE ASP MET GLY ASP HIS LEU TRP VAL ALA
SEQRES  18 O  381  ARG PHE ILE LEU HIS ARG VAL CYS GLU ASP PHE GLY VAL
SEQRES  19 O  381  ILE ALA THR PHE ASP PRO LYS PRO ILE PRO GLY ASN TRP
SEQRES  20 O  381  ASN GLY ALA GLY CYS HIS THR ASN PHE SER THR LYS ALA
SEQRES  21 O  381  MET ARG GLU GLU ASN GLY LEU LYS TYR ILE GLU GLU SER
SEQRES  22 O  381  ILE GLU LYS LEU SER LYS ARG HIS GLN TYR HIS ILE ARG
SEQRES  23 O  381  ALA TYR ASP PRO LYS GLY GLY LEU ASP ASN ALA ARG ARG
SEQRES  24 O  381  LEU THR GLY PHE HIS GLU THR SER ASN ILE ASN ASP PHE
SEQRES  25 O  381  SER ALA GLY VAL ALA ASN ARG GLY ALA SER ILE ARG ILE
SEQRES  26 O  381  PRO ARG THR VAL GLY GLN GLU LYS LYS GLY TYR PHE GLU
SEQRES  27 O  381  ASP ARG ARG PRO SER ALA ASN CYS ASP PRO PHE SER VAL
SEQRES  28 O  381  THR GLU ALA LEU ILE ARG THR CYS LEU LEU ASN GLU THR
SEQRES  29 O  381  GLY ASP GLU PRO PHE GLN TYR LYS ASN LEU GLU HIS HIS
SEQRES  30 O  381  HIS HIS HIS HIS
HET     CL  A1373       1
HET     CL  B1373       1
HET     CL  C1373       1
HET     CL  D1373       1
HET     CL  E1373       1
HET     CL  F1373       1
HET     CL  G1373       1
HET     CL  H1373       1
HET     CL  I1373       1
HET     CL  J1373       1
HET     CL  K1373       1
HET     CL  L1373       1
HET     CL  M1373       1
HET     CL  N1373       1
HET     CL  O1373       1
HET     MG  A 401       1
HET     MG  B 401       1
HET     MG  C 401       1
HET     MG  D 401       1
HET     MG  E 401       1
HET     MG  F 401       1
HET     MG  G 401       1
HET     MG  H 401       1
HET     MG  I 401       1
HET     MG  J 401       1
HET     MG  K 401       1
HET     MG  L 401       1
HET     MG  M 401       1
HET     MG  N 401       1
HET     MG  O 401       1
HETNAM      MG MAGNESIUM ION
HETNAM      CL CHLORIDE ION
FORMUL  16   MG    15(MG 2+)
FORMUL  17   CL    15(CL 1-)
HELIX    1   1 ALA A    5  LEU A    9  5                                   5
HELIX    2   2 ASN A   10  SER A   19  1                                  10
HELIX    3   3 GLY A   53  LEU A   57  5                                   5
HELIX    4   4 SER A   65  PHE A   68  5                                   4
HELIX    5   5 LEU A  113  MET A  123  1                                  11
HELIX    6   6 VAL A  124  HIS A  128  5                                   5
HELIX    7   7 GLY A  172  GLY A  187  1                                  16
HELIX    8   8 ILE A  212  GLY A  233  1                                  22
HELIX    9   9 THR A  258  GLU A  263  1                                   6
HELIX   10  10 GLY A  266  LYS A  279  1                                  14
HELIX   11  11 ARG A  280  TYR A  288  1                                   9
HELIX   12  12 ASP A  295  ARG A  299  5                                   5
HELIX   13  13 PRO A  326  LYS A  333  1                                   8
HELIX   14  14 ASP A  347  LEU A  360  1                                  14
HELIX   15  15 ALA B    5  LEU B    9  5                                   5
HELIX   16  16 ASN B   10  SER B   19  1                                  10
HELIX   17  17 GLY B   53  LEU B   57  5                                   5
HELIX   18  18 SER B   65  THR B   67  5                                   3
HELIX   19  19 LEU B  113  MET B  123  1                                  11
HELIX   20  20 VAL B  124  HIS B  128  5                                   5
HELIX   21  21 GLY B  172  GLY B  187  1                                  16
HELIX   22  22 ILE B  212  GLY B  233  1                                  22
HELIX   23  23 THR B  258  GLU B  263  1                                   6
HELIX   24  24 GLY B  266  LYS B  279  1                                  14
HELIX   25  25 ARG B  280  TYR B  288  1                                   9
HELIX   26  26 ASP B  295  ARG B  299  5                                   5
HELIX   27  27 PRO B  326  LYS B  333  1                                   8
HELIX   28  28 ASP B  347  LEU B  360  1                                  14
HELIX   29  29 ALA C    5  LEU C    9  5                                   5
HELIX   30  30 ASN C   10  SER C   19  1                                  10
HELIX   31  31 GLY C   53  LEU C   57  5                                   5
HELIX   32  32 SER C   65  PHE C   68  5                                   4
HELIX   33  33 LEU C  113  MET C  123  1                                  11
HELIX   34  34 VAL C  124  HIS C  128  5                                   5
HELIX   35  35 GLY C  172  GLY C  187  1                                  16
HELIX   36  36 ILE C  212  GLY C  233  1                                  22
HELIX   37  37 THR C  258  GLU C  263  1                                   6
HELIX   38  38 GLY C  266  LYS C  279  1                                  14
HELIX   39  39 ARG C  280  TYR C  288  1                                   9
HELIX   40  40 ASP C  295  ARG C  299  5                                   5
HELIX   41  41 PRO C  326  LYS C  333  1                                   8
HELIX   42  42 ASP C  347  LEU C  360  1                                  14
HELIX   43  43 ALA D    5  LEU D    9  5                                   5
HELIX   44  44 ASN D   10  SER D   19  1                                  10
HELIX   45  45 GLY D   53  LEU D   57  5                                   5
HELIX   46  46 SER D   65  THR D   67  5                                   3
HELIX   47  47 LEU D  113  MET D  123  1                                  11
HELIX   48  48 VAL D  124  HIS D  128  5                                   5
HELIX   49  49 GLY D  172  GLY D  187  1                                  16
HELIX   50  50 ILE D  212  GLY D  233  1                                  22
HELIX   51  51 THR D  258  GLU D  263  1                                   6
HELIX   52  52 GLY D  266  LYS D  279  1                                  14
HELIX   53  53 ARG D  280  TYR D  288  1                                   9
HELIX   54  54 ASP D  295  ARG D  299  5                                   5
HELIX   55  55 PRO D  326  LYS D  333  1                                   8
HELIX   56  56 ASP D  347  LEU D  360  1                                  14
HELIX   57  57 SER E    4  LEU E    9  5                                   6
HELIX   58  58 ASN E   10  SER E   19  1                                  10
HELIX   59  59 GLY E   53  LEU E   57  5                                   5
HELIX   60  60 SER E   65  PHE E   68  5                                   4
HELIX   61  61 LEU E  113  MET E  123  1                                  11
HELIX   62  62 VAL E  124  HIS E  128  5                                   5
HELIX   63  63 GLY E  172  GLY E  187  1                                  16
HELIX   64  64 ILE E  212  GLY E  233  1                                  22
HELIX   65  65 THR E  258  GLU E  263  1                                   6
HELIX   66  66 GLY E  266  LYS E  279  1                                  14
HELIX   67  67 ARG E  280  TYR E  288  1                                   9
HELIX   68  68 ASP E  295  ARG E  299  5                                   5
HELIX   69  69 PRO E  326  LYS E  333  1                                   8
HELIX   70  70 ASP E  347  LEU E  360  1                                  14
HELIX   71  71 ALA F    5  LEU F    9  5                                   5
HELIX   72  72 ASN F   10  SER F   19  1                                  10
HELIX   73  73 GLY F   53  LEU F   57  5                                   5
HELIX   74  74 SER F   65  THR F   67  5                                   3
HELIX   75  75 LEU F  113  MET F  123  1                                  11
HELIX   76  76 VAL F  124  HIS F  128  5                                   5
HELIX   77  77 GLY F  172  GLY F  187  1                                  16
HELIX   78  78 ILE F  212  GLY F  233  1                                  22
HELIX   79  79 THR F  258  GLU F  263  1                                   6
HELIX   80  80 GLY F  266  LYS F  279  1                                  14
HELIX   81  81 ARG F  280  TYR F  288  1                                   9
HELIX   82  82 ASP F  295  ARG F  299  5                                   5
HELIX   83  83 PRO F  326  LYS F  333  1                                   8
HELIX   84  84 ASP F  347  LEU F  360  1                                  14
HELIX   85  85 ALA G    5  LEU G    9  5                                   5
HELIX   86  86 ASN G   10  SER G   19  1                                  10
HELIX   87  87 GLY G   53  LEU G   57  5                                   5
HELIX   88  88 SER G   65  PHE G   68  5                                   4
HELIX   89  89 LEU G  113  MET G  123  1                                  11
HELIX   90  90 VAL G  124  HIS G  128  5                                   5
HELIX   91  91 GLY G  172  GLY G  187  1                                  16
HELIX   92  92 ILE G  212  GLY G  233  1                                  22
HELIX   93  93 THR G  258  GLU G  263  1                                   6
HELIX   94  94 GLY G  266  LYS G  279  1                                  14
HELIX   95  95 ARG G  280  TYR G  288  1                                   9
HELIX   96  96 ASP G  295  ARG G  299  5                                   5
HELIX   97  97 PRO G  326  LYS G  333  1                                   8
HELIX   98  98 ASP G  347  LEU G  360  1                                  14
HELIX   99  99 SER H    4  LEU H    9  5                                   6
HELIX  100 100 ASN H   10  SER H   19  1                                  10
HELIX  101 101 GLY H   53  LEU H   57  5                                   5
HELIX  102 102 SER H   65  THR H   67  5                                   3
HELIX  103 103 LEU H  113  VAL H  124  1                                  12
HELIX  104 104 SER H  125  HIS H  128  5                                   4
HELIX  105 105 GLY H  172  GLY H  187  1                                  16
HELIX  106 106 ILE H  212  GLY H  233  1                                  22
HELIX  107 107 THR H  258  GLU H  263  1                                   6
HELIX  108 108 GLY H  266  LYS H  279  1                                  14
HELIX  109 109 ARG H  280  TYR H  288  1                                   9
HELIX  110 110 ASP H  295  ARG H  299  5                                   5
HELIX  111 111 PRO H  326  LYS H  333  1                                   8
HELIX  112 112 ASP H  347  LEU H  360  1                                  14
HELIX  113 113 SER I    4  LEU I    9  5                                   6
HELIX  114 114 ASN I   10  SER I   19  1                                  10
HELIX  115 115 GLY I   53  LEU I   57  5                                   5
HELIX  116 116 SER I   65  PHE I   68  5                                   4
HELIX  117 117 LEU I  113  MET I  123  1                                  11
HELIX  118 118 VAL I  124  HIS I  128  5                                   5
HELIX  119 119 GLY I  172  GLY I  187  1                                  16
HELIX  120 120 ILE I  212  GLY I  233  1                                  22
HELIX  121 121 THR I  258  GLU I  263  1                                   6
HELIX  122 122 GLY I  266  LYS I  279  1                                  14
HELIX  123 123 ARG I  280  TYR I  288  1                                   9
HELIX  124 124 ASP I  295  ARG I  299  5                                   5
HELIX  125 125 PRO I  326  LYS I  333  1                                   8
HELIX  126 126 ASP I  347  LEU I  360  1                                  14
HELIX  127 127 SER J    4  LEU J    9  5                                   6
HELIX  128 128 ASN J   10  SER J   19  1                                  10
HELIX  129 129 GLY J   53  LEU J   57  5                                   5
HELIX  130 130 SER J   65  THR J   67  5                                   3
HELIX  131 131 LEU J  113  MET J  123  1                                  11
HELIX  132 132 VAL J  124  HIS J  128  5                                   5
HELIX  133 133 GLY J  172  GLY J  187  1                                  16
HELIX  134 134 ILE J  212  GLY J  233  1                                  22
HELIX  135 135 THR J  258  GLU J  263  1                                   6
HELIX  136 136 GLY J  266  LYS J  279  1                                  14
HELIX  137 137 ARG J  280  TYR J  288  1                                   9
HELIX  138 138 ASP J  295  ARG J  299  5                                   5
HELIX  139 139 PRO J  326  LYS J  333  1                                   8
HELIX  140 140 ASP J  347  LEU J  360  1                                  14
HELIX  141 141 ALA K    5  LEU K    9  5                                   5
HELIX  142 142 ASN K   10  SER K   19  1                                  10
HELIX  143 143 GLY K   53  LEU K   57  5                                   5
HELIX  144 144 SER K   65  PHE K   68  5                                   4
HELIX  145 145 LEU K  113  MET K  123  1                                  11
HELIX  146 146 VAL K  124  HIS K  128  5                                   5
HELIX  147 147 GLY K  172  GLY K  187  1                                  16
HELIX  148 148 ILE K  212  GLY K  233  1                                  22
HELIX  149 149 THR K  258  GLU K  263  1                                   6
HELIX  150 150 GLY K  266  LYS K  279  1                                  14
HELIX  151 151 ARG K  280  TYR K  288  1                                   9
HELIX  152 152 ASP K  295  ARG K  299  5                                   5
HELIX  153 153 PRO K  326  LYS K  333  1                                   8
HELIX  154 154 ASP K  347  LEU K  360  1                                  14
HELIX  155 155 ALA L    5  LEU L    9  5                                   5
HELIX  156 156 ASN L   10  SER L   19  1                                  10
HELIX  157 157 GLY L   53  LEU L   57  5                                   5
HELIX  158 158 SER L   65  PHE L   68  5                                   4
HELIX  159 159 LEU L  113  MET L  123  1                                  11
HELIX  160 160 VAL L  124  HIS L  128  5                                   5
HELIX  161 161 GLY L  172  GLY L  187  1                                  16
HELIX  162 162 ILE L  212  GLY L  233  1                                  22
HELIX  163 163 THR L  258  GLU L  263  1                                   6
HELIX  164 164 GLY L  266  LYS L  279  1                                  14
HELIX  165 165 ARG L  280  TYR L  288  1                                   9
HELIX  166 166 ASP L  295  ARG L  299  5                                   5
HELIX  167 167 PRO L  326  LYS L  333  1                                   8
HELIX  168 168 ASP L  347  LEU L  360  1                                  14
HELIX  169 169 ALA M    5  LEU M    9  5                                   5
HELIX  170 170 ASN M   10  SER M   19  1                                  10
HELIX  171 171 GLY M   53  LEU M   57  5                                   5
HELIX  172 172 SER M   65  THR M   67  5                                   3
HELIX  173 173 LEU M  113  VAL M  124  1                                  12
HELIX  174 174 SER M  125  HIS M  128  5                                   4
HELIX  175 175 GLY M  172  GLY M  187  1                                  16
HELIX  176 176 ILE M  212  GLY M  233  1                                  22
HELIX  177 177 THR M  258  GLU M  263  1                                   6
HELIX  178 178 GLY M  266  LYS M  279  1                                  14
HELIX  179 179 ARG M  280  TYR M  288  1                                   9
HELIX  180 180 ASP M  295  ARG M  299  5                                   5
HELIX  181 181 PRO M  326  LYS M  333  1                                   8
HELIX  182 182 ASP M  347  LEU M  360  1                                  14
HELIX  183 183 ALA N    5  LEU N    9  5                                   5
HELIX  184 184 ASN N   10  SER N   19  1                                  10
HELIX  185 185 GLY N   53  LEU N   57  5                                   5
HELIX  186 186 SER N   65  THR N   67  5                                   3
HELIX  187 187 LEU N  113  MET N  123  1                                  11
HELIX  188 188 VAL N  124  HIS N  128  5                                   5
HELIX  189 189 GLY N  172  GLY N  187  1                                  16
HELIX  190 190 ILE N  212  GLY N  233  1                                  22
HELIX  191 191 THR N  258  GLU N  263  1                                   6
HELIX  192 192 GLY N  266  LYS N  279  1                                  14
HELIX  193 193 ARG N  280  TYR N  288  1                                   9
HELIX  194 194 ASP N  295  ARG N  299  5                                   5
HELIX  195 195 PRO N  326  LYS N  333  1                                   8
HELIX  196 196 ASP N  347  LEU N  360  1                                  14
HELIX  197 197 ALA O    5  LEU O    9  5                                   5
HELIX  198 198 ASN O   10  SER O   19  1                                  10
HELIX  199 199 GLY O   53  LEU O   57  5                                   5
HELIX  200 200 SER O   65  PHE O   68  5                                   4
HELIX  201 201 LEU O  113  VAL O  124  1                                  12
HELIX  202 202 SER O  125  HIS O  128  5                                   4
HELIX  203 203 GLY O  172  GLY O  187  1                                  16
HELIX  204 204 ILE O  212  GLY O  233  1                                  22
HELIX  205 205 THR O  258  GLU O  263  1                                   6
HELIX  206 206 GLY O  266  LYS O  279  1                                  14
HELIX  207 207 ARG O  280  TYR O  288  1                                   9
HELIX  208 208 ASP O  295  ARG O  299  5                                   5
HELIX  209 209 PRO O  326  LYS O  333  1                                   8
HELIX  210 210 ASP O  347  LEU O  360  1                                  14
SHEET    1  AA12 TRP A  60  ASP A  63  0
SHEET    2  AA12 ASP A  76  ARG A  86 -1  O  MET A  77   N  PHE A  62
SHEET    3  AA12 LYS A  95  PHE A 102 -1  O  LEU A  96   N  PHE A  85
SHEET    4  AA12 VAL A  26  ILE A  33  1  O  GLN A  27   N  LYS A  95
SHEET    5  AA12 LEU A  40  LEU A  47 -1  O  ARG A  41   N  TRP A  32
SHEET    6  AA12 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46
SHEET    7  AA12 GLN B 201  GLU B 210 -1  O  GLU B 203   N  ASN B 194
SHEET    8  AA12 TRP B 130  MET B 140 -1  O  PHE B 131   N  CYS B 209
SHEET    9  AA12 CYS B 252  SER B 257 -1  O  HIS B 253   N  GLU B 134
SHEET   10  AA12 PHE B 337  ASP B 339 -1  O  PHE B 337   N  PHE B 256
SHEET   11  AA12 ILE B 323  ILE B 325 -1  O  ARG B 324   N  GLU B 338
SHEET   12  AA12 ALA B 314  VAL B 316  1  O  GLY B 315   N  ILE B 325
SHEET    1  AB 9 TRP A  60  ASP A  63  0
SHEET    2  AB 9 ASP A  76  ARG A  86 -1  O  MET A  77   N  PHE A  62
SHEET    3  AB 9 LYS A  95  PHE A 102 -1  O  LEU A  96   N  PHE A  85
SHEET    4  AB 9 VAL A  26  ILE A  33  1  O  GLN A  27   N  LYS A  95
SHEET    5  AB 9 LEU A  40  LEU A  47 -1  O  ARG A  41   N  TRP A  32
SHEET    6  AB 9 ILE B 190  ALA B 195 -1  O  ALA B 191   N  THR A  46
SHEET    7  AB 9 GLN B 201  GLU B 210 -1  O  GLU B 203   N  ASN B 194
SHEET    8  AB 9 TRP B 130  MET B 140 -1  O  PHE B 131   N  CYS B 209
SHEET    9  AB 9 ILE B 235  THR B 237 -1  O  ILE B 235   N  MET B 140
SHEET    1  AC 6 ILE A 235  THR A 237  0
SHEET    2  AC 6 TRP A 130  MET A 140 -1  O  THR A 138   N  THR A 237
SHEET    3  AC 6 CYS A 252  SER A 257 -1  O  HIS A 253   N  GLU A 134
SHEET    4  AC 6 PHE A 337  ASP A 339 -1  O  PHE A 337   N  PHE A 256
SHEET    5  AC 6 ILE A 323  ILE A 325 -1  O  ARG A 324   N  GLU A 338
SHEET    6  AC 6 ALA A 314  VAL A 316  1  O  GLY A 315   N  ILE A 325
SHEET    1  AD 9 ILE A 235  THR A 237  0
SHEET    2  AD 9 TRP A 130  MET A 140 -1  O  THR A 138   N  THR A 237
SHEET    3  AD 9 GLN A 201  GLU A 210 -1  O  TRP A 202   N  TYR A 137
SHEET    4  AD 9 ILE A 190  ALA A 195 -1  N  ALA A 191   O  GLN A 205
SHEET    5  AD 9 LEU E  40  LEU E  47 -1  O  THR E  44   N  THR A 193
SHEET    6  AD 9 VAL E  26  ILE E  33 -1  O  VAL E  26   N  LEU E  47
SHEET    7  AD 9 LYS E  95  PHE E 102  1  O  LYS E  95   N  MET E  29
SHEET    8  AD 9 ASP E  76  ARG E  86 -1  O  TYR E  78   N  PHE E 102
SHEET    9  AD 9 TRP E  60  ASP E  63 -1  O  TRP E  60   N  LEU E  79
SHEET    1  BA12 TRP B  60  ASP B  63  0
SHEET    2  BA12 ASP B  76  ARG B  86 -1  O  MET B  77   N  PHE B  62
SHEET    3  BA12 LYS B  95  PHE B 102 -1  O  LEU B  96   N  PHE B  85
SHEET    4  BA12 VAL B  26  ILE B  33  1  O  GLN B  27   N  LYS B  95
SHEET    5  BA12 LEU B  40  LEU B  47 -1  O  ARG B  41   N  TRP B  32
SHEET    6  BA12 ILE C 190  ALA C 195 -1  O  ALA C 191   N  THR B  46
SHEET    7  BA12 GLN C 201  GLU C 210 -1  O  GLU C 203   N  ASN C 194
SHEET    8  BA12 TRP C 130  MET C 140 -1  O  PHE C 131   N  CYS C 209
SHEET    9  BA12 CYS C 252  SER C 257 -1  O  HIS C 253   N  GLU C 134
SHEET   10  BA12 PHE C 337  ASP C 339 -1  O  PHE C 337   N  PHE C 256
SHEET   11  BA12 ILE C 323  ILE C 325 -1  O  ARG C 324   N  GLU C 338
SHEET   12  BA12 ALA C 314  VAL C 316  1  O  GLY C 315   N  ILE C 325
SHEET    1  BB 9 TRP B  60  ASP B  63  0
SHEET    2  BB 9 ASP B  76  ARG B  86 -1  O  MET B  77   N  PHE B  62
SHEET    3  BB 9 LYS B  95  PHE B 102 -1  O  LEU B  96   N  PHE B  85
SHEET    4  BB 9 VAL B  26  ILE B  33  1  O  GLN B  27   N  LYS B  95
SHEET    5  BB 9 LEU B  40  LEU B  47 -1  O  ARG B  41   N  TRP B  32
SHEET    6  BB 9 ILE C 190  ALA C 195 -1  O  ALA C 191   N  THR B  46
SHEET    7  BB 9 GLN C 201  GLU C 210 -1  O  GLU C 203   N  ASN C 194
SHEET    8  BB 9 TRP C 130  MET C 140 -1  O  PHE C 131   N  CYS C 209
SHEET    9  BB 9 ILE C 235  THR C 237 -1  O  ILE C 235   N  MET C 140
SHEET    1  CA15 TRP C  60  ASP C  63  0
SHEET    2  CA15 ASP C  76  ARG C  86 -1  O  MET C  77   N  PHE C  62
SHEET    3  CA15 LYS C  95  PHE C 102 -1  O  LEU C  96   N  PHE C  85
SHEET    4  CA15 VAL C  26  ILE C  33  1  O  GLN C  27   N  LYS C  95
SHEET    5  CA15 LEU C  40  LEU C  47 -1  O  ARG C  41   N  TRP C  32
SHEET    6  CA15 ILE D 190  ALA D 195 -1  O  ALA D 191   N  THR C  46
SHEET    7  CA15 GLN D 201  GLU D 210 -1  O  GLU D 203   N  ASN D 194
SHEET    8  CA15 TRP D 130  MET D 140 -1  O  PHE D 131   N  CYS D 209
SHEET    9  CA15 ILE D 235  THR D 237 -1  O  ILE D 235   N  MET D 140
SHEET   10  CA15 TRP D 130  MET D 140 -1  O  THR D 138   N  THR D 237
SHEET   11  CA15 ALA D 314  VAL D 316
SHEET   12  CA15 ILE D 323  ILE D 325  1  O  ILE D 323   N  GLY D 315
SHEET   13  CA15 PHE D 337  ASP D 339 -1  O  GLU D 338   N  ARG D 324
SHEET   14  CA15 CYS D 252  SER D 257 -1  O  THR D 254   N  ASP D 339
SHEET   15  CA15 TRP D 130  MET D 140 -1  O  TRP D 130   N  SER D 257
SHEET    1  DA15 TRP D  60  ASP D  63  0
SHEET    2  DA15 ASP D  76  ARG D  86 -1  O  MET D  77   N  PHE D  62
SHEET    3  DA15 LYS D  95  PHE D 102 -1  O  LEU D  96   N  PHE D  85
SHEET    4  DA15 VAL D  26  ILE D  33  1  O  GLN D  27   N  LYS D  95
SHEET    5  DA15 LEU D  40  LEU D  47 -1  O  ARG D  41   N  TRP D  32
SHEET    6  DA15 ILE E 190  ALA E 195 -1  O  ALA E 191   N  THR D  46
SHEET    7  DA15 GLN E 201  GLU E 210 -1  O  GLU E 203   N  ASN E 194
SHEET    8  DA15 TRP E 130  MET E 140 -1  O  PHE E 131   N  CYS E 209
SHEET    9  DA15 ILE E 235  THR E 237 -1  O  ILE E 235   N  MET E 140
SHEET   10  DA15 TRP E 130  MET E 140 -1  O  THR E 138   N  THR E 237
SHEET   11  DA15 ALA E 314  VAL E 316
SHEET   12  DA15 ILE E 323  ILE E 325  1  O  ILE E 323   N  GLY E 315
SHEET   13  DA15 PHE E 337  ASP E 339 -1  O  GLU E 338   N  ARG E 324
SHEET   14  DA15 CYS E 252  SER E 257 -1  O  THR E 254   N  ASP E 339
SHEET   15  DA15 TRP E 130  MET E 140 -1  O  TRP E 130   N  SER E 257
SHEET    1  FA15 TRP F  60  ASP F  63  0
SHEET    2  FA15 ASP F  76  ARG F  86 -1  O  MET F  77   N  PHE F  62
SHEET    3  FA15 LYS F  95  PHE F 102 -1  O  LEU F  96   N  PHE F  85
SHEET    4  FA15 VAL F  26  ILE F  33  1  O  GLN F  27   N  LYS F  95
SHEET    5  FA15 LEU F  40  LEU F  47 -1  O  ARG F  41   N  TRP F  32
SHEET    6  FA15 ILE G 190  ALA G 195 -1  O  ALA G 191   N  THR F  46
SHEET    7  FA15 GLN G 201  GLU G 210 -1  O  GLU G 203   N  ASN G 194
SHEET    8  FA15 TRP G 130  MET G 140 -1  O  PHE G 131   N  CYS G 209
SHEET    9  FA15 ILE G 235  THR G 237 -1  O  ILE G 235   N  MET G 140
SHEET   10  FA15 TRP G 130  MET G 140 -1  O  THR G 138   N  THR G 237
SHEET   11  FA15 ALA G 314  VAL G 316
SHEET   12  FA15 ILE G 323  ILE G 325  1  O  ILE G 323   N  GLY G 315
SHEET   13  FA15 PHE G 337  ASP G 339 -1  O  GLU G 338   N  ARG G 324
SHEET   14  FA15 CYS G 252  SER G 257 -1  O  THR G 254   N  ASP G 339
SHEET   15  FA15 TRP G 130  MET G 140 -1  O  TRP G 130   N  SER G 257
SHEET    1  FB15 ILE F 235  THR F 237  0
SHEET    2  FB15 TRP F 130  MET F 140 -1  O  THR F 138   N  THR F 237
SHEET    3  FB15 ALA F 314  VAL F 316
SHEET    4  FB15 ILE F 323  ILE F 325  1  O  ILE F 323   N  GLY F 315
SHEET    5  FB15 PHE F 337  ASP F 339 -1  O  GLU F 338   N  ARG F 324
SHEET    6  FB15 CYS F 252  SER F 257 -1  O  THR F 254   N  ASP F 339
SHEET    7  FB15 TRP F 130  MET F 140 -1  O  TRP F 130   N  SER F 257
SHEET    8  FB15 TRP J  60  ASP J  63
SHEET    9  FB15 ASP J  76  ARG J  86 -1  O  MET J  77   N  PHE J  62
SHEET   10  FB15 LYS J  95  PHE J 102 -1  O  LEU J  96   N  PHE J  85
SHEET   11  FB15 VAL J  26  ILE J  33  1  O  GLN J  27   N  LYS J  95
SHEET   12  FB15 LEU J  40  LEU J  47 -1  O  ARG J  41   N  TRP J  32
SHEET   13  FB15 ILE F 190  ALA F 195 -1  O  ALA F 191   N  THR J  46
SHEET   14  FB15 GLN F 201  GLU F 210 -1  O  GLU F 203   N  ASN F 194
SHEET   15  FB15 TRP F 130  MET F 140 -1  O  PHE F 131   N  CYS F 209
SHEET    1  GA15 TRP G  60  ASP G  63  0
SHEET    2  GA15 ASP G  76  ARG G  86 -1  O  MET G  77   N  PHE G  62
SHEET    3  GA15 LYS G  95  PHE G 102 -1  O  LEU G  96   N  PHE G  85
SHEET    4  GA15 VAL G  26  ILE G  33  1  O  GLN G  27   N  LYS G  95
SHEET    5  GA15 LEU G  40  LEU G  47 -1  O  ARG G  41   N  TRP G  32
SHEET    6  GA15 ILE H 190  ALA H 195 -1  O  ALA H 191   N  THR G  46
SHEET    7  GA15 GLN H 201  GLU H 210 -1  O  GLU H 203   N  ASN H 194
SHEET    8  GA15 TRP H 130  MET H 140 -1  O  PHE H 131   N  CYS H 209
SHEET    9  GA15 ILE H 235  THR H 237 -1  O  ILE H 235   N  MET H 140
SHEET   10  GA15 TRP H 130  MET H 140 -1  O  THR H 138   N  THR H 237
SHEET   11  GA15 ALA H 314  VAL H 316
SHEET   12  GA15 ILE H 323  ILE H 325  1  O  ILE H 323   N  GLY H 315
SHEET   13  GA15 PHE H 337  ASP H 339 -1  O  GLU H 338   N  ARG H 324
SHEET   14  GA15 CYS H 252  SER H 257 -1  O  THR H 254   N  ASP H 339
SHEET   15  GA15 TRP H 130  MET H 140 -1  O  TRP H 130   N  SER H 257
SHEET    1  HA15 TRP H  60  ASP H  63  0
SHEET    2  HA15 ASP H  76  ARG H  86 -1  O  MET H  77   N  PHE H  62
SHEET    3  HA15 LYS H  95  PHE H 102 -1  O  LEU H  96   N  PHE H  85
SHEET    4  HA15 VAL H  26  ILE H  33  1  O  GLN H  27   N  LYS H  95
SHEET    5  HA15 LEU H  40  LEU H  47 -1  O  ARG H  41   N  TRP H  32
SHEET    6  HA15 ILE I 190  ALA I 195 -1  O  ALA I 191   N  THR H  46
SHEET    7  HA15 GLN I 201  GLU I 210 -1  O  GLU I 203   N  ASN I 194
SHEET    8  HA15 TRP I 130  MET I 140 -1  O  PHE I 131   N  CYS I 209
SHEET    9  HA15 ILE I 235  THR I 237 -1  O  ILE I 235   N  MET I 140
SHEET   10  HA15 TRP I 130  MET I 140 -1  O  THR I 138   N  THR I 237
SHEET   11  HA15 ALA I 314  VAL I 316
SHEET   12  HA15 ILE I 323  ILE I 325  1  O  ILE I 323   N  GLY I 315
SHEET   13  HA15 PHE I 337  ASP I 339 -1  O  GLU I 338   N  ARG I 324
SHEET   14  HA15 CYS I 252  SER I 257 -1  O  THR I 254   N  ASP I 339
SHEET   15  HA15 TRP I 130  MET I 140 -1  O  TRP I 130   N  SER I 257
SHEET    1  IA15 TRP I  60  ASP I  63  0
SHEET    2  IA15 ASP I  76  ARG I  86 -1  O  MET I  77   N  PHE I  62
SHEET    3  IA15 LYS I  95  PHE I 102 -1  O  LEU I  96   N  PHE I  85
SHEET    4  IA15 VAL I  26  ILE I  33  1  O  GLN I  27   N  LYS I  95
SHEET    5  IA15 LEU I  40  LEU I  47 -1  O  ARG I  41   N  TRP I  32
SHEET    6  IA15 ILE J 190  ALA J 195 -1  O  ALA J 191   N  THR I  46
SHEET    7  IA15 GLN J 201  GLU J 210 -1  O  GLU J 203   N  ASN J 194
SHEET    8  IA15 TRP J 130  MET J 140 -1  O  PHE J 131   N  CYS J 209
SHEET    9  IA15 ILE J 235  THR J 237 -1  O  ILE J 235   N  MET J 140
SHEET   10  IA15 TRP J 130  MET J 140 -1  O  THR J 138   N  THR J 237
SHEET   11  IA15 ALA J 314  VAL J 316
SHEET   12  IA15 ILE J 323  ILE J 325  1  O  ILE J 323   N  GLY J 315
SHEET   13  IA15 PHE J 337  ASP J 339 -1  O  GLU J 338   N  ARG J 324
SHEET   14  IA15 CYS J 252  SER J 257 -1  O  THR J 254   N  ASP J 339
SHEET   15  IA15 TRP J 130  MET J 140 -1  O  TRP J 130   N  SER J 257
SHEET    1  KA15 TRP K  60  ASP K  63  0
SHEET    2  KA15 ASP K  76  ARG K  86 -1  O  MET K  77   N  PHE K  62
SHEET    3  KA15 LYS K  95  PHE K 102 -1  O  LEU K  96   N  PHE K  85
SHEET    4  KA15 VAL K  26  ILE K  33  1  O  GLN K  27   N  LYS K  95
SHEET    5  KA15 LEU K  40  LEU K  47 -1  O  ARG K  41   N  TRP K  32
SHEET    6  KA15 ILE L 190  ALA L 195 -1  O  ALA L 191   N  THR K  46
SHEET    7  KA15 GLN L 201  GLU L 210 -1  O  GLU L 203   N  ASN L 194
SHEET    8  KA15 TRP L 130  MET L 140 -1  O  PHE L 131   N  CYS L 209
SHEET    9  KA15 ILE L 235  THR L 237 -1  O  ILE L 235   N  MET L 140
SHEET   10  KA15 TRP L 130  MET L 140 -1  O  THR L 138   N  THR L 237
SHEET   11  KA15 ALA L 314  VAL L 316
SHEET   12  KA15 ILE L 323  ILE L 325  1  O  ILE L 323   N  GLY L 315
SHEET   13  KA15 PHE L 337  ASP L 339 -1  O  GLU L 338   N  ARG L 324
SHEET   14  KA15 CYS L 252  SER L 257 -1  O  THR L 254   N  ASP L 339
SHEET   15  KA15 TRP L 130  MET L 140 -1  O  TRP L 130   N  SER L 257
SHEET    1  KB15 ILE K 235  THR K 237  0
SHEET    2  KB15 TRP K 130  MET K 140 -1  O  THR K 138   N  THR K 237
SHEET    3  KB15 ALA K 314  VAL K 316
SHEET    4  KB15 ILE K 323  ILE K 325  1  O  ILE K 323   N  GLY K 315
SHEET    5  KB15 PHE K 337  ASP K 339 -1  O  GLU K 338   N  ARG K 324
SHEET    6  KB15 CYS K 252  SER K 257 -1  O  THR K 254   N  ASP K 339
SHEET    7  KB15 TRP K 130  MET K 140 -1  O  TRP K 130   N  SER K 257
SHEET    8  KB15 TRP O  60  ASP O  63
SHEET    9  KB15 ASP O  76  ARG O  86 -1  O  MET O  77   N  PHE O  62
SHEET   10  KB15 LYS O  95  PHE O 102 -1  O  LEU O  96   N  PHE O  85
SHEET   11  KB15 VAL O  26  ILE O  33  1  O  GLN O  27   N  LYS O  95
SHEET   12  KB15 LEU O  40  LEU O  47 -1  O  ARG O  41   N  TRP O  32
SHEET   13  KB15 ILE K 190  ALA K 195 -1  O  ALA K 191   N  THR O  46
SHEET   14  KB15 GLN K 201  GLU K 210 -1  O  GLU K 203   N  ASN K 194
SHEET   15  KB15 TRP K 130  MET K 140 -1  O  PHE K 131   N  CYS K 209
SHEET    1  LA15 TRP L  60  ASP L  63  0
SHEET    2  LA15 ASP L  76  ARG L  86 -1  O  MET L  77   N  PHE L  62
SHEET    3  LA15 LYS L  95  PHE L 102 -1  O  LEU L  96   N  PHE L  85
SHEET    4  LA15 VAL L  26  ILE L  33  1  O  GLN L  27   N  LYS L  95
SHEET    5  LA15 LEU L  40  LEU L  47 -1  O  ARG L  41   N  TRP L  32
SHEET    6  LA15 ILE M 190  ALA M 195 -1  O  ALA M 191   N  THR L  46
SHEET    7  LA15 GLN M 201  GLU M 210 -1  O  GLU M 203   N  ASN M 194
SHEET    8  LA15 TRP M 130  MET M 140 -1  O  PHE M 131   N  CYS M 209
SHEET    9  LA15 ILE M 235  THR M 237 -1  O  ILE M 235   N  MET M 140
SHEET   10  LA15 TRP M 130  MET M 140 -1  O  THR M 138   N  THR M 237
SHEET   11  LA15 ALA M 314  VAL M 316
SHEET   12  LA15 ILE M 323  ILE M 325  1  O  ILE M 323   N  GLY M 315
SHEET   13  LA15 PHE M 337  ASP M 339 -1  O  GLU M 338   N  ARG M 324
SHEET   14  LA15 CYS M 252  SER M 257 -1  O  THR M 254   N  ASP M 339
SHEET   15  LA15 TRP M 130  MET M 140 -1  O  TRP M 130   N  SER M 257
SHEET    1  MA15 TRP M  60  ASP M  63  0
SHEET    2  MA15 ASP M  76  ARG M  86 -1  O  MET M  77   N  PHE M  62
SHEET    3  MA15 LYS M  95  PHE M 102 -1  O  LEU M  96   N  PHE M  85
SHEET    4  MA15 VAL M  26  ILE M  33  1  O  GLN M  27   N  LYS M  95
SHEET    5  MA15 LEU M  40  LEU M  47 -1  O  ARG M  41   N  TRP M  32
SHEET    6  MA15 ILE N 190  ALA N 195 -1  O  ALA N 191   N  THR M  46
SHEET    7  MA15 GLN N 201  GLU N 210 -1  O  GLU N 203   N  ASN N 194
SHEET    8  MA15 TRP N 130  MET N 140 -1  O  PHE N 131   N  CYS N 209
SHEET    9  MA15 ILE N 235  THR N 237 -1  O  ILE N 235   N  MET N 140
SHEET   10  MA15 TRP N 130  MET N 140 -1  O  THR N 138   N  THR N 237
SHEET   11  MA15 ALA N 314  VAL N 316
SHEET   12  MA15 ILE N 323  ILE N 325  1  O  ILE N 323   N  GLY N 315
SHEET   13  MA15 PHE N 337  ASP N 339 -1  O  GLU N 338   N  ARG N 324
SHEET   14  MA15 CYS N 252  SER N 257 -1  O  THR N 254   N  ASP N 339
SHEET   15  MA15 TRP N 130  MET N 140 -1  O  TRP N 130   N  SER N 257
SHEET    1  NA15 TRP N  60  ASP N  63  0
SHEET    2  NA15 ASP N  76  ARG N  86 -1  O  MET N  77   N  PHE N  62
SHEET    3  NA15 LYS N  95  PHE N 102 -1  O  LEU N  96   N  PHE N  85
SHEET    4  NA15 VAL N  26  ILE N  33  1  O  GLN N  27   N  LYS N  95
SHEET    5  NA15 LEU N  40  LEU N  47 -1  O  ARG N  41   N  TRP N  32
SHEET    6  NA15 ILE O 190  ALA O 195 -1  O  ALA O 191   N  THR N  46
SHEET    7  NA15 GLN O 201  GLU O 210 -1  O  GLU O 203   N  ASN O 194
SHEET    8  NA15 TRP O 130  MET O 140 -1  O  PHE O 131   N  CYS O 209
SHEET    9  NA15 ILE O 235  THR O 237 -1  O  ILE O 235   N  MET O 140
SHEET   10  NA15 TRP O 130  MET O 140 -1  O  THR O 138   N  THR O 237
SHEET   11  NA15 ALA O 314  VAL O 316
SHEET   12  NA15 ILE O 323  ILE O 325  1  O  ILE O 323   N  GLY O 315
SHEET   13  NA15 PHE O 337  ASP O 339 -1  O  GLU O 338   N  ARG O 324
SHEET   14  NA15 CYS O 252  SER O 257 -1  O  THR O 254   N  ASP O 339
SHEET   15  NA15 TRP O 130  MET O 140 -1  O  TRP O 130   N  SER O 257
LINK        MG    MG A 401                 OE2 GLU A 196     1555   1555  2.33
LINK        MG    MG A 401                 OE1 GLU A 136     1555   1555  2.48
LINK        MG    MG A 401                 OE1 GLU A 203     1555   1555  1.91
LINK        MG    MG B 401                 OE2 GLU B 196     1555   1555  2.39
LINK        MG    MG B 401                 OE1 GLU B 203     1555   1555  1.94
LINK        MG    MG B 401                 OE1 GLU B 136     1555   1555  2.43
LINK        MG    MG C 401                 OE1 GLU C 136     1555   1555  2.55
LINK        MG    MG C 401                 OE1 GLU C 203     1555   1555  2.03
LINK        MG    MG C 401                 OE2 GLU C 196     1555   1555  2.39
LINK        MG    MG D 401                 OE2 GLU D 196     1555   1555  2.44
LINK        MG    MG D 401                 OE1 GLU D 136     1555   1555  2.32
LINK        MG    MG D 401                 OE1 GLU D 203     1555   1555  1.94
LINK        MG    MG E 401                 OE1 GLU E 203     1555   1555  1.96
LINK        MG    MG E 401                 OE1 GLU E 136     1555   1555  2.25
LINK        MG    MG E 401                 OE2 GLU E 196     1555   1555  2.38
LINK        MG    MG F 401                 OE1 GLU F 136     1555   1555  2.48
LINK        MG    MG F 401                 OE2 GLU F 196     1555   1555  2.38
LINK        MG    MG F 401                 OE1 GLU F 203     1555   1555  2.09
LINK        MG    MG G 401                 OE1 GLU G 136     1555   1555  2.35
LINK        MG    MG G 401                 OE2 GLU G 196     1555   1555  2.47
LINK        MG    MG G 401                 OE1 GLU G 203     1555   1555  1.95
LINK        MG    MG H 401                 OE1 GLU H 136     1555   1555  2.37
LINK        MG    MG H 401                 OE1 GLU H 203     1555   1555  1.87
LINK        MG    MG H 401                 OE2 GLU H 196     1555   1555  2.36
LINK        MG    MG I 401                 OE2 GLU I 196     1555   1555  2.67
LINK        MG    MG I 401                 OE1 GLU I 203     1555   1555  1.94
LINK        MG    MG I 401                 OE1 GLU I 136     1555   1555  2.35
LINK        MG    MG J 401                 OE2 GLU J 196     1555   1555  2.48
LINK        MG    MG J 401                 OE1 GLU J 203     1555   1555  2.00
LINK        MG    MG J 401                 OE1 GLU J 136     1555   1555  2.43
LINK        MG    MG K 401                 OE1 GLU K 203     1555   1555  1.94
LINK        MG    MG K 401                 OE2 GLU K 196     1555   1555  2.28
LINK        MG    MG K 401                 OE1 GLU K 136     1555   1555  2.29
LINK        MG    MG L 401                 OE1 GLU L 203     1555   1555  2.01
LINK        MG    MG L 401                 OE1 GLU L 136     1555   1555  2.47
LINK        MG    MG L 401                 OE2 GLU L 196     1555   1555  2.37
LINK        MG    MG M 401                 OE1 GLU M 136     1555   1555  2.39
LINK        MG    MG M 401                 OE1 GLU M 203     1555   1555  1.96
LINK        MG    MG M 401                 OE2 GLU M 196     1555   1555  2.37
LINK        MG    MG N 401                 OE2 GLU N 196     1555   1555  2.60
LINK        MG    MG N 401                 OE1 GLU N 136     1555   1555  2.43
LINK        MG    MG N 401                 OE1 GLU N 203     1555   1555  1.87
LINK        MG    MG O 401                 OE2 GLU O 196     1555   1555  2.50
LINK        MG    MG O 401                 OE1 GLU O 203     1555   1555  1.91
LINK        MG    MG O 401                 OE1 GLU O 136     1555   1555  2.30
CISPEP   1 ASP A   92    PRO A   93          0         0.39
CISPEP   2 GLY A  207    PRO A  208          0        -0.92
CISPEP   3 ASP B   92    PRO B   93          0         3.71
CISPEP   4 GLY B  207    PRO B  208          0         1.27
CISPEP   5 ASP C   92    PRO C   93          0         4.38
CISPEP   6 GLY C  207    PRO C  208          0         0.96
CISPEP   7 ASP D   92    PRO D   93          0         2.20
CISPEP   8 GLY D  207    PRO D  208          0         2.19
CISPEP   9 ASP E   92    PRO E   93          0         3.88
CISPEP  10 GLY E  207    PRO E  208          0         0.49
CISPEP  11 ASP F   92    PRO F   93          0         2.91
CISPEP  12 GLY F  207    PRO F  208          0        -0.96
CISPEP  13 ASP G   92    PRO G   93          0         2.30
CISPEP  14 GLY G  207    PRO G  208          0         0.75
CISPEP  15 ASP H   92    PRO H   93          0         4.53
CISPEP  16 GLY H  207    PRO H  208          0         0.43
CISPEP  17 ASP I   92    PRO I   93          0         4.09
CISPEP  18 GLY I  207    PRO I  208          0        -2.26
CISPEP  19 ASP J   92    PRO J   93          0         1.99
CISPEP  20 GLY J  207    PRO J  208          0         0.37
CISPEP  21 ASP K   92    PRO K   93          0         1.44
CISPEP  22 GLY K  207    PRO K  208          0         0.38
CISPEP  23 ASP L   92    PRO L   93          0         2.18
CISPEP  24 GLY L  207    PRO L  208          0         1.28
CISPEP  25 ASP M   92    PRO M   93          0         2.71
CISPEP  26 GLY M  207    PRO M  208          0         0.71
CISPEP  27 ASP N   92    PRO N   93          0         0.98
CISPEP  28 GLY N  207    PRO N  208          0         1.59
CISPEP  29 ASP O   92    PRO O   93          0         2.33
CISPEP  30 GLY O  207    PRO O  208          0         0.99
SITE     1 AC1  4 MET A  29  LYS A  43  THR A  44  THR B 193
SITE     1 AC2  2 THR B  44  THR C 193
SITE     1 AC3  3 LYS C  43  THR C  44  THR D 193
SITE     1 AC4  3 MET D  29  THR D  44  THR E 193
SITE     1 AC5  2 THR A 193  THR E  44
SITE     1 AC6  3 LYS F  43  THR F  44  THR G 193
SITE     1 AC7  3 MET G  29  THR G  44  THR H 193
SITE     1 AC8  4 MET H  29  LYS H  43  THR H  44  THR I 193
SITE     1 AC9  3 MET I  29  THR I  44  THR J 193
SITE     1 BC1  4 THR F 193  MET J  29  LYS J  43  THR J  44
SITE     1 BC2  4 MET K  29  LYS K  43  THR K  44  THR L 193
SITE     1 BC3  2 MET L  29  THR L  44
SITE     1 BC4  3 MET M  29  THR M  44  THR N 193
SITE     1 BC5  3 MET N  29  THR N  44  THR O 193
SITE     1 BC6  2 THR K 193  THR O  44
SITE     1 BC7  3 GLU A 136  GLU A 196  GLU A 203
SITE     1 BC8  3 GLU B 136  GLU B 196  GLU B 203
SITE     1 BC9  3 GLU C 136  GLU C 196  GLU C 203
SITE     1 CC1  3 GLU D 136  GLU D 196  GLU D 203
SITE     1 CC2  3 GLU E 136  GLU E 196  GLU E 203
SITE     1 CC3  3 GLU F 136  GLU F 196  GLU F 203
SITE     1 CC4  4 GLU G 134  GLU G 136  GLU G 196  GLU G 203
SITE     1 CC5  3 GLU H 136  GLU H 196  GLU H 203
SITE     1 CC6  3 GLU I 136  GLU I 196  GLU I 203
SITE     1 CC7  3 GLU J 136  GLU J 196  GLU J 203
SITE     1 CC8  3 GLU K 136  GLU K 196  GLU K 203
SITE     1 CC9  3 GLU L 136  GLU L 196  GLU L 203
SITE     1 DC1  3 GLU M 136  GLU M 196  GLU M 203
SITE     1 DC2  4 GLU N 134  GLU N 136  GLU N 196  GLU N 203
SITE     1 DC3  3 GLU O 136  GLU O 196  GLU O 203
CRYST1  183.590  485.602  192.156  90.00  90.00  90.00 C 2 2 21    120
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      0.005447  0.000000  0.000000        0.00000
SCALE2      0.000000  0.002059  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005204        0.00000
MTRIX1   1  0.308390  0.009611  0.951211       27.30328    1
MTRIX2   1  0.080855  0.996065 -0.036278       -2.68032    1
MTRIX3   1 -0.947817  0.088098  0.306400       28.67525    1
MTRIX1   2 -0.804349  0.089814  0.587330       63.82787    1
MTRIX2   2  0.144215  0.988460  0.046348       -4.52986    1
MTRIX3   2 -0.576390  0.121982 -0.808019        9.01381    1
MTRIX1   3 -0.802277  0.134165 -0.581680       58.53264    1
MTRIX2   3  0.072441  0.989096  0.128223       -1.54064    1
MTRIX3   3  0.592541  0.060733 -0.803248      -32.18757    1
MTRIX1   4  0.310780  0.078438 -0.947240       19.23977    1
MTRIX2   4 -0.012399  0.996839  0.078477        1.10542    1
MTRIX3   4  0.950401 -0.012644  0.310771      -38.11840    1
MTRIX1   5  0.446656 -0.128672  0.885405       43.48824    1
MTRIX2   5 -0.132616 -0.988195 -0.076709      327.57129    1
MTRIX3   5  0.884823 -0.083157 -0.458447      -22.57100    1
MTRIX1   6 -0.707465 -0.053981  0.704684       82.37330    1
MTRIX2   6 -0.047005 -0.991277 -0.123126      324.32779    1
MTRIX3   6  0.705183 -0.120231  0.698757      -10.64501    1
MTRIX1   7 -0.889698 -0.004699 -0.456526       84.40288    1
MTRIX2   7  0.034176 -0.997827 -0.056332      321.54889    1
MTRIX3   7 -0.455269 -0.065721  0.887925       31.07947    1
MTRIX1   8  0.147494 -0.035618 -0.988421       45.07067    1
MTRIX2   8 -0.014022 -0.999326  0.033919      323.84741    1
MTRIX3   8 -0.988964  0.008857 -0.147894       44.06144    1
MTRIX1   9  0.981417 -0.110124 -0.157143       18.98172    1
MTRIX2   9 -0.108497 -0.993917  0.018921      327.11673    1
MTRIX3   9 -0.158270 -0.001520 -0.987395       10.78190    1
MTRIX1  10 -0.995567  0.055376  0.076031       82.50835    1
MTRIX2  10  0.061527  0.994806  0.081092       79.11620    1
MTRIX3  10 -0.071146  0.085411 -0.993802       87.07421    1
MTRIX1  11 -0.378121  0.058682 -0.923895       56.59372    1
MTRIX2  11  0.018747  0.998270  0.055734       80.57099    1
MTRIX3  11  0.925566  0.003754 -0.378567       55.61307    1
MTRIX1  12  0.762318 -0.015546 -0.647017       18.04815    1
MTRIX2  12  0.027382  0.999591  0.008245       80.15544    1
MTRIX3  12  0.646624 -0.024002  0.762431       70.42603    1
MTRIX1  13  0.849393 -0.069523  0.523162       20.83094    1
MTRIX2  13  0.076350  0.997045  0.008537       78.36236    1
MTRIX3  13 -0.522209  0.032692  0.852191      112.17180    1
MTRIX1  14 -0.233876 -0.027314  0.971883       60.71241    1
MTRIX2  14  0.083954  0.995305  0.048175       78.35348    1
MTRIX3  14 -0.968635  0.092860 -0.230485      123.65450    1
      
PROCHECK
Go to PROCHECK summary
 References