HEADER LYASE/METAL BINDING PROTEIN 15-SEP-04 1XFW
TITLE CRYSTAL STRUCTURE OF ANTHRAX EDEMA FACTOR (EF) IN COMPLEX WITH
TITLE 2 CALMODULIN AND 3'5' CYCLIC AMP (CAMP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-SENSITIVE ADENYLATE CYCLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ATP PYROPHOSPHATE-LYASE, ADENYLYL CYCLASE, EDEMA FACTOR, EF,
COMPND 5 ANTHRAX EDEMA TOXIN ADENYLATE CYCLASE COMPONENT;
COMPND 6 EC: 4.6.1.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CALMODULIN 2;
COMPND 10 CHAIN: O, P, Q, R, S, T;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_TAXID: 1392;
SOURCE 4 GENE: CYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-PROTEIN INTERACTION, LYASE-METAL BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.SHEN,N.L.ZHUKOVSKAYA,Q.GUO,J.FLORIAN,W.J.TANG
REVDAT 5 14-FEB-24 1XFW 1 REMARK SEQADV LINK
REVDAT 4 20-DEC-17 1XFW 1 JRNL
REVDAT 3 24-FEB-09 1XFW 1 VERSN
REVDAT 2 31-MAY-05 1XFW 1 TITLE
REVDAT 1 03-MAY-05 1XFW 0
JRNL AUTH Y.SHEN,N.L.ZHUKOVSKAYA,Q.GUO,J.FLORIAN,W.J.TANG
JRNL TITL CALCIUM-INDEPENDENT CALMODULIN BINDING AND TWO-METAL-ION
JRNL TITL 2 CATALYTIC MECHANISM OF ANTHRAX EDEMA FACTOR.
JRNL REF EMBO J. V. 24 929 2005
JRNL REFN ISSN 0261-4189
JRNL PMID 15719022
JRNL DOI 10.1038/SJ.EMBOJ.7600574
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 517178.020
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 106659
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 SET) : 0.266
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5372
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 15006
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE : 0.3830
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 862
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 42828
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 156
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.09000
REMARK 3 B22 (A**2) : -0.96000
REMARK 3 B33 (A**2) : 7.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM SIGMAA (A) : 0.66
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.70
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.010
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.780 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.610 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.780 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.26
REMARK 3 BSOL : 48.24
REMARK 3
REMARK 3 NCS MODEL : CONSTR
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CMP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : CMP.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030317.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 190
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MACSCIENCE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106659
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
REMARK 200 R SYM FOR SHELL (I) : 0.46500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG400, MAGNESIUM CHLORIDE, PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 160.25050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.52200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 160.25050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 92.52200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, O
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, Q
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, R
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, S
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, T
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: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 84540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -167.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, O
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, R
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 159.70352
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -92.52200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 142.45295
REMARK 350
REMARK 350 BIOMOLECULE: 8
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 84530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, Q
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -0.54698
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 142.45295
REMARK 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 84500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, T
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, S
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 159.15653
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -92.52200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 284.90590
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 24
REMARK 465 HIS A 25
REMARK 465 HIS A 26
REMARK 465 HIS A 27
REMARK 465 HIS A 28
REMARK 465 HIS A 29
REMARK 465 HIS A 30
REMARK 465 ALA A 31
REMARK 465 ALA A 32
REMARK 465 ALA A 33
REMARK 465 MET A 34
REMARK 465 ASN A 35
REMARK 465 GLU A 36
REMARK 465 HIS A 37
REMARK 465 TYR A 38
REMARK 465 THR A 39
REMARK 465 GLU A 40
REMARK 465 SER A 41
REMARK 465 ASP A 42
REMARK 465 ILE A 43
REMARK 465 LYS A 44
REMARK 465 ARG A 45
REMARK 465 ASN A 46
REMARK 465 HIS A 47
REMARK 465 LYS A 48
REMARK 465 THR A 49
REMARK 465 GLU A 50
REMARK 465 LYS A 51
REMARK 465 ASN A 52
REMARK 465 LYS A 53
REMARK 465 THR A 54
REMARK 465 GLU A 55
REMARK 465 LYS A 56
REMARK 465 GLU A 57
REMARK 465 LYS A 58
REMARK 465 PHE A 59
REMARK 465 LYS A 60
REMARK 465 ASP A 61
REMARK 465 SER A 62
REMARK 465 ILE A 63
REMARK 465 GLU A 799
REMARK 465 LYS A 800
REMARK 465 MET B 24
REMARK 465 HIS B 25
REMARK 465 HIS B 26
REMARK 465 HIS B 27
REMARK 465 HIS B 28
REMARK 465 HIS B 29
REMARK 465 HIS B 30
REMARK 465 ALA B 31
REMARK 465 ALA B 32
REMARK 465 ALA B 33
REMARK 465 MET B 34
REMARK 465 ASN B 35
REMARK 465 GLU B 36
REMARK 465 HIS B 37
REMARK 465 TYR B 38
REMARK 465 THR B 39
REMARK 465 GLU B 40
REMARK 465 SER B 41
REMARK 465 ASP B 42
REMARK 465 ILE B 43
REMARK 465 LYS B 44
REMARK 465 ARG B 45
REMARK 465 ASN B 46
REMARK 465 HIS B 47
REMARK 465 LYS B 48
REMARK 465 THR B 49
REMARK 465 GLU B 50
REMARK 465 LYS B 51
REMARK 465 ASN B 52
REMARK 465 LYS B 53
REMARK 465 THR B 54
REMARK 465 GLU B 55
REMARK 465 LYS B 56
REMARK 465 GLU B 57
REMARK 465 LYS B 58
REMARK 465 PHE B 59
REMARK 465 LYS B 60
REMARK 465 ASP B 61
REMARK 465 SER B 62
REMARK 465 ILE B 63
REMARK 465 GLU B 799
REMARK 465 LYS B 800
REMARK 465 MET C 24
REMARK 465 HIS C 25
REMARK 465 HIS C 26
REMARK 465 HIS C 27
REMARK 465 HIS C 28
REMARK 465 HIS C 29
REMARK 465 HIS C 30
REMARK 465 ALA C 31
REMARK 465 ALA C 32
REMARK 465 ALA C 33
REMARK 465 MET C 34
REMARK 465 ASN C 35
REMARK 465 GLU C 36
REMARK 465 HIS C 37
REMARK 465 TYR C 38
REMARK 465 THR C 39
REMARK 465 GLU C 40
REMARK 465 SER C 41
REMARK 465 ASP C 42
REMARK 465 ILE C 43
REMARK 465 LYS C 44
REMARK 465 ARG C 45
REMARK 465 ASN C 46
REMARK 465 HIS C 47
REMARK 465 LYS C 48
REMARK 465 THR C 49
REMARK 465 GLU C 50
REMARK 465 LYS C 51
REMARK 465 ASN C 52
REMARK 465 LYS C 53
REMARK 465 THR C 54
REMARK 465 GLU C 55
REMARK 465 LYS C 56
REMARK 465 GLU C 57
REMARK 465 LYS C 58
REMARK 465 PHE C 59
REMARK 465 LYS C 60
REMARK 465 ASP C 61
REMARK 465 SER C 62
REMARK 465 ILE C 63
REMARK 465 GLU C 799
REMARK 465 LYS C 800
REMARK 465 MET D 24
REMARK 465 HIS D 25
REMARK 465 HIS D 26
REMARK 465 HIS D 27
REMARK 465 HIS D 28
REMARK 465 HIS D 29
REMARK 465 HIS D 30
REMARK 465 ALA D 31
REMARK 465 ALA D 32
REMARK 465 ALA D 33
REMARK 465 MET D 34
REMARK 465 ASN D 35
REMARK 465 GLU D 36
REMARK 465 HIS D 37
REMARK 465 TYR D 38
REMARK 465 THR D 39
REMARK 465 GLU D 40
REMARK 465 SER D 41
REMARK 465 ASP D 42
REMARK 465 ILE D 43
REMARK 465 LYS D 44
REMARK 465 ARG D 45
REMARK 465 ASN D 46
REMARK 465 HIS D 47
REMARK 465 LYS D 48
REMARK 465 THR D 49
REMARK 465 GLU D 50
REMARK 465 LYS D 51
REMARK 465 ASN D 52
REMARK 465 LYS D 53
REMARK 465 THR D 54
REMARK 465 GLU D 55
REMARK 465 LYS D 56
REMARK 465 GLU D 57
REMARK 465 LYS D 58
REMARK 465 PHE D 59
REMARK 465 LYS D 60
REMARK 465 ASP D 61
REMARK 465 SER D 62
REMARK 465 ILE D 63
REMARK 465 GLU D 799
REMARK 465 LYS D 800
REMARK 465 MET E 24
REMARK 465 HIS E 25
REMARK 465 HIS E 26
REMARK 465 HIS E 27
REMARK 465 HIS E 28
REMARK 465 HIS E 29
REMARK 465 HIS E 30
REMARK 465 ALA E 31
REMARK 465 ALA E 32
REMARK 465 ALA E 33
REMARK 465 MET E 34
REMARK 465 ASN E 35
REMARK 465 GLU E 36
REMARK 465 HIS E 37
REMARK 465 TYR E 38
REMARK 465 THR E 39
REMARK 465 GLU E 40
REMARK 465 SER E 41
REMARK 465 ASP E 42
REMARK 465 ILE E 43
REMARK 465 LYS E 44
REMARK 465 ARG E 45
REMARK 465 ASN E 46
REMARK 465 HIS E 47
REMARK 465 LYS E 48
REMARK 465 THR E 49
REMARK 465 GLU E 50
REMARK 465 LYS E 51
REMARK 465 ASN E 52
REMARK 465 LYS E 53
REMARK 465 THR E 54
REMARK 465 GLU E 55
REMARK 465 LYS E 56
REMARK 465 GLU E 57
REMARK 465 LYS E 58
REMARK 465 PHE E 59
REMARK 465 LYS E 60
REMARK 465 ASP E 61
REMARK 465 SER E 62
REMARK 465 ILE E 63
REMARK 465 GLU E 799
REMARK 465 LYS E 800
REMARK 465 MET F 24
REMARK 465 HIS F 25
REMARK 465 HIS F 26
REMARK 465 HIS F 27
REMARK 465 HIS F 28
REMARK 465 HIS F 29
REMARK 465 HIS F 30
REMARK 465 ALA F 31
REMARK 465 ALA F 32
REMARK 465 ALA F 33
REMARK 465 MET F 34
REMARK 465 ASN F 35
REMARK 465 GLU F 36
REMARK 465 HIS F 37
REMARK 465 TYR F 38
REMARK 465 THR F 39
REMARK 465 GLU F 40
REMARK 465 SER F 41
REMARK 465 ASP F 42
REMARK 465 ILE F 43
REMARK 465 LYS F 44
REMARK 465 ARG F 45
REMARK 465 ASN F 46
REMARK 465 HIS F 47
REMARK 465 LYS F 48
REMARK 465 THR F 49
REMARK 465 GLU F 50
REMARK 465 LYS F 51
REMARK 465 ASN F 52
REMARK 465 LYS F 53
REMARK 465 THR F 54
REMARK 465 GLU F 55
REMARK 465 LYS F 56
REMARK 465 GLU F 57
REMARK 465 LYS F 58
REMARK 465 PHE F 59
REMARK 465 LYS F 60
REMARK 465 ASP F 61
REMARK 465 SER F 62
REMARK 465 ILE F 63
REMARK 465 GLU F 799
REMARK 465 LYS F 800
REMARK 465 MET O 0
REMARK 465 ALA O 1
REMARK 465 ASP O 2
REMARK 465 MET P 0
REMARK 465 ALA P 1
REMARK 465 ASP P 2
REMARK 465 MET Q 0
REMARK 465 ALA Q 1
REMARK 465 ASP Q 2
REMARK 465 MET R 0
REMARK 465 ALA R 1
REMARK 465 ASP R 2
REMARK 465 MET S 0
REMARK 465 ALA S 1
REMARK 465 ASP S 2
REMARK 465 MET T 0
REMARK 465 ALA T 1
REMARK 465 ASP T 2
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 676 CG1 CG2
REMARK 470 ASP A 684 CG OD1 OD2
REMARK 470 VAL B 676 CG1 CG2
REMARK 470 ASP B 684 CG OD1 OD2
REMARK 470 VAL C 676 CG1 CG2
REMARK 470 ASP C 684 CG OD1 OD2
REMARK 470 VAL D 676 CG1 CG2
REMARK 470 ASP D 684 CG OD1 OD2
REMARK 470 VAL E 676 CG1 CG2
REMARK 470 ASP E 684 CG OD1 OD2
REMARK 470 VAL F 676 CG1 CG2
REMARK 470 ASP F 684 CG OD1 OD2
REMARK 470 GLN O 3 CG CD OE1 NE2
REMARK 470 LEU O 4 CG CD1 CD2
REMARK 470 GLN P 3 CG CD OE1 NE2
REMARK 470 LEU P 4 CG CD1 CD2
REMARK 470 GLN Q 3 CG CD OE1 NE2
REMARK 470 LEU Q 4 CG CD1 CD2
REMARK 470 GLN R 3 CG CD OE1 NE2
REMARK 470 LEU R 4 CG CD1 CD2
REMARK 470 GLN S 3 CG CD OE1 NE2
REMARK 470 LEU S 4 CG CD1 CD2
REMARK 470 GLN T 3 CG CD OE1 NE2
REMARK 470 LEU T 4 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU F 179 CB SER F 183 1.58
REMARK 500 O LEU B 179 CB SER B 183 1.66
REMARK 500 O LEU A 179 CB SER A 183 1.67
REMARK 500 O LEU E 179 CB SER E 183 1.69
REMARK 500 O LEU D 179 CB SER D 183 1.71
REMARK 500 O LEU C 179 CB SER C 183 1.73
REMARK 500 O LEU F 179 N SER F 183 1.91
REMARK 500 O GLU F 191 N LEU F 193 1.92
REMARK 500 O LEU E 179 N SER E 183 1.92
REMARK 500 O LEU B 179 N SER B 183 1.94
REMARK 500 O LEU A 179 N SER A 183 1.99
REMARK 500 O LEU C 179 N SER C 183 2.03
REMARK 500 O LEU D 179 N SER D 183 2.04
REMARK 500 O LEU B 179 CA SER B 183 2.04
REMARK 500 O LEU E 179 CA SER E 183 2.05
REMARK 500 O LEU F 179 CA SER F 183 2.05
REMARK 500 C LYS F 186 O LEU F 188 2.07
REMARK 500 C LYS A 186 O LEU A 188 2.07
REMARK 500 C LYS E 186 O LEU E 188 2.07
REMARK 500 O LEU A 179 CA SER A 183 2.08
REMARK 500 C LYS C 186 O LEU C 188 2.09
REMARK 500 C LYS B 186 O LEU B 188 2.09
REMARK 500 C LYS D 186 O LEU D 188 2.10
REMARK 500 O LYS F 186 O LEU F 188 2.11
REMARK 500 O LYS A 186 O LEU A 188 2.11
REMARK 500 O LYS E 186 O LEU E 188 2.11
REMARK 500 O LYS C 186 O LEU C 188 2.13
REMARK 500 O LYS B 186 O LEU B 188 2.13
REMARK 500 O LEU D 179 CA SER D 183 2.13
REMARK 500 O LYS D 186 O LEU D 188 2.14
REMARK 500 O LEU C 179 CA SER C 183 2.14
REMARK 500 NH2 ARG A 540 OE1 GLU O 87 2.16
REMARK 500 NH2 ARG F 540 OE1 GLU T 87 2.16
REMARK 500 O GLU C 191 N LEU C 193 2.17
REMARK 500 NH2 ARG B 540 OE1 GLU P 87 2.18
REMARK 500 NH2 ARG E 540 OE1 GLU S 87 2.18
REMARK 500 NH2 ARG D 540 OE1 GLU R 87 2.19
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 GLU C 123 C GLU C 124 N -0.145
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 147 N - CA - C ANGL. DEV. = 20.4 DEGREES
REMARK 500 TYR A 159 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA A 160 C - N - CA ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA A 160 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU A 188 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 ARG B 147 N - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500 TYR B 159 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA B 160 C - N - CA ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA B 160 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU B 188 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 ASP B 623 C - N - CA ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG C 147 N - CA - C ANGL. DEV. = 20.4 DEGREES
REMARK 500 TYR C 159 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA C 160 C - N - CA ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA C 160 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU C 188 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 ARG D 147 N - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500 TYR D 159 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA D 160 C - N - CA ANGL. DEV. = -15.4 DEGREES
REMARK 500 ALA D 160 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU D 188 N - CA - C ANGL. DEV. = -21.1 DEGREES
REMARK 500 LYS D 622 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASP D 623 C - N - CA ANGL. DEV. = -18.9 DEGREES
REMARK 500 MET E 128 N - CA - C ANGL. DEV. = -17.4 DEGREES
REMARK 500 ARG E 147 N - CA - C ANGL. DEV. = 20.4 DEGREES
REMARK 500 TYR E 159 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA E 160 C - N - CA ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA E 160 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 LEU E 188 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 ARG F 147 N - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500 TYR F 159 CA - C - N ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA F 160 C - N - CA ANGL. DEV. = -15.5 DEGREES
REMARK 500 ALA F 160 N - CA - C ANGL. DEV. = 19.8 DEGREES
REMARK 500 LEU F 188 N - CA - C ANGL. DEV. = -21.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 70 -73.14 -62.12
REMARK 500 THR A 75 -151.51 -95.01
REMARK 500 GLN A 80 9.67 -58.18
REMARK 500 ASP A 84 -10.47 -47.68
REMARK 500 LYS A 91 -53.14 -24.24
REMARK 500 LEU A 100 24.04 -70.97
REMARK 500 ASP A 108 -87.94 -89.49
REMARK 500 LEU A 111 -68.92 -95.29
REMARK 500 VAL A 112 -178.36 -58.27
REMARK 500 GLU A 113 63.76 -60.45
REMARK 500 GLU A 116 15.55 -59.79
REMARK 500 LEU A 117 14.34 -154.26
REMARK 500 ASP A 119 -156.48 -86.56
REMARK 500 SER A 121 -87.09 -112.60
REMARK 500 GLU A 123 -146.28 -90.74
REMARK 500 LYS A 125 -78.15 -96.38
REMARK 500 ASN A 129 -70.86 -113.44
REMARK 500 LYS A 134 -40.69 -130.74
REMARK 500 PRO A 136 31.16 -99.80
REMARK 500 PHE A 137 -75.53 0.52
REMARK 500 ALA A 138 -71.26 -18.13
REMARK 500 GLU A 148 -82.40 -117.55
REMARK 500 LYS A 157 -97.24 -113.50
REMARK 500 GLN A 165 -3.53 -48.45
REMARK 500 SER A 166 2.96 -60.32
REMARK 500 GLU A 172 -60.28 -97.26
REMARK 500 ASP A 180 -84.22 -66.05
REMARK 500 ILE A 181 -4.33 -46.38
REMARK 500 SER A 183 -104.45 -60.19
REMARK 500 LYS A 186 -11.87 -140.52
REMARK 500 SER A 187 -81.48 -50.16
REMARK 500 LEU A 188 171.86 -57.85
REMARK 500 PHE A 192 -43.26 -22.96
REMARK 500 SER A 200 33.70 -74.32
REMARK 500 ASP A 202 18.86 -149.87
REMARK 500 ASP A 204 -76.46 -76.90
REMARK 500 SER A 206 41.50 -73.70
REMARK 500 LEU A 208 41.70 -77.79
REMARK 500 PHE A 210 23.03 -143.27
REMARK 500 LYS A 213 -17.89 -159.50
REMARK 500 LYS A 215 -96.13 -120.58
REMARK 500 LEU A 218 42.74 -149.57
REMARK 500 ASN A 222 70.05 -106.01
REMARK 500 LYS A 223 136.66 -174.46
REMARK 500 ASP A 226 -132.13 -105.20
REMARK 500 GLU A 232 -49.87 -26.77
REMARK 500 ALA A 240 -72.92 -91.67
REMARK 500 ASP A 252 -70.48 -108.35
REMARK 500 LYS A 278 -74.30 -54.58
REMARK 500 LYS A 290 -87.68 -70.37
REMARK 500
REMARK 500 THIS ENTRY HAS 847 RAMACHANDRAN OUTLIERS.
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 900 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 491 OD2
REMARK 620 2 ASP A 491 OD1 52.5
REMARK 620 3 ASP A 493 OD2 67.2 67.4
REMARK 620 4 HIS A 577 NE2 123.7 81.6 65.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 901 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 491 OD2
REMARK 620 2 ASP B 491 OD1 50.4
REMARK 620 3 ASP B 493 OD2 64.0 64.1
REMARK 620 4 HIS B 577 NE2 120.3 80.5 65.0
REMARK 620 5 CMP B 902 O1P 111.3 161.3 114.3 116.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 491 OD1
REMARK 620 2 ASP C 491 OD2 53.5
REMARK 620 3 ASP C 493 OD2 66.1 67.5
REMARK 620 4 HIS C 577 NE2 79.4 123.0 64.8
REMARK 620 5 CMP C 903 O1P 169.4 116.6 115.7 111.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 903 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 491 OD2
REMARK 620 2 ASP D 491 OD1 50.6
REMARK 620 3 ASP D 493 OD2 63.3 62.3
REMARK 620 4 HIS D 577 NE2 118.5 78.8 63.2
REMARK 620 5 CMP D 904 O1P 113.6 164.2 113.4 113.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 904 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 491 OD1
REMARK 620 2 ASP E 491 OD2 52.4
REMARK 620 3 ASP E 493 OD2 65.7 66.5
REMARK 620 4 HIS E 577 NE2 79.0 121.4 64.6
REMARK 620 5 CMP E 905 O1P 167.5 116.1 116.6 113.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 905 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 491 OD1
REMARK 620 2 ASP F 491 OD2 53.1
REMARK 620 3 ASP F 493 OD2 65.8 67.5
REMARK 620 4 HIS F 577 NE2 77.3 121.2 64.2
REMARK 620 5 CMP F 906 O1P 169.4 117.3 116.7 113.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP O 20 OD2
REMARK 620 2 ASP O 22 OD2 122.9
REMARK 620 3 ASP O 22 OD1 89.2 52.8
REMARK 620 4 ASP O 24 OD1 84.9 87.2 126.2
REMARK 620 5 ASP O 24 OD2 124.6 51.3 103.6 44.1
REMARK 620 6 THR O 26 O 92.7 142.7 148.4 85.4 101.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP O 93 OD1
REMARK 620 2 ASP O 95 OD1 75.1
REMARK 620 3 ASP O 95 OD2 95.2 44.8
REMARK 620 4 ASN O 97 ND2 50.6 93.4 75.9
REMARK 620 5 ASN O 97 OD1 107.5 102.0 57.6 57.6
REMARK 620 6 TYR O 99 O 64.6 136.9 149.1 73.2 104.3
REMARK 620 7 GLU O 104 OE1 101.7 86.7 121.5 150.7 150.8 86.8
REMARK 620 8 GLU O 104 OE2 86.4 48.4 88.6 131.3 143.8 111.8 38.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP O 129 OD2
REMARK 620 2 ASP O 131 OD1 69.7
REMARK 620 3 ASP O 133 OD1 111.5 79.0
REMARK 620 4 GLN O 135 O 94.2 162.6 114.3
REMARK 620 5 GLU O 140 OE1 91.2 81.6 142.3 92.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA P 703 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP P 20 OD2
REMARK 620 2 ASP P 22 OD2 116.0
REMARK 620 3 ASP P 22 OD1 82.3 52.6
REMARK 620 4 ASP P 24 OD1 79.2 87.4 120.6
REMARK 620 5 ASP P 24 OD2 120.3 52.9 104.3 45.9
REMARK 620 6 THR P 26 O 88.3 153.6 147.7 87.4 107.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA P 804 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP P 93 OD1
REMARK 620 2 ASP P 95 OD1 78.6
REMARK 620 3 ASP P 95 OD2 97.6 44.6
REMARK 620 4 ASN P 97 OD1 109.7 101.9 57.5
REMARK 620 5 ASN P 97 ND2 52.7 96.3 76.6 57.5
REMARK 620 6 TYR P 99 O 67.3 143.0 151.0 102.8 74.6
REMARK 620 7 GLU P 104 OE1 105.7 88.6 121.4 144.4 155.8 87.2
REMARK 620 8 GLU P 104 OE2 89.1 49.4 89.3 142.9 135.8 114.1 39.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA P 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP P 129 OD2
REMARK 620 2 ASP P 131 OD1 68.3
REMARK 620 3 ASP P 133 OD1 110.7 77.6
REMARK 620 4 GLN P 135 O 95.2 161.8 117.0
REMARK 620 5 GLU P 140 OE1 90.3 80.1 140.5 92.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA Q 705 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Q 20 OD2
REMARK 620 2 ASP Q 22 OD1 85.1
REMARK 620 3 ASP Q 22 OD2 118.6 52.5
REMARK 620 4 ASP Q 24 OD1 81.6 123.0 87.4
REMARK 620 5 ASP Q 24 OD2 122.1 103.6 52.0 45.3
REMARK 620 6 THR Q 26 O 90.8 148.5 148.8 87.0 105.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA Q 806 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Q 93 OD1
REMARK 620 2 ASP Q 95 OD1 85.1
REMARK 620 3 ASP Q 95 OD2 100.5 42.4
REMARK 620 4 ASN Q 97 ND2 57.7 99.6 75.2
REMARK 620 5 ASN Q 97 OD1 112.7 96.4 54.0 55.7
REMARK 620 6 TYR Q 99 O 73.5 156.3 150.9 77.8 101.2
REMARK 620 7 GLU Q 104 OE2 95.1 50.8 88.6 143.8 135.7 120.0
REMARK 620 8 GLU Q 104 OE1 116.6 89.2 116.0 168.7 130.7 91.3 41.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA Q 805 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Q 129 OD2
REMARK 620 2 ASP Q 131 OD1 67.9
REMARK 620 3 ASP Q 133 OD1 108.3 77.5
REMARK 620 4 GLN Q 135 O 92.1 159.3 115.3
REMARK 620 5 GLU Q 140 OE1 90.2 81.1 143.5 94.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA R 707 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 20 OD2
REMARK 620 2 ASP R 22 OD2 119.9
REMARK 620 3 ASP R 22 OD1 84.1 54.2
REMARK 620 4 ASP R 24 OD2 122.7 54.3 107.5
REMARK 620 5 ASP R 24 OD1 80.1 90.7 125.4 46.9
REMARK 620 6 THR R 26 O 86.3 152.6 144.8 106.2 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA R 808 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 93 OD1
REMARK 620 2 ASP R 95 OD1 77.9
REMARK 620 3 ASP R 95 OD2 97.6 45.7
REMARK 620 4 ASN R 97 OD1 108.5 103.6 58.2
REMARK 620 5 ASN R 97 ND2 51.6 96.5 77.2 57.5
REMARK 620 6 TYR R 99 O 65.1 140.2 149.4 101.8 72.3
REMARK 620 7 GLU R 104 OE1 104.4 89.5 123.8 146.4 152.6 86.0
REMARK 620 8 GLU R 104 OE2 89.1 49.7 90.5 145.1 135.5 113.0 40.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA R 807 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 129 OD2
REMARK 620 2 ASP R 131 OD1 70.8
REMARK 620 3 ASP R 133 OD1 111.9 80.4
REMARK 620 4 GLN R 135 O 93.7 163.2 112.2
REMARK 620 5 GLU R 140 OE1 92.5 83.2 143.7 91.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA S 709 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP S 20 OD2
REMARK 620 2 ASP S 22 OD2 118.0
REMARK 620 3 ASP S 22 OD1 84.1 51.0
REMARK 620 4 ASP S 24 OD2 124.8 51.7 102.0
REMARK 620 5 ASP S 24 OD1 84.9 87.4 122.9 45.6
REMARK 620 6 THR S 26 O 93.5 148.1 145.3 107.4 91.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA S 810 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP S 93 OD1
REMARK 620 2 ASP S 95 OD2 91.6
REMARK 620 3 ASP S 95 OD1 71.0 43.6
REMARK 620 4 ASN S 97 OD1 105.2 56.3 99.1
REMARK 620 5 ASN S 97 ND2 48.8 73.3 88.3 57.3
REMARK 620 6 TYR S 99 O 62.8 146.0 131.3 106.8 73.0
REMARK 620 7 GLU S 104 OE1 97.5 119.7 84.1 156.9 145.8 87.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA S 809 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP S 129 OD2
REMARK 620 2 ASP S 131 OD1 69.1
REMARK 620 3 ASP S 133 OD1 109.8 78.7
REMARK 620 4 GLN S 135 O 92.4 160.6 114.3
REMARK 620 5 GLU S 140 OE1 91.3 82.4 144.0 92.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 711 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP T 20 OD2
REMARK 620 2 ASP T 22 OD2 121.1
REMARK 620 3 ASP T 22 OD1 86.0 52.4
REMARK 620 4 ASP T 24 OD1 84.7 89.1 125.8
REMARK 620 5 ASP T 24 OD2 126.0 52.4 104.1 46.1
REMARK 620 6 THR T 26 O 91.7 146.8 144.8 88.8 105.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 812 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP T 93 OD1
REMARK 620 2 ASP T 95 OD2 95.9
REMARK 620 3 ASP T 95 OD1 74.8 45.3
REMARK 620 4 ASN T 97 ND2 49.9 77.1 93.5
REMARK 620 5 ASN T 97 OD1 107.4 59.0 103.6 58.0
REMARK 620 6 TYR T 99 O 63.4 148.9 135.3 71.9 103.3
REMARK 620 7 GLU T 104 OE2 85.7 89.8 49.2 130.9 146.6 110.0
REMARK 620 8 GLU T 104 OE1 99.7 123.5 87.8 147.5 152.5 84.5 38.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA T 811 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP T 129 OD2
REMARK 620 2 ASP T 131 OD1 69.4
REMARK 620 3 ASP T 133 OD1 110.8 78.3
REMARK 620 4 GLN T 135 O 94.3 162.6 114.4
REMARK 620 5 GLU T 140 OE1 91.7 81.7 141.9 93.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA P 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA P 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA P 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Q 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Q 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA Q 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA R 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA R 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA R 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA S 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA S 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA S 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA T 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP D 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP E 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMP F 906
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XFU RELATED DB: PDB
REMARK 900 RELATED ID: 1XFV RELATED DB: PDB
REMARK 900 RELATED ID: 1XFX RELATED DB: PDB
REMARK 900 RELATED ID: 1XFY RELATED DB: PDB
REMARK 900 RELATED ID: 1XFZ RELATED DB: PDB
DBREF 1XFW A 33 800 UNP P40136 CYAA_BACAN 33 800
DBREF 1XFW B 33 800 UNP P40136 CYAA_BACAN 33 800
DBREF 1XFW C 33 800 UNP P40136 CYAA_BACAN 33 800
DBREF 1XFW D 33 800 UNP P40136 CYAA_BACAN 33 800
DBREF 1XFW E 33 800 UNP P40136 CYAA_BACAN 33 800
DBREF 1XFW F 33 800 UNP P40136 CYAA_BACAN 33 800
DBREF 1XFW O 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 1XFW P 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 1XFW Q 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 1XFW R 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 1XFW S 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 1XFW T 0 148 UNP P62158 CALM_HUMAN 1 149
SEQADV 1XFW MET A 24 UNP P40136 INITIATING METHIONINE
SEQADV 1XFW HIS A 25 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS A 26 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS A 27 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS A 28 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS A 29 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS A 30 UNP P40136 EXPRESSION TAG
SEQADV 1XFW ALA A 31 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW ALA A 32 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW MET B 24 UNP P40136 INITIATING METHIONINE
SEQADV 1XFW HIS B 25 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS B 26 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS B 27 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS B 28 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS B 29 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS B 30 UNP P40136 EXPRESSION TAG
SEQADV 1XFW ALA B 31 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW ALA B 32 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW MET C 24 UNP P40136 INITIATING METHIONINE
SEQADV 1XFW HIS C 25 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS C 26 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS C 27 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS C 28 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS C 29 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS C 30 UNP P40136 EXPRESSION TAG
SEQADV 1XFW ALA C 31 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW ALA C 32 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW MET D 24 UNP P40136 INITIATING METHIONINE
SEQADV 1XFW HIS D 25 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS D 26 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS D 27 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS D 28 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS D 29 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS D 30 UNP P40136 EXPRESSION TAG
SEQADV 1XFW ALA D 31 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW ALA D 32 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW MET E 24 UNP P40136 INITIATING METHIONINE
SEQADV 1XFW HIS E 25 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS E 26 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS E 27 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS E 28 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS E 29 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS E 30 UNP P40136 EXPRESSION TAG
SEQADV 1XFW ALA E 31 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW ALA E 32 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW MET F 24 UNP P40136 INITIATING METHIONINE
SEQADV 1XFW HIS F 25 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS F 26 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS F 27 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS F 28 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS F 29 UNP P40136 EXPRESSION TAG
SEQADV 1XFW HIS F 30 UNP P40136 EXPRESSION TAG
SEQADV 1XFW ALA F 31 UNP P40136 CLONING ARTIFACT
SEQADV 1XFW ALA F 32 UNP P40136 CLONING ARTIFACT
SEQRES 1 A 777 MET HIS HIS HIS HIS HIS HIS ALA ALA ALA MET ASN GLU
SEQRES 2 A 777 HIS TYR THR GLU SER ASP ILE LYS ARG ASN HIS LYS THR
SEQRES 3 A 777 GLU LYS ASN LYS THR GLU LYS GLU LYS PHE LYS ASP SER
SEQRES 4 A 777 ILE ASN ASN LEU VAL LYS THR GLU PHE THR ASN GLU THR
SEQRES 5 A 777 LEU ASP LYS ILE GLN GLN THR GLN ASP LEU LEU LYS LYS
SEQRES 6 A 777 ILE PRO LYS ASP VAL LEU GLU ILE TYR SER GLU LEU GLY
SEQRES 7 A 777 GLY GLU ILE TYR PHE THR ASP ILE ASP LEU VAL GLU HIS
SEQRES 8 A 777 LYS GLU LEU GLN ASP LEU SER GLU GLU GLU LYS ASN SER
SEQRES 9 A 777 MET ASN SER ARG GLY GLU LYS VAL PRO PHE ALA SER ARG
SEQRES 10 A 777 PHE VAL PHE GLU LYS LYS ARG GLU THR PRO LYS LEU ILE
SEQRES 11 A 777 ILE ASN ILE LYS ASP TYR ALA ILE ASN SER GLU GLN SER
SEQRES 12 A 777 LYS GLU VAL TYR TYR GLU ILE GLY LYS GLY ILE SER LEU
SEQRES 13 A 777 ASP ILE ILE SER LYS ASP LYS SER LEU ASP PRO GLU PHE
SEQRES 14 A 777 LEU ASN LEU ILE LYS SER LEU SER ASP ASP SER ASP SER
SEQRES 15 A 777 SER ASP LEU LEU PHE SER GLN LYS PHE LYS GLU LYS LEU
SEQRES 16 A 777 GLU LEU ASN ASN LYS SER ILE ASP ILE ASN PHE ILE LYS
SEQRES 17 A 777 GLU ASN LEU THR GLU PHE GLN HIS ALA PHE SER LEU ALA
SEQRES 18 A 777 PHE SER TYR TYR PHE ALA PRO ASP HIS ARG THR VAL LEU
SEQRES 19 A 777 GLU LEU TYR ALA PRO ASP MET PHE GLU TYR MET ASN LYS
SEQRES 20 A 777 LEU GLU LYS GLY GLY PHE GLU LYS ILE SER GLU SER LEU
SEQRES 21 A 777 LYS LYS GLU GLY VAL GLU LYS ASP ARG ILE ASP VAL LEU
SEQRES 22 A 777 LYS GLY GLU LYS ALA LEU LYS ALA SER GLY LEU VAL PRO
SEQRES 23 A 777 GLU HIS ALA ASP ALA PHE LYS LYS ILE ALA ARG GLU LEU
SEQRES 24 A 777 ASN THR TYR ILE LEU PHE ARG PRO VAL ASN LYS LEU ALA
SEQRES 25 A 777 THR ASN LEU ILE LYS SER GLY VAL ALA THR LYS GLY LEU
SEQRES 26 A 777 ASN VAL HIS GLY LYS SER SER ASP TRP GLY PRO VAL ALA
SEQRES 27 A 777 GLY TYR ILE PRO PHE ASP GLN ASP LEU SER LYS LYS HIS
SEQRES 28 A 777 GLY GLN GLN LEU ALA VAL GLU LYS GLY ASN LEU GLU ASN
SEQRES 29 A 777 LYS LYS SER ILE THR GLU HIS GLU GLY GLU ILE GLY LYS
SEQRES 30 A 777 ILE PRO LEU LYS LEU ASP HIS LEU ARG ILE GLU GLU LEU
SEQRES 31 A 777 LYS GLU ASN GLY ILE ILE LEU LYS GLY LYS LYS GLU ILE
SEQRES 32 A 777 ASP ASN GLY LYS LYS TYR TYR LEU LEU GLU SER ASN ASN
SEQRES 33 A 777 GLN VAL TYR GLU PHE ARG ILE SER ASP GLU ASN ASN GLU
SEQRES 34 A 777 VAL GLN TYR LYS THR LYS GLU GLY LYS ILE THR VAL LEU
SEQRES 35 A 777 GLY GLU LYS PHE ASN TRP ARG ASN ILE GLU VAL MET ALA
SEQRES 36 A 777 LYS ASN VAL GLU GLY VAL LEU LYS PRO LEU THR ALA ASP
SEQRES 37 A 777 TYR ASP LEU PHE ALA LEU ALA PRO SER LEU THR GLU ILE
SEQRES 38 A 777 LYS LYS GLN ILE PRO GLN LYS GLU TRP ASP LYS VAL VAL
SEQRES 39 A 777 ASN THR PRO ASN SER LEU GLU LYS GLN LYS GLY VAL THR
SEQRES 40 A 777 ASN LEU LEU ILE LYS TYR GLY ILE GLU ARG LYS PRO ASP
SEQRES 41 A 777 SER THR LYS GLY THR LEU SER ASN TRP GLN LYS GLN MET
SEQRES 42 A 777 LEU ASP ARG LEU ASN GLU ALA VAL LYS TYR THR GLY TYR
SEQRES 43 A 777 THR GLY GLY ASP VAL VAL ASN HIS GLY THR GLU GLN ASP
SEQRES 44 A 777 ASN GLU GLU PHE PRO GLU LYS ASP ASN GLU ILE PHE ILE
SEQRES 45 A 777 ILE ASN PRO GLU GLY GLU PHE ILE LEU THR LYS ASN TRP
SEQRES 46 A 777 GLU MET THR GLY ARG PHE ILE GLU LYS ASN ILE THR GLY
SEQRES 47 A 777 LYS ASP TYR LEU TYR TYR PHE ASN ARG SER TYR ASN LYS
SEQRES 48 A 777 ILE ALA PRO GLY ASN LYS ALA TYR ILE GLU TRP THR ASP
SEQRES 49 A 777 PRO ILE THR LYS ALA LYS ILE ASN THR ILE PRO THR SER
SEQRES 50 A 777 ALA GLU PHE ILE LYS ASN LEU SER SER ILE ARG ARG SER
SEQRES 51 A 777 SER ASN VAL GLY VAL TYR LYS ASP SER GLY ASP LYS ASP
SEQRES 52 A 777 GLU PHE ALA LYS LYS GLU SER VAL LYS LYS ILE ALA GLY
SEQRES 53 A 777 TYR LEU SER ASP TYR TYR ASN SER ALA ASN HIS ILE PHE
SEQRES 54 A 777 SER GLN GLU LYS LYS ARG LYS ILE SER ILE PHE ARG GLY
SEQRES 55 A 777 ILE GLN ALA TYR ASN GLU ILE GLU ASN VAL LEU LYS SER
SEQRES 56 A 777 LYS GLN ILE ALA PRO GLU TYR LYS ASN TYR PHE GLN TYR
SEQRES 57 A 777 LEU LYS GLU ARG ILE THR ASN GLN VAL GLN LEU LEU LEU
SEQRES 58 A 777 THR HIS GLN LYS SER ASN ILE GLU PHE LYS LEU LEU TYR
SEQRES 59 A 777 LYS GLN LEU ASN PHE THR GLU ASN GLU THR ASP ASN PHE
SEQRES 60 A 777 GLU VAL PHE GLN LYS ILE ILE ASP GLU LYS
SEQRES 1 B 777 MET HIS HIS HIS HIS HIS HIS ALA ALA ALA MET ASN GLU
SEQRES 2 B 777 HIS TYR THR GLU SER ASP ILE LYS ARG ASN HIS LYS THR
SEQRES 3 B 777 GLU LYS ASN LYS THR GLU LYS GLU LYS PHE LYS ASP SER
SEQRES 4 B 777 ILE ASN ASN LEU VAL LYS THR GLU PHE THR ASN GLU THR
SEQRES 5 B 777 LEU ASP LYS ILE GLN GLN THR GLN ASP LEU LEU LYS LYS
SEQRES 6 B 777 ILE PRO LYS ASP VAL LEU GLU ILE TYR SER GLU LEU GLY
SEQRES 7 B 777 GLY GLU ILE TYR PHE THR ASP ILE ASP LEU VAL GLU HIS
SEQRES 8 B 777 LYS GLU LEU GLN ASP LEU SER GLU GLU GLU LYS ASN SER
SEQRES 9 B 777 MET ASN SER ARG GLY GLU LYS VAL PRO PHE ALA SER ARG
SEQRES 10 B 777 PHE VAL PHE GLU LYS LYS ARG GLU THR PRO LYS LEU ILE
SEQRES 11 B 777 ILE ASN ILE LYS ASP TYR ALA ILE ASN SER GLU GLN SER
SEQRES 12 B 777 LYS GLU VAL TYR TYR GLU ILE GLY LYS GLY ILE SER LEU
SEQRES 13 B 777 ASP ILE ILE SER LYS ASP LYS SER LEU ASP PRO GLU PHE
SEQRES 14 B 777 LEU ASN LEU ILE LYS SER LEU SER ASP ASP SER ASP SER
SEQRES 15 B 777 SER ASP LEU LEU PHE SER GLN LYS PHE LYS GLU LYS LEU
SEQRES 16 B 777 GLU LEU ASN ASN LYS SER ILE ASP ILE ASN PHE ILE LYS
SEQRES 17 B 777 GLU ASN LEU THR GLU PHE GLN HIS ALA PHE SER LEU ALA
SEQRES 18 B 777 PHE SER TYR TYR PHE ALA PRO ASP HIS ARG THR VAL LEU
SEQRES 19 B 777 GLU LEU TYR ALA PRO ASP MET PHE GLU TYR MET ASN LYS
SEQRES 20 B 777 LEU GLU LYS GLY GLY PHE GLU LYS ILE SER GLU SER LEU
SEQRES 21 B 777 LYS LYS GLU GLY VAL GLU LYS ASP ARG ILE ASP VAL LEU
SEQRES 22 B 777 LYS GLY GLU LYS ALA LEU LYS ALA SER GLY LEU VAL PRO
SEQRES 23 B 777 GLU HIS ALA ASP ALA PHE LYS LYS ILE ALA ARG GLU LEU
SEQRES 24 B 777 ASN THR TYR ILE LEU PHE ARG PRO VAL ASN LYS LEU ALA
SEQRES 25 B 777 THR ASN LEU ILE LYS SER GLY VAL ALA THR LYS GLY LEU
SEQRES 26 B 777 ASN VAL HIS GLY LYS SER SER ASP TRP GLY PRO VAL ALA
SEQRES 27 B 777 GLY TYR ILE PRO PHE ASP GLN ASP LEU SER LYS LYS HIS
SEQRES 28 B 777 GLY GLN GLN LEU ALA VAL GLU LYS GLY ASN LEU GLU ASN
SEQRES 29 B 777 LYS LYS SER ILE THR GLU HIS GLU GLY GLU ILE GLY LYS
SEQRES 30 B 777 ILE PRO LEU LYS LEU ASP HIS LEU ARG ILE GLU GLU LEU
SEQRES 31 B 777 LYS GLU ASN GLY ILE ILE LEU LYS GLY LYS LYS GLU ILE
SEQRES 32 B 777 ASP ASN GLY LYS LYS TYR TYR LEU LEU GLU SER ASN ASN
SEQRES 33 B 777 GLN VAL TYR GLU PHE ARG ILE SER ASP GLU ASN ASN GLU
SEQRES 34 B 777 VAL GLN TYR LYS THR LYS GLU GLY LYS ILE THR VAL LEU
SEQRES 35 B 777 GLY GLU LYS PHE ASN TRP ARG ASN ILE GLU VAL MET ALA
SEQRES 36 B 777 LYS ASN VAL GLU GLY VAL LEU LYS PRO LEU THR ALA ASP
SEQRES 37 B 777 TYR ASP LEU PHE ALA LEU ALA PRO SER LEU THR GLU ILE
SEQRES 38 B 777 LYS LYS GLN ILE PRO GLN LYS GLU TRP ASP LYS VAL VAL
SEQRES 39 B 777 ASN THR PRO ASN SER LEU GLU LYS GLN LYS GLY VAL THR
SEQRES 40 B 777 ASN LEU LEU ILE LYS TYR GLY ILE GLU ARG LYS PRO ASP
SEQRES 41 B 777 SER THR LYS GLY THR LEU SER ASN TRP GLN LYS GLN MET
SEQRES 42 B 777 LEU ASP ARG LEU ASN GLU ALA VAL LYS TYR THR GLY TYR
SEQRES 43 B 777 THR GLY GLY ASP VAL VAL ASN HIS GLY THR GLU GLN ASP
SEQRES 44 B 777 ASN GLU GLU PHE PRO GLU LYS ASP ASN GLU ILE PHE ILE
SEQRES 45 B 777 ILE ASN PRO GLU GLY GLU PHE ILE LEU THR LYS ASN TRP
SEQRES 46 B 777 GLU MET THR GLY ARG PHE ILE GLU LYS ASN ILE THR GLY
SEQRES 47 B 777 LYS ASP TYR LEU TYR TYR PHE ASN ARG SER TYR ASN LYS
SEQRES 48 B 777 ILE ALA PRO GLY ASN LYS ALA TYR ILE GLU TRP THR ASP
SEQRES 49 B 777 PRO ILE THR LYS ALA LYS ILE ASN THR ILE PRO THR SER
SEQRES 50 B 777 ALA GLU PHE ILE LYS ASN LEU SER SER ILE ARG ARG SER
SEQRES 51 B 777 SER ASN VAL GLY VAL TYR LYS ASP SER GLY ASP LYS ASP
SEQRES 52 B 777 GLU PHE ALA LYS LYS GLU SER VAL LYS LYS ILE ALA GLY
SEQRES 53 B 777 TYR LEU SER ASP TYR TYR ASN SER ALA ASN HIS ILE PHE
SEQRES 54 B 777 SER GLN GLU LYS LYS ARG LYS ILE SER ILE PHE ARG GLY
SEQRES 55 B 777 ILE GLN ALA TYR ASN GLU ILE GLU ASN VAL LEU LYS SER
SEQRES 56 B 777 LYS GLN ILE ALA PRO GLU TYR LYS ASN TYR PHE GLN TYR
SEQRES 57 B 777 LEU LYS GLU ARG ILE THR ASN GLN VAL GLN LEU LEU LEU
SEQRES 58 B 777 THR HIS GLN LYS SER ASN ILE GLU PHE LYS LEU LEU TYR
SEQRES 59 B 777 LYS GLN LEU ASN PHE THR GLU ASN GLU THR ASP ASN PHE
SEQRES 60 B 777 GLU VAL PHE GLN LYS ILE ILE ASP GLU LYS
SEQRES 1 C 777 MET HIS HIS HIS HIS HIS HIS ALA ALA ALA MET ASN GLU
SEQRES 2 C 777 HIS TYR THR GLU SER ASP ILE LYS ARG ASN HIS LYS THR
SEQRES 3 C 777 GLU LYS ASN LYS THR GLU LYS GLU LYS PHE LYS ASP SER
SEQRES 4 C 777 ILE ASN ASN LEU VAL LYS THR GLU PHE THR ASN GLU THR
SEQRES 5 C 777 LEU ASP LYS ILE GLN GLN THR GLN ASP LEU LEU LYS LYS
SEQRES 6 C 777 ILE PRO LYS ASP VAL LEU GLU ILE TYR SER GLU LEU GLY
SEQRES 7 C 777 GLY GLU ILE TYR PHE THR ASP ILE ASP LEU VAL GLU HIS
SEQRES 8 C 777 LYS GLU LEU GLN ASP LEU SER GLU GLU GLU LYS ASN SER
SEQRES 9 C 777 MET ASN SER ARG GLY GLU LYS VAL PRO PHE ALA SER ARG
SEQRES 10 C 777 PHE VAL PHE GLU LYS LYS ARG GLU THR PRO LYS LEU ILE
SEQRES 11 C 777 ILE ASN ILE LYS ASP TYR ALA ILE ASN SER GLU GLN SER
SEQRES 12 C 777 LYS GLU VAL TYR TYR GLU ILE GLY LYS GLY ILE SER LEU
SEQRES 13 C 777 ASP ILE ILE SER LYS ASP LYS SER LEU ASP PRO GLU PHE
SEQRES 14 C 777 LEU ASN LEU ILE LYS SER LEU SER ASP ASP SER ASP SER
SEQRES 15 C 777 SER ASP LEU LEU PHE SER GLN LYS PHE LYS GLU LYS LEU
SEQRES 16 C 777 GLU LEU ASN ASN LYS SER ILE ASP ILE ASN PHE ILE LYS
SEQRES 17 C 777 GLU ASN LEU THR GLU PHE GLN HIS ALA PHE SER LEU ALA
SEQRES 18 C 777 PHE SER TYR TYR PHE ALA PRO ASP HIS ARG THR VAL LEU
SEQRES 19 C 777 GLU LEU TYR ALA PRO ASP MET PHE GLU TYR MET ASN LYS
SEQRES 20 C 777 LEU GLU LYS GLY GLY PHE GLU LYS ILE SER GLU SER LEU
SEQRES 21 C 777 LYS LYS GLU GLY VAL GLU LYS ASP ARG ILE ASP VAL LEU
SEQRES 22 C 777 LYS GLY GLU LYS ALA LEU LYS ALA SER GLY LEU VAL PRO
SEQRES 23 C 777 GLU HIS ALA ASP ALA PHE LYS LYS ILE ALA ARG GLU LEU
SEQRES 24 C 777 ASN THR TYR ILE LEU PHE ARG PRO VAL ASN LYS LEU ALA
SEQRES 25 C 777 THR ASN LEU ILE LYS SER GLY VAL ALA THR LYS GLY LEU
SEQRES 26 C 777 ASN VAL HIS GLY LYS SER SER ASP TRP GLY PRO VAL ALA
SEQRES 27 C 777 GLY TYR ILE PRO PHE ASP GLN ASP LEU SER LYS LYS HIS
SEQRES 28 C 777 GLY GLN GLN LEU ALA VAL GLU LYS GLY ASN LEU GLU ASN
SEQRES 29 C 777 LYS LYS SER ILE THR GLU HIS GLU GLY GLU ILE GLY LYS
SEQRES 30 C 777 ILE PRO LEU LYS LEU ASP HIS LEU ARG ILE GLU GLU LEU
SEQRES 31 C 777 LYS GLU ASN GLY ILE ILE LEU LYS GLY LYS LYS GLU ILE
SEQRES 32 C 777 ASP ASN GLY LYS LYS TYR TYR LEU LEU GLU SER ASN ASN
SEQRES 33 C 777 GLN VAL TYR GLU PHE ARG ILE SER ASP GLU ASN ASN GLU
SEQRES 34 C 777 VAL GLN TYR LYS THR LYS GLU GLY LYS ILE THR VAL LEU
SEQRES 35 C 777 GLY GLU LYS PHE ASN TRP ARG ASN ILE GLU VAL MET ALA
SEQRES 36 C 777 LYS ASN VAL GLU GLY VAL LEU LYS PRO LEU THR ALA ASP
SEQRES 37 C 777 TYR ASP LEU PHE ALA LEU ALA PRO SER LEU THR GLU ILE
SEQRES 38 C 777 LYS LYS GLN ILE PRO GLN LYS GLU TRP ASP LYS VAL VAL
SEQRES 39 C 777 ASN THR PRO ASN SER LEU GLU LYS GLN LYS GLY VAL THR
SEQRES 40 C 777 ASN LEU LEU ILE LYS TYR GLY ILE GLU ARG LYS PRO ASP
SEQRES 41 C 777 SER THR LYS GLY THR LEU SER ASN TRP GLN LYS GLN MET
SEQRES 42 C 777 LEU ASP ARG LEU ASN GLU ALA VAL LYS TYR THR GLY TYR
SEQRES 43 C 777 THR GLY GLY ASP VAL VAL ASN HIS GLY THR GLU GLN ASP
SEQRES 44 C 777 ASN GLU GLU PHE PRO GLU LYS ASP ASN GLU ILE PHE ILE
SEQRES 45 C 777 ILE ASN PRO GLU GLY GLU PHE ILE LEU THR LYS ASN TRP
SEQRES 46 C 777 GLU MET THR GLY ARG PHE ILE GLU LYS ASN ILE THR GLY
SEQRES 47 C 777 LYS ASP TYR LEU TYR TYR PHE ASN ARG SER TYR ASN LYS
SEQRES 48 C 777 ILE ALA PRO GLY ASN LYS ALA TYR ILE GLU TRP THR ASP
SEQRES 49 C 777 PRO ILE THR LYS ALA LYS ILE ASN THR ILE PRO THR SER
SEQRES 50 C 777 ALA GLU PHE ILE LYS ASN LEU SER SER ILE ARG ARG SER
SEQRES 51 C 777 SER ASN VAL GLY VAL TYR LYS ASP SER GLY ASP LYS ASP
SEQRES 52 C 777 GLU PHE ALA LYS LYS GLU SER VAL LYS LYS ILE ALA GLY
SEQRES 53 C 777 TYR LEU SER ASP TYR TYR ASN SER ALA ASN HIS ILE PHE
SEQRES 54 C 777 SER GLN GLU LYS LYS ARG LYS ILE SER ILE PHE ARG GLY
SEQRES 55 C 777 ILE GLN ALA TYR ASN GLU ILE GLU ASN VAL LEU LYS SER
SEQRES 56 C 777 LYS GLN ILE ALA PRO GLU TYR LYS ASN TYR PHE GLN TYR
SEQRES 57 C 777 LEU LYS GLU ARG ILE THR ASN GLN VAL GLN LEU LEU LEU
SEQRES 58 C 777 THR HIS GLN LYS SER ASN ILE GLU PHE LYS LEU LEU TYR
SEQRES 59 C 777 LYS GLN LEU ASN PHE THR GLU ASN GLU THR ASP ASN PHE
SEQRES 60 C 777 GLU VAL PHE GLN LYS ILE ILE ASP GLU LYS
SEQRES 1 D 777 MET HIS HIS HIS HIS HIS HIS ALA ALA ALA MET ASN GLU
SEQRES 2 D 777 HIS TYR THR GLU SER ASP ILE LYS ARG ASN HIS LYS THR
SEQRES 3 D 777 GLU LYS ASN LYS THR GLU LYS GLU LYS PHE LYS ASP SER
SEQRES 4 D 777 ILE ASN ASN LEU VAL LYS THR GLU PHE THR ASN GLU THR
SEQRES 5 D 777 LEU ASP LYS ILE GLN GLN THR GLN ASP LEU LEU LYS LYS
SEQRES 6 D 777 ILE PRO LYS ASP VAL LEU GLU ILE TYR SER GLU LEU GLY
SEQRES 7 D 777 GLY GLU ILE TYR PHE THR ASP ILE ASP LEU VAL GLU HIS
SEQRES 8 D 777 LYS GLU LEU GLN ASP LEU SER GLU GLU GLU LYS ASN SER
SEQRES 9 D 777 MET ASN SER ARG GLY GLU LYS VAL PRO PHE ALA SER ARG
SEQRES 10 D 777 PHE VAL PHE GLU LYS LYS ARG GLU THR PRO LYS LEU ILE
SEQRES 11 D 777 ILE ASN ILE LYS ASP TYR ALA ILE ASN SER GLU GLN SER
SEQRES 12 D 777 LYS GLU VAL TYR TYR GLU ILE GLY LYS GLY ILE SER LEU
SEQRES 13 D 777 ASP ILE ILE SER LYS ASP LYS SER LEU ASP PRO GLU PHE
SEQRES 14 D 777 LEU ASN LEU ILE LYS SER LEU SER ASP ASP SER ASP SER
SEQRES 15 D 777 SER ASP LEU LEU PHE SER GLN LYS PHE LYS GLU LYS LEU
SEQRES 16 D 777 GLU LEU ASN ASN LYS SER ILE ASP ILE ASN PHE ILE LYS
SEQRES 17 D 777 GLU ASN LEU THR GLU PHE GLN HIS ALA PHE SER LEU ALA
SEQRES 18 D 777 PHE SER TYR TYR PHE ALA PRO ASP HIS ARG THR VAL LEU
SEQRES 19 D 777 GLU LEU TYR ALA PRO ASP MET PHE GLU TYR MET ASN LYS
SEQRES 20 D 777 LEU GLU LYS GLY GLY PHE GLU LYS ILE SER GLU SER LEU
SEQRES 21 D 777 LYS LYS GLU GLY VAL GLU LYS ASP ARG ILE ASP VAL LEU
SEQRES 22 D 777 LYS GLY GLU LYS ALA LEU LYS ALA SER GLY LEU VAL PRO
SEQRES 23 D 777 GLU HIS ALA ASP ALA PHE LYS LYS ILE ALA ARG GLU LEU
SEQRES 24 D 777 ASN THR TYR ILE LEU PHE ARG PRO VAL ASN LYS LEU ALA
SEQRES 25 D 777 THR ASN LEU ILE LYS SER GLY VAL ALA THR LYS GLY LEU
SEQRES 26 D 777 ASN VAL HIS GLY LYS SER SER ASP TRP GLY PRO VAL ALA
SEQRES 27 D 777 GLY TYR ILE PRO PHE ASP GLN ASP LEU SER LYS LYS HIS
SEQRES 28 D 777 GLY GLN GLN LEU ALA VAL GLU LYS GLY ASN LEU GLU ASN
SEQRES 29 D 777 LYS LYS SER ILE THR GLU HIS GLU GLY GLU ILE GLY LYS
SEQRES 30 D 777 ILE PRO LEU LYS LEU ASP HIS LEU ARG ILE GLU GLU LEU
SEQRES 31 D 777 LYS GLU ASN GLY ILE ILE LEU LYS GLY LYS LYS GLU ILE
SEQRES 32 D 777 ASP ASN GLY LYS LYS TYR TYR LEU LEU GLU SER ASN ASN
SEQRES 33 D 777 GLN VAL TYR GLU PHE ARG ILE SER ASP GLU ASN ASN GLU
SEQRES 34 D 777 VAL GLN TYR LYS THR LYS GLU GLY LYS ILE THR VAL LEU
SEQRES 35 D 777 GLY GLU LYS PHE ASN TRP ARG ASN ILE GLU VAL MET ALA
SEQRES 36 D 777 LYS ASN VAL GLU GLY VAL LEU LYS PRO LEU THR ALA ASP
SEQRES 37 D 777 TYR ASP LEU PHE ALA LEU ALA PRO SER LEU THR GLU ILE
SEQRES 38 D 777 LYS LYS GLN ILE PRO GLN LYS GLU TRP ASP LYS VAL VAL
SEQRES 39 D 777 ASN THR PRO ASN SER LEU GLU LYS GLN LYS GLY VAL THR
SEQRES 40 D 777 ASN LEU LEU ILE LYS TYR GLY ILE GLU ARG LYS PRO ASP
SEQRES 41 D 777 SER THR LYS GLY THR LEU SER ASN TRP GLN LYS GLN MET
SEQRES 42 D 777 LEU ASP ARG LEU ASN GLU ALA VAL LYS TYR THR GLY TYR
SEQRES 43 D 777 THR GLY GLY ASP VAL VAL ASN HIS GLY THR GLU GLN ASP
SEQRES 44 D 777 ASN GLU GLU PHE PRO GLU LYS ASP ASN GLU ILE PHE ILE
SEQRES 45 D 777 ILE ASN PRO GLU GLY GLU PHE ILE LEU THR LYS ASN TRP
SEQRES 46 D 777 GLU MET THR GLY ARG PHE ILE GLU LYS ASN ILE THR GLY
SEQRES 47 D 777 LYS ASP TYR LEU TYR TYR PHE ASN ARG SER TYR ASN LYS
SEQRES 48 D 777 ILE ALA PRO GLY ASN LYS ALA TYR ILE GLU TRP THR ASP
SEQRES 49 D 777 PRO ILE THR LYS ALA LYS ILE ASN THR ILE PRO THR SER
SEQRES 50 D 777 ALA GLU PHE ILE LYS ASN LEU SER SER ILE ARG ARG SER
SEQRES 51 D 777 SER ASN VAL GLY VAL TYR LYS ASP SER GLY ASP LYS ASP
SEQRES 52 D 777 GLU PHE ALA LYS LYS GLU SER VAL LYS LYS ILE ALA GLY
SEQRES 53 D 777 TYR LEU SER ASP TYR TYR ASN SER ALA ASN HIS ILE PHE
SEQRES 54 D 777 SER GLN GLU LYS LYS ARG LYS ILE SER ILE PHE ARG GLY
SEQRES 55 D 777 ILE GLN ALA TYR ASN GLU ILE GLU ASN VAL LEU LYS SER
SEQRES 56 D 777 LYS GLN ILE ALA PRO GLU TYR LYS ASN TYR PHE GLN TYR
SEQRES 57 D 777 LEU LYS GLU ARG ILE THR ASN GLN VAL GLN LEU LEU LEU
SEQRES 58 D 777 THR HIS GLN LYS SER ASN ILE GLU PHE LYS LEU LEU TYR
SEQRES 59 D 777 LYS GLN LEU ASN PHE THR GLU ASN GLU THR ASP ASN PHE
SEQRES 60 D 777 GLU VAL PHE GLN LYS ILE ILE ASP GLU LYS
SEQRES 1 E 777 MET HIS HIS HIS HIS HIS HIS ALA ALA ALA MET ASN GLU
SEQRES 2 E 777 HIS TYR THR GLU SER ASP ILE LYS ARG ASN HIS LYS THR
SEQRES 3 E 777 GLU LYS ASN LYS THR GLU LYS GLU LYS PHE LYS ASP SER
SEQRES 4 E 777 ILE ASN ASN LEU VAL LYS THR GLU PHE THR ASN GLU THR
SEQRES 5 E 777 LEU ASP LYS ILE GLN GLN THR GLN ASP LEU LEU LYS LYS
SEQRES 6 E 777 ILE PRO LYS ASP VAL LEU GLU ILE TYR SER GLU LEU GLY
SEQRES 7 E 777 GLY GLU ILE TYR PHE THR ASP ILE ASP LEU VAL GLU HIS
SEQRES 8 E 777 LYS GLU LEU GLN ASP LEU SER GLU GLU GLU LYS ASN SER
SEQRES 9 E 777 MET ASN SER ARG GLY GLU LYS VAL PRO PHE ALA SER ARG
SEQRES 10 E 777 PHE VAL PHE GLU LYS LYS ARG GLU THR PRO LYS LEU ILE
SEQRES 11 E 777 ILE ASN ILE LYS ASP TYR ALA ILE ASN SER GLU GLN SER
SEQRES 12 E 777 LYS GLU VAL TYR TYR GLU ILE GLY LYS GLY ILE SER LEU
SEQRES 13 E 777 ASP ILE ILE SER LYS ASP LYS SER LEU ASP PRO GLU PHE
SEQRES 14 E 777 LEU ASN LEU ILE LYS SER LEU SER ASP ASP SER ASP SER
SEQRES 15 E 777 SER ASP LEU LEU PHE SER GLN LYS PHE LYS GLU LYS LEU
SEQRES 16 E 777 GLU LEU ASN ASN LYS SER ILE ASP ILE ASN PHE ILE LYS
SEQRES 17 E 777 GLU ASN LEU THR GLU PHE GLN HIS ALA PHE SER LEU ALA
SEQRES 18 E 777 PHE SER TYR TYR PHE ALA PRO ASP HIS ARG THR VAL LEU
SEQRES 19 E 777 GLU LEU TYR ALA PRO ASP MET PHE GLU TYR MET ASN LYS
SEQRES 20 E 777 LEU GLU LYS GLY GLY PHE GLU LYS ILE SER GLU SER LEU
SEQRES 21 E 777 LYS LYS GLU GLY VAL GLU LYS ASP ARG ILE ASP VAL LEU
SEQRES 22 E 777 LYS GLY GLU LYS ALA LEU LYS ALA SER GLY LEU VAL PRO
SEQRES 23 E 777 GLU HIS ALA ASP ALA PHE LYS LYS ILE ALA ARG GLU LEU
SEQRES 24 E 777 ASN THR TYR ILE LEU PHE ARG PRO VAL ASN LYS LEU ALA
SEQRES 25 E 777 THR ASN LEU ILE LYS SER GLY VAL ALA THR LYS GLY LEU
SEQRES 26 E 777 ASN VAL HIS GLY LYS SER SER ASP TRP GLY PRO VAL ALA
SEQRES 27 E 777 GLY TYR ILE PRO PHE ASP GLN ASP LEU SER LYS LYS HIS
SEQRES 28 E 777 GLY GLN GLN LEU ALA VAL GLU LYS GLY ASN LEU GLU ASN
SEQRES 29 E 777 LYS LYS SER ILE THR GLU HIS GLU GLY GLU ILE GLY LYS
SEQRES 30 E 777 ILE PRO LEU LYS LEU ASP HIS LEU ARG ILE GLU GLU LEU
SEQRES 31 E 777 LYS GLU ASN GLY ILE ILE LEU LYS GLY LYS LYS GLU ILE
SEQRES 32 E 777 ASP ASN GLY LYS LYS TYR TYR LEU LEU GLU SER ASN ASN
SEQRES 33 E 777 GLN VAL TYR GLU PHE ARG ILE SER ASP GLU ASN ASN GLU
SEQRES 34 E 777 VAL GLN TYR LYS THR LYS GLU GLY LYS ILE THR VAL LEU
SEQRES 35 E 777 GLY GLU LYS PHE ASN TRP ARG ASN ILE GLU VAL MET ALA
SEQRES 36 E 777 LYS ASN VAL GLU GLY VAL LEU LYS PRO LEU THR ALA ASP
SEQRES 37 E 777 TYR ASP LEU PHE ALA LEU ALA PRO SER LEU THR GLU ILE
SEQRES 38 E 777 LYS LYS GLN ILE PRO GLN LYS GLU TRP ASP LYS VAL VAL
SEQRES 39 E 777 ASN THR PRO ASN SER LEU GLU LYS GLN LYS GLY VAL THR
SEQRES 40 E 777 ASN LEU LEU ILE LYS TYR GLY ILE GLU ARG LYS PRO ASP
SEQRES 41 E 777 SER THR LYS GLY THR LEU SER ASN TRP GLN LYS GLN MET
SEQRES 42 E 777 LEU ASP ARG LEU ASN GLU ALA VAL LYS TYR THR GLY TYR
SEQRES 43 E 777 THR GLY GLY ASP VAL VAL ASN HIS GLY THR GLU GLN ASP
SEQRES 44 E 777 ASN GLU GLU PHE PRO GLU LYS ASP ASN GLU ILE PHE ILE
SEQRES 45 E 777 ILE ASN PRO GLU GLY GLU PHE ILE LEU THR LYS ASN TRP
SEQRES 46 E 777 GLU MET THR GLY ARG PHE ILE GLU LYS ASN ILE THR GLY
SEQRES 47 E 777 LYS ASP TYR LEU TYR TYR PHE ASN ARG SER TYR ASN LYS
SEQRES 48 E 777 ILE ALA PRO GLY ASN LYS ALA TYR ILE GLU TRP THR ASP
SEQRES 49 E 777 PRO ILE THR LYS ALA LYS ILE ASN THR ILE PRO THR SER
SEQRES 50 E 777 ALA GLU PHE ILE LYS ASN LEU SER SER ILE ARG ARG SER
SEQRES 51 E 777 SER ASN VAL GLY VAL TYR LYS ASP SER GLY ASP LYS ASP
SEQRES 52 E 777 GLU PHE ALA LYS LYS GLU SER VAL LYS LYS ILE ALA GLY
SEQRES 53 E 777 TYR LEU SER ASP TYR TYR ASN SER ALA ASN HIS ILE PHE
SEQRES 54 E 777 SER GLN GLU LYS LYS ARG LYS ILE SER ILE PHE ARG GLY
SEQRES 55 E 777 ILE GLN ALA TYR ASN GLU ILE GLU ASN VAL LEU LYS SER
SEQRES 56 E 777 LYS GLN ILE ALA PRO GLU TYR LYS ASN TYR PHE GLN TYR
SEQRES 57 E 777 LEU LYS GLU ARG ILE THR ASN GLN VAL GLN LEU LEU LEU
SEQRES 58 E 777 THR HIS GLN LYS SER ASN ILE GLU PHE LYS LEU LEU TYR
SEQRES 59 E 777 LYS GLN LEU ASN PHE THR GLU ASN GLU THR ASP ASN PHE
SEQRES 60 E 777 GLU VAL PHE GLN LYS ILE ILE ASP GLU LYS
SEQRES 1 F 777 MET HIS HIS HIS HIS HIS HIS ALA ALA ALA MET ASN GLU
SEQRES 2 F 777 HIS TYR THR GLU SER ASP ILE LYS ARG ASN HIS LYS THR
SEQRES 3 F 777 GLU LYS ASN LYS THR GLU LYS GLU LYS PHE LYS ASP SER
SEQRES 4 F 777 ILE ASN ASN LEU VAL LYS THR GLU PHE THR ASN GLU THR
SEQRES 5 F 777 LEU ASP LYS ILE GLN GLN THR GLN ASP LEU LEU LYS LYS
SEQRES 6 F 777 ILE PRO LYS ASP VAL LEU GLU ILE TYR SER GLU LEU GLY
SEQRES 7 F 777 GLY GLU ILE TYR PHE THR ASP ILE ASP LEU VAL GLU HIS
SEQRES 8 F 777 LYS GLU LEU GLN ASP LEU SER GLU GLU GLU LYS ASN SER
SEQRES 9 F 777 MET ASN SER ARG GLY GLU LYS VAL PRO PHE ALA SER ARG
SEQRES 10 F 777 PHE VAL PHE GLU LYS LYS ARG GLU THR PRO LYS LEU ILE
SEQRES 11 F 777 ILE ASN ILE LYS ASP TYR ALA ILE ASN SER GLU GLN SER
SEQRES 12 F 777 LYS GLU VAL TYR TYR GLU ILE GLY LYS GLY ILE SER LEU
SEQRES 13 F 777 ASP ILE ILE SER LYS ASP LYS SER LEU ASP PRO GLU PHE
SEQRES 14 F 777 LEU ASN LEU ILE LYS SER LEU SER ASP ASP SER ASP SER
SEQRES 15 F 777 SER ASP LEU LEU PHE SER GLN LYS PHE LYS GLU LYS LEU
SEQRES 16 F 777 GLU LEU ASN ASN LYS SER ILE ASP ILE ASN PHE ILE LYS
SEQRES 17 F 777 GLU ASN LEU THR GLU PHE GLN HIS ALA PHE SER LEU ALA
SEQRES 18 F 777 PHE SER TYR TYR PHE ALA PRO ASP HIS ARG THR VAL LEU
SEQRES 19 F 777 GLU LEU TYR ALA PRO ASP MET PHE GLU TYR MET ASN LYS
SEQRES 20 F 777 LEU GLU LYS GLY GLY PHE GLU LYS ILE SER GLU SER LEU
SEQRES 21 F 777 LYS LYS GLU GLY VAL GLU LYS ASP ARG ILE ASP VAL LEU
SEQRES 22 F 777 LYS GLY GLU LYS ALA LEU LYS ALA SER GLY LEU VAL PRO
SEQRES 23 F 777 GLU HIS ALA ASP ALA PHE LYS LYS ILE ALA ARG GLU LEU
SEQRES 24 F 777 ASN THR TYR ILE LEU PHE ARG PRO VAL ASN LYS LEU ALA
SEQRES 25 F 777 THR ASN LEU ILE LYS SER GLY VAL ALA THR LYS GLY LEU
SEQRES 26 F 777 ASN VAL HIS GLY LYS SER SER ASP TRP GLY PRO VAL ALA
SEQRES 27 F 777 GLY TYR ILE PRO PHE ASP GLN ASP LEU SER LYS LYS HIS
SEQRES 28 F 777 GLY GLN GLN LEU ALA VAL GLU LYS GLY ASN LEU GLU ASN
SEQRES 29 F 777 LYS LYS SER ILE THR GLU HIS GLU GLY GLU ILE GLY LYS
SEQRES 30 F 777 ILE PRO LEU LYS LEU ASP HIS LEU ARG ILE GLU GLU LEU
SEQRES 31 F 777 LYS GLU ASN GLY ILE ILE LEU LYS GLY LYS LYS GLU ILE
SEQRES 32 F 777 ASP ASN GLY LYS LYS TYR TYR LEU LEU GLU SER ASN ASN
SEQRES 33 F 777 GLN VAL TYR GLU PHE ARG ILE SER ASP GLU ASN ASN GLU
SEQRES 34 F 777 VAL GLN TYR LYS THR LYS GLU GLY LYS ILE THR VAL LEU
SEQRES 35 F 777 GLY GLU LYS PHE ASN TRP ARG ASN ILE GLU VAL MET ALA
SEQRES 36 F 777 LYS ASN VAL GLU GLY VAL LEU LYS PRO LEU THR ALA ASP
SEQRES 37 F 777 TYR ASP LEU PHE ALA LEU ALA PRO SER LEU THR GLU ILE
SEQRES 38 F 777 LYS LYS GLN ILE PRO GLN LYS GLU TRP ASP LYS VAL VAL
SEQRES 39 F 777 ASN THR PRO ASN SER LEU GLU LYS GLN LYS GLY VAL THR
SEQRES 40 F 777 ASN LEU LEU ILE LYS TYR GLY ILE GLU ARG LYS PRO ASP
SEQRES 41 F 777 SER THR LYS GLY THR LEU SER ASN TRP GLN LYS GLN MET
SEQRES 42 F 777 LEU ASP ARG LEU ASN GLU ALA VAL LYS TYR THR GLY TYR
SEQRES 43 F 777 THR GLY GLY ASP VAL VAL ASN HIS GLY THR GLU GLN ASP
SEQRES 44 F 777 ASN GLU GLU PHE PRO GLU LYS ASP ASN GLU ILE PHE ILE
SEQRES 45 F 777 ILE ASN PRO GLU GLY GLU PHE ILE LEU THR LYS ASN TRP
SEQRES 46 F 777 GLU MET THR GLY ARG PHE ILE GLU LYS ASN ILE THR GLY
SEQRES 47 F 777 LYS ASP TYR LEU TYR TYR PHE ASN ARG SER TYR ASN LYS
SEQRES 48 F 777 ILE ALA PRO GLY ASN LYS ALA TYR ILE GLU TRP THR ASP
SEQRES 49 F 777 PRO ILE THR LYS ALA LYS ILE ASN THR ILE PRO THR SER
SEQRES 50 F 777 ALA GLU PHE ILE LYS ASN LEU SER SER ILE ARG ARG SER
SEQRES 51 F 777 SER ASN VAL GLY VAL TYR LYS ASP SER GLY ASP LYS ASP
SEQRES 52 F 777 GLU PHE ALA LYS LYS GLU SER VAL LYS LYS ILE ALA GLY
SEQRES 53 F 777 TYR LEU SER ASP TYR TYR ASN SER ALA ASN HIS ILE PHE
SEQRES 54 F 777 SER GLN GLU LYS LYS ARG LYS ILE SER ILE PHE ARG GLY
SEQRES 55 F 777 ILE GLN ALA TYR ASN GLU ILE GLU ASN VAL LEU LYS SER
SEQRES 56 F 777 LYS GLN ILE ALA PRO GLU TYR LYS ASN TYR PHE GLN TYR
SEQRES 57 F 777 LEU LYS GLU ARG ILE THR ASN GLN VAL GLN LEU LEU LEU
SEQRES 58 F 777 THR HIS GLN LYS SER ASN ILE GLU PHE LYS LEU LEU TYR
SEQRES 59 F 777 LYS GLN LEU ASN PHE THR GLU ASN GLU THR ASP ASN PHE
SEQRES 60 F 777 GLU VAL PHE GLN LYS ILE ILE ASP GLU LYS
SEQRES 1 O 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 O 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 O 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 O 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 O 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 O 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 O 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 O 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 O 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 O 149 THR ASP GLU GLU VAL ASP GLN MET ILE ARG GLU ALA ASP
SEQRES 11 O 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 O 149 GLN MET MET THR ALA LYS
SEQRES 1 P 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 P 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 P 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 P 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 P 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 P 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 P 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 P 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 P 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 P 149 THR ASP GLU GLU VAL ASP GLN MET ILE ARG GLU ALA ASP
SEQRES 11 P 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 P 149 GLN MET MET THR ALA LYS
SEQRES 1 Q 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 Q 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 Q 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 Q 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 Q 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 Q 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 Q 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 Q 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 Q 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 Q 149 THR ASP GLU GLU VAL ASP GLN MET ILE ARG GLU ALA ASP
SEQRES 11 Q 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 Q 149 GLN MET MET THR ALA LYS
SEQRES 1 R 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 R 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 R 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 R 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 R 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 R 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 R 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 R 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 R 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 R 149 THR ASP GLU GLU VAL ASP GLN MET ILE ARG GLU ALA ASP
SEQRES 11 R 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 R 149 GLN MET MET THR ALA LYS
SEQRES 1 S 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 S 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 S 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 S 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 S 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 S 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 S 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 S 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 S 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 S 149 THR ASP GLU GLU VAL ASP GLN MET ILE ARG GLU ALA ASP
SEQRES 11 S 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 S 149 GLN MET MET THR ALA LYS
SEQRES 1 T 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 T 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 T 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 T 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 T 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 T 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 T 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 T 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 T 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 T 149 THR ASP GLU GLU VAL ASP GLN MET ILE ARG GLU ALA ASP
SEQRES 11 T 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 T 149 GLN MET MET THR ALA LYS
HET MG A 900 1
HET CMP A 901 22
HET MG B 901 1
HET CMP B 902 22
HET MG C 902 1
HET CMP C 903 22
HET MG D 903 1
HET CMP D 904 22
HET MG E 904 1
HET CMP E 905 22
HET MG F 905 1
HET CMP F 906 22
HET CA O 701 1
HET CA O 801 1
HET CA O 802 1
HET CA P 703 1
HET CA P 803 1
HET CA P 804 1
HET CA Q 705 1
HET CA Q 805 1
HET CA Q 806 1
HET CA R 707 1
HET CA R 807 1
HET CA R 808 1
HET CA S 709 1
HET CA S 809 1
HET CA S 810 1
HET CA T 711 1
HET CA T 811 1
HET CA T 812 1
HETNAM MG MAGNESIUM ION
HETNAM CMP ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
HETNAM CA CALCIUM ION
HETSYN CMP CYCLIC AMP; CAMP
FORMUL 13 MG 6(MG 2+)
FORMUL 14 CMP 6(C10 H12 N5 O6 P)
FORMUL 25 CA 18(CA 2+)
FORMUL 43 HOH *6(H2 O)
HELIX 1 1 THR A 75 LYS A 87 1 13
HELIX 2 2 PRO A 90 LEU A 100 1 11
HELIX 3 3 PRO A 136 ARG A 140 5 5
HELIX 4 4 GLU A 168 ILE A 177 1 10
HELIX 5 5 GLU A 191 SER A 198 1 8
HELIX 6 6 LEU A 234 GLU A 236 5 3
HELIX 7 7 PHE A 237 ALA A 250 1 14
HELIX 8 8 THR A 255 TYR A 260 1 6
HELIX 9 9 PRO A 262 GLY A 274 1 13
HELIX 10 10 GLY A 274 GLU A 289 1 16
HELIX 11 11 LYS A 297 GLY A 306 1 10
HELIX 12 12 VAL A 308 ASN A 323 1 16
HELIX 13 13 ASN A 332 GLY A 342 1 11
HELIX 14 14 ASP A 367 SER A 371 5 5
HELIX 15 15 GLY A 383 HIS A 394 1 12
HELIX 16 16 ASP A 406 ASN A 416 1 11
HELIX 17 17 SER A 500 LYS A 506 1 7
HELIX 18 18 LYS A 511 ASN A 518 1 8
HELIX 19 19 LEU A 523 GLY A 537 1 15
HELIX 20 20 SER A 550 VAL A 564 1 15
HELIX 21 21 THR A 579 ASN A 583 5 5
HELIX 22 22 ASN A 607 ILE A 619 1 13
HELIX 23 23 THR A 620 ASP A 623 5 4
HELIX 24 24 ASP A 647 ALA A 652 1 6
HELIX 25 25 THR A 659 SER A 674 1 16
HELIX 26 26 ASP A 684 TYR A 705 1 22
HELIX 27 27 ASN A 706 PHE A 712 5 7
HELIX 28 28 SER A 713 LYS A 737 1 25
HELIX 29 29 ALA A 742 LEU A 763 1 22
HELIX 30 30 GLU A 772 GLN A 779 1 8
HELIX 31 31 GLU A 786 ILE A 796 1 11
HELIX 32 32 THR B 75 LYS B 87 1 13
HELIX 33 33 PRO B 90 LEU B 100 1 11
HELIX 34 34 PRO B 136 ARG B 140 5 5
HELIX 35 35 GLU B 168 ILE B 177 1 10
HELIX 36 36 GLU B 191 SER B 198 1 8
HELIX 37 37 LEU B 234 GLU B 236 5 3
HELIX 38 38 PHE B 237 ALA B 250 1 14
HELIX 39 39 THR B 255 TYR B 260 1 6
HELIX 40 40 PRO B 262 GLY B 274 1 13
HELIX 41 41 GLY B 274 GLU B 289 1 16
HELIX 42 42 LYS B 297 GLY B 306 1 10
HELIX 43 43 VAL B 308 ASN B 323 1 16
HELIX 44 44 ASN B 332 GLY B 342 1 11
HELIX 45 45 ASP B 367 SER B 371 5 5
HELIX 46 46 GLY B 383 HIS B 394 1 12
HELIX 47 47 ASP B 406 ASN B 416 1 11
HELIX 48 48 SER B 500 LYS B 506 1 7
HELIX 49 49 LYS B 511 ASN B 518 1 8
HELIX 50 50 LEU B 523 GLY B 537 1 15
HELIX 51 51 SER B 550 VAL B 564 1 15
HELIX 52 52 THR B 579 ASN B 583 5 5
HELIX 53 53 ASN B 607 ILE B 619 1 13
HELIX 54 54 ASP B 647 ALA B 652 1 6
HELIX 55 55 THR B 659 SER B 674 1 16
HELIX 56 56 ASP B 684 TYR B 705 1 22
HELIX 57 57 ASN B 706 PHE B 712 5 7
HELIX 58 58 SER B 713 LYS B 737 1 25
HELIX 59 59 ALA B 742 LEU B 763 1 22
HELIX 60 60 GLU B 772 GLN B 779 1 8
HELIX 61 61 GLU B 786 ILE B 796 1 11
HELIX 62 62 THR C 75 LYS C 87 1 13
HELIX 63 63 PRO C 90 LEU C 100 1 11
HELIX 64 64 PRO C 136 ARG C 140 5 5
HELIX 65 65 GLU C 168 ILE C 177 1 10
HELIX 66 66 GLU C 191 SER C 198 1 8
HELIX 67 67 LEU C 234 GLU C 236 5 3
HELIX 68 68 PHE C 237 ALA C 250 1 14
HELIX 69 69 THR C 255 TYR C 260 1 6
HELIX 70 70 PRO C 262 GLY C 274 1 13
HELIX 71 71 GLY C 274 GLU C 289 1 16
HELIX 72 72 LYS C 297 GLY C 306 1 10
HELIX 73 73 VAL C 308 ASN C 323 1 16
HELIX 74 74 ASN C 332 GLY C 342 1 11
HELIX 75 75 ASP C 367 SER C 371 5 5
HELIX 76 76 GLY C 383 HIS C 394 1 12
HELIX 77 77 ASP C 406 ASN C 416 1 11
HELIX 78 78 SER C 500 LYS C 506 1 7
HELIX 79 79 LYS C 511 ASN C 518 1 8
HELIX 80 80 LEU C 523 GLY C 537 1 15
HELIX 81 81 SER C 550 VAL C 564 1 15
HELIX 82 82 THR C 579 ASN C 583 5 5
HELIX 83 83 ASN C 607 ILE C 619 1 13
HELIX 84 84 THR C 620 ASP C 623 5 4
HELIX 85 85 ASP C 647 ALA C 652 1 6
HELIX 86 86 THR C 659 SER C 674 1 16
HELIX 87 87 ASP C 684 TYR C 705 1 22
HELIX 88 88 ASN C 706 PHE C 712 5 7
HELIX 89 89 SER C 713 LYS C 737 1 25
HELIX 90 90 ALA C 742 LEU C 763 1 22
HELIX 91 91 GLU C 772 GLN C 779 1 8
HELIX 92 92 GLU C 786 ILE C 796 1 11
HELIX 93 93 THR D 75 LYS D 87 1 13
HELIX 94 94 PRO D 90 LEU D 100 1 11
HELIX 95 95 PRO D 136 ARG D 140 5 5
HELIX 96 96 GLU D 168 ILE D 177 1 10
HELIX 97 97 GLU D 191 SER D 198 1 8
HELIX 98 98 LEU D 234 GLU D 236 5 3
HELIX 99 99 PHE D 237 ALA D 250 1 14
HELIX 100 100 THR D 255 TYR D 260 1 6
HELIX 101 101 PRO D 262 GLY D 274 1 13
HELIX 102 102 GLY D 274 GLU D 289 1 16
HELIX 103 103 LYS D 297 GLY D 306 1 10
HELIX 104 104 VAL D 308 ASN D 323 1 16
HELIX 105 105 ASN D 332 GLY D 342 1 11
HELIX 106 106 ASP D 367 SER D 371 5 5
HELIX 107 107 GLY D 383 HIS D 394 1 12
HELIX 108 108 ASP D 406 ASN D 416 1 11
HELIX 109 109 SER D 500 LYS D 506 1 7
HELIX 110 110 LYS D 511 ASN D 518 1 8
HELIX 111 111 LEU D 523 GLY D 537 1 15
HELIX 112 112 SER D 550 VAL D 564 1 15
HELIX 113 113 THR D 579 ASN D 583 5 5
HELIX 114 114 ASN D 607 ILE D 619 1 13
HELIX 115 115 ASP D 647 ALA D 652 1 6
HELIX 116 116 THR D 659 SER D 674 1 16
HELIX 117 117 ASP D 684 TYR D 705 1 22
HELIX 118 118 ASN D 706 PHE D 712 5 7
HELIX 119 119 SER D 713 LYS D 737 1 25
HELIX 120 120 ALA D 742 LEU D 763 1 22
HELIX 121 121 GLU D 772 GLN D 779 1 8
HELIX 122 122 GLU D 786 ILE D 796 1 11
HELIX 123 123 THR E 75 LYS E 87 1 13
HELIX 124 124 PRO E 90 LEU E 100 1 11
HELIX 125 125 PRO E 136 ARG E 140 5 5
HELIX 126 126 GLU E 168 ILE E 177 1 10
HELIX 127 127 GLU E 191 SER E 198 1 8
HELIX 128 128 LEU E 234 GLU E 236 5 3
HELIX 129 129 PHE E 237 ALA E 250 1 14
HELIX 130 130 THR E 255 TYR E 260 1 6
HELIX 131 131 PRO E 262 GLY E 274 1 13
HELIX 132 132 GLY E 274 GLU E 289 1 16
HELIX 133 133 LYS E 297 GLY E 306 1 10
HELIX 134 134 VAL E 308 ASN E 323 1 16
HELIX 135 135 ASN E 332 GLY E 342 1 11
HELIX 136 136 ASP E 367 SER E 371 5 5
HELIX 137 137 GLY E 383 HIS E 394 1 12
HELIX 138 138 ASP E 406 ASN E 416 1 11
HELIX 139 139 SER E 500 LYS E 506 1 7
HELIX 140 140 LYS E 511 ASN E 518 1 8
HELIX 141 141 LEU E 523 GLY E 537 1 15
HELIX 142 142 SER E 550 VAL E 564 1 15
HELIX 143 143 THR E 579 ASN E 583 5 5
HELIX 144 144 ASN E 607 ILE E 619 1 13
HELIX 145 145 THR E 620 ASP E 623 5 4
HELIX 146 146 ASP E 647 ALA E 652 1 6
HELIX 147 147 THR E 659 SER E 674 1 16
HELIX 148 148 ASP E 684 TYR E 705 1 22
HELIX 149 149 ASN E 706 PHE E 712 5 7
HELIX 150 150 SER E 713 LYS E 737 1 25
HELIX 151 151 ALA E 742 LEU E 763 1 22
HELIX 152 152 GLU E 772 GLN E 779 1 8
HELIX 153 153 GLU E 786 ILE E 796 1 11
HELIX 154 154 THR F 75 LYS F 87 1 13
HELIX 155 155 PRO F 90 LEU F 100 1 11
HELIX 156 156 PRO F 136 ARG F 140 5 5
HELIX 157 157 GLU F 168 ILE F 177 1 10
HELIX 158 158 GLU F 191 SER F 198 1 8
HELIX 159 159 LEU F 234 GLU F 236 5 3
HELIX 160 160 PHE F 237 ALA F 250 1 14
HELIX 161 161 THR F 255 TYR F 260 1 6
HELIX 162 162 PRO F 262 GLY F 274 1 13
HELIX 163 163 GLY F 274 GLU F 289 1 16
HELIX 164 164 LYS F 297 GLY F 306 1 10
HELIX 165 165 VAL F 308 ASN F 323 1 16
HELIX 166 166 ASN F 332 GLY F 342 1 11
HELIX 167 167 ASP F 367 SER F 371 5 5
HELIX 168 168 GLY F 383 HIS F 394 1 12
HELIX 169 169 ASP F 406 ASN F 416 1 11
HELIX 170 170 SER F 500 LYS F 506 1 7
HELIX 171 171 LYS F 511 ASN F 518 1 8
HELIX 172 172 LEU F 523 GLY F 537 1 15
HELIX 173 173 SER F 550 VAL F 564 1 15
HELIX 174 174 THR F 579 ASN F 583 5 5
HELIX 175 175 ASN F 607 ILE F 619 1 13
HELIX 176 176 ASP F 647 ALA F 652 1 6
HELIX 177 177 THR F 659 SER F 674 1 16
HELIX 178 178 ASP F 684 TYR F 705 1 22
HELIX 179 179 ASN F 706 PHE F 712 5 7
HELIX 180 180 SER F 713 LYS F 737 1 25
HELIX 181 181 ALA F 742 LEU F 763 1 22
HELIX 182 182 GLU F 772 GLN F 779 1 8
HELIX 183 183 GLU F 786 ILE F 796 1 11
HELIX 184 184 GLU O 6 ALA O 15 1 10
HELIX 185 185 THR O 29 GLY O 40 1 12
HELIX 186 186 ALA O 46 GLU O 54 1 9
HELIX 187 187 PHE O 65 THR O 70 1 6
HELIX 188 188 ASP O 80 ASP O 93 1 14
HELIX 189 189 SER O 101 LEU O 112 1 12
HELIX 190 190 THR O 117 VAL O 121 5 5
HELIX 191 191 GLN O 123 ASP O 129 1 7
HELIX 192 192 TYR O 138 ALA O 147 1 10
HELIX 193 193 GLU P 6 ALA P 15 1 10
HELIX 194 194 THR P 29 GLY P 40 1 12
HELIX 195 195 ALA P 46 GLU P 54 1 9
HELIX 196 196 PHE P 65 THR P 70 1 6
HELIX 197 197 ASP P 80 ASP P 93 1 14
HELIX 198 198 SER P 101 LEU P 112 1 12
HELIX 199 199 THR P 117 VAL P 121 5 5
HELIX 200 200 GLN P 123 ASP P 129 1 7
HELIX 201 201 TYR P 138 ALA P 147 1 10
HELIX 202 202 GLU Q 6 ALA Q 15 1 10
HELIX 203 203 THR Q 29 GLY Q 40 1 12
HELIX 204 204 ALA Q 46 GLU Q 54 1 9
HELIX 205 205 PHE Q 65 THR Q 70 1 6
HELIX 206 206 ASP Q 80 ASP Q 93 1 14
HELIX 207 207 SER Q 101 LEU Q 112 1 12
HELIX 208 208 THR Q 117 VAL Q 121 5 5
HELIX 209 209 GLN Q 123 ASP Q 129 1 7
HELIX 210 210 TYR Q 138 ALA Q 147 1 10
HELIX 211 211 GLU R 6 ALA R 15 1 10
HELIX 212 212 THR R 29 GLY R 40 1 12
HELIX 213 213 ALA R 46 GLU R 54 1 9
HELIX 214 214 PHE R 65 THR R 70 1 6
HELIX 215 215 ASP R 80 ASP R 93 1 14
HELIX 216 216 SER R 101 LEU R 112 1 12
HELIX 217 217 THR R 117 VAL R 121 5 5
HELIX 218 218 GLN R 123 ASP R 129 1 7
HELIX 219 219 TYR R 138 ALA R 147 1 10
HELIX 220 220 GLU S 6 ALA S 15 1 10
HELIX 221 221 THR S 29 GLY S 40 1 12
HELIX 222 222 ALA S 46 GLU S 54 1 9
HELIX 223 223 PHE S 65 THR S 70 1 6
HELIX 224 224 ASP S 80 ASP S 93 1 14
HELIX 225 225 SER S 101 LEU S 112 1 12
HELIX 226 226 THR S 117 VAL S 121 5 5
HELIX 227 227 GLN S 123 ASP S 129 1 7
HELIX 228 228 TYR S 138 ALA S 147 1 10
HELIX 229 229 GLU T 6 ALA T 15 1 10
HELIX 230 230 THR T 29 GLY T 40 1 12
HELIX 231 231 ALA T 46 GLU T 54 1 9
HELIX 232 232 PHE T 65 THR T 70 1 6
HELIX 233 233 ASP T 80 ASP T 93 1 14
HELIX 234 234 SER T 101 LEU T 112 1 12
HELIX 235 235 THR T 117 VAL T 121 5 5
HELIX 236 236 GLN T 123 ASP T 129 1 7
HELIX 237 237 TYR T 138 ALA T 147 1 10
SHEET 1 A 4 VAL A 67 THR A 69 0
SHEET 2 A 4 GLU A 103 THR A 107 1 O PHE A 106 N LYS A 68
SHEET 3 A 4 LYS A 151 ASN A 155 1 O ILE A 154 N TYR A 105
SHEET 4 A 4 VAL A 142 LYS A 145 -1 N PHE A 143 O ILE A 153
SHEET 1 B 4 LEU A 494 PRO A 499 0
SHEET 2 B 4 THR A 324 PHE A 328 -1 N LEU A 327 O PHE A 495
SHEET 3 B 4 PHE A 594 ILE A 596 -1 O PHE A 594 N PHE A 328
SHEET 4 B 4 PHE A 602 LEU A 604 -1 O ILE A 603 N ILE A 595
SHEET 1 C 4 ALA A 344 THR A 345 0
SHEET 2 C 4 LEU A 485 THR A 489 1 O THR A 489 N ALA A 344
SHEET 3 C 4 GLU A 475 ASN A 480 -1 N MET A 477 O LEU A 488
SHEET 4 C 4 GLY A 399 PRO A 402 -1 N GLY A 399 O ALA A 478
SHEET 1 D 5 LEU A 420 ASP A 427 0
SHEET 2 D 5 LYS A 430 GLU A 436 -1 O LYS A 430 N ASP A 427
SHEET 3 D 5 TYR A 442 ILE A 446 -1 O ILE A 446 N TYR A 433
SHEET 4 D 5 VAL A 453 THR A 457 -1 O GLN A 454 N ARG A 445
SHEET 5 D 5 ARG A 472 ASN A 473 -1 O ARG A 472 N TYR A 455
SHEET 1 E 2 ILE A 635 ALA A 636 0
SHEET 2 E 2 ALA A 641 TYR A 642 -1 O ALA A 641 N ALA A 636
SHEET 1 F 4 VAL B 67 THR B 69 0
SHEET 2 F 4 GLU B 103 THR B 107 1 O PHE B 106 N LYS B 68
SHEET 3 F 4 LYS B 151 ASN B 155 1 O ILE B 154 N TYR B 105
SHEET 4 F 4 VAL B 142 LYS B 145 -1 N PHE B 143 O ILE B 153
SHEET 1 G 4 LEU B 494 PRO B 499 0
SHEET 2 G 4 THR B 324 PHE B 328 -1 N LEU B 327 O PHE B 495
SHEET 3 G 4 PHE B 594 ILE B 596 -1 O PHE B 594 N PHE B 328
SHEET 4 G 4 PHE B 602 LEU B 604 -1 O ILE B 603 N ILE B 595
SHEET 1 H 4 ALA B 344 THR B 345 0
SHEET 2 H 4 LEU B 485 THR B 489 1 O THR B 489 N ALA B 344
SHEET 3 H 4 GLU B 475 ASN B 480 -1 N MET B 477 O LEU B 488
SHEET 4 H 4 GLY B 399 PRO B 402 -1 N GLY B 399 O ALA B 478
SHEET 1 I 5 LEU B 420 ASP B 427 0
SHEET 2 I 5 LYS B 430 GLU B 436 -1 O LYS B 430 N ASP B 427
SHEET 3 I 5 TYR B 442 ILE B 446 -1 O ILE B 446 N TYR B 433
SHEET 4 I 5 VAL B 453 THR B 457 -1 O GLN B 454 N ARG B 445
SHEET 5 I 5 ARG B 472 ASN B 473 -1 O ARG B 472 N TYR B 455
SHEET 1 J 2 ILE B 635 ALA B 636 0
SHEET 2 J 2 ALA B 641 TYR B 642 -1 O ALA B 641 N ALA B 636
SHEET 1 K 4 VAL C 67 THR C 69 0
SHEET 2 K 4 GLU C 103 THR C 107 1 O PHE C 106 N LYS C 68
SHEET 3 K 4 LYS C 151 ASN C 155 1 O ILE C 154 N TYR C 105
SHEET 4 K 4 VAL C 142 LYS C 145 -1 N PHE C 143 O ILE C 153
SHEET 1 L 4 LEU C 494 PRO C 499 0
SHEET 2 L 4 THR C 324 PHE C 328 -1 N LEU C 327 O PHE C 495
SHEET 3 L 4 PHE C 594 ILE C 596 -1 O PHE C 594 N PHE C 328
SHEET 4 L 4 PHE C 602 LEU C 604 -1 O ILE C 603 N ILE C 595
SHEET 1 M 4 ALA C 344 THR C 345 0
SHEET 2 M 4 LEU C 485 THR C 489 1 O THR C 489 N ALA C 344
SHEET 3 M 4 GLU C 475 ASN C 480 -1 N MET C 477 O LEU C 488
SHEET 4 M 4 GLY C 399 PRO C 402 -1 N GLY C 399 O ALA C 478
SHEET 1 N 5 LEU C 420 ASP C 427 0
SHEET 2 N 5 LYS C 430 GLU C 436 -1 O LYS C 430 N ASP C 427
SHEET 3 N 5 TYR C 442 ILE C 446 -1 O ILE C 446 N TYR C 433
SHEET 4 N 5 VAL C 453 THR C 457 -1 O GLN C 454 N ARG C 445
SHEET 5 N 5 ARG C 472 ASN C 473 -1 O ARG C 472 N TYR C 455
SHEET 1 O 2 ILE C 635 ALA C 636 0
SHEET 2 O 2 ALA C 641 TYR C 642 -1 O ALA C 641 N ALA C 636
SHEET 1 P 4 VAL D 67 THR D 69 0
SHEET 2 P 4 GLU D 103 THR D 107 1 O PHE D 106 N LYS D 68
SHEET 3 P 4 LYS D 151 ASN D 155 1 O ILE D 154 N TYR D 105
SHEET 4 P 4 VAL D 142 LYS D 145 -1 N PHE D 143 O ILE D 153
SHEET 1 Q 4 LEU D 494 PRO D 499 0
SHEET 2 Q 4 THR D 324 PHE D 328 -1 N LEU D 327 O PHE D 495
SHEET 3 Q 4 PHE D 594 ILE D 596 -1 O PHE D 594 N PHE D 328
SHEET 4 Q 4 PHE D 602 LEU D 604 -1 O ILE D 603 N ILE D 595
SHEET 1 R 4 ALA D 344 THR D 345 0
SHEET 2 R 4 LEU D 485 THR D 489 1 O THR D 489 N ALA D 344
SHEET 3 R 4 GLU D 475 ASN D 480 -1 N MET D 477 O LEU D 488
SHEET 4 R 4 GLY D 399 PRO D 402 -1 N GLY D 399 O ALA D 478
SHEET 1 S 5 LEU D 420 ASP D 427 0
SHEET 2 S 5 LYS D 430 GLU D 436 -1 O LYS D 430 N ASP D 427
SHEET 3 S 5 TYR D 442 ILE D 446 -1 O ILE D 446 N TYR D 433
SHEET 4 S 5 VAL D 453 THR D 457 -1 O GLN D 454 N ARG D 445
SHEET 5 S 5 ARG D 472 ASN D 473 -1 O ARG D 472 N TYR D 455
SHEET 1 T 2 ILE D 635 ALA D 636 0
SHEET 2 T 2 ALA D 641 TYR D 642 -1 O ALA D 641 N ALA D 636
SHEET 1 U 4 VAL E 67 THR E 69 0
SHEET 2 U 4 GLU E 103 THR E 107 1 O PHE E 106 N LYS E 68
SHEET 3 U 4 LYS E 151 ASN E 155 1 O ILE E 154 N TYR E 105
SHEET 4 U 4 VAL E 142 LYS E 145 -1 N PHE E 143 O ILE E 153
SHEET 1 V 4 LEU E 494 PRO E 499 0
SHEET 2 V 4 THR E 324 PHE E 328 -1 N LEU E 327 O PHE E 495
SHEET 3 V 4 PHE E 594 ILE E 596 -1 O PHE E 594 N PHE E 328
SHEET 4 V 4 PHE E 602 LEU E 604 -1 O ILE E 603 N ILE E 595
SHEET 1 W 4 ALA E 344 THR E 345 0
SHEET 2 W 4 LEU E 485 THR E 489 1 O THR E 489 N ALA E 344
SHEET 3 W 4 GLU E 475 ASN E 480 -1 N MET E 477 O LEU E 488
SHEET 4 W 4 GLY E 399 PRO E 402 -1 N GLY E 399 O ALA E 478
SHEET 1 X 5 LEU E 420 ASP E 427 0
SHEET 2 X 5 LYS E 430 GLU E 436 -1 O LYS E 430 N ASP E 427
SHEET 3 X 5 TYR E 442 ILE E 446 -1 O ILE E 446 N TYR E 433
SHEET 4 X 5 VAL E 453 THR E 457 -1 O GLN E 454 N ARG E 445
SHEET 5 X 5 ARG E 472 ASN E 473 -1 O ARG E 472 N TYR E 455
SHEET 1 Y 2 ILE E 635 ALA E 636 0
SHEET 2 Y 2 ALA E 641 TYR E 642 -1 O ALA E 641 N ALA E 636
SHEET 1 Z 4 VAL F 67 THR F 69 0
SHEET 2 Z 4 GLU F 103 THR F 107 1 O PHE F 106 N LYS F 68
SHEET 3 Z 4 LYS F 151 ASN F 155 1 O ILE F 154 N TYR F 105
SHEET 4 Z 4 VAL F 142 LYS F 145 -1 N PHE F 143 O ILE F 153
SHEET 1 AA 4 LEU F 494 PRO F 499 0
SHEET 2 AA 4 THR F 324 PHE F 328 -1 N LEU F 327 O PHE F 495
SHEET 3 AA 4 PHE F 594 ILE F 596 -1 O PHE F 594 N PHE F 328
SHEET 4 AA 4 PHE F 602 LEU F 604 -1 O ILE F 603 N ILE F 595
SHEET 1 AB 4 ALA F 344 THR F 345 0
SHEET 2 AB 4 LEU F 485 THR F 489 1 O THR F 489 N ALA F 344
SHEET 3 AB 4 GLU F 475 ASN F 480 -1 N MET F 477 O LEU F 488
SHEET 4 AB 4 GLY F 399 PRO F 402 -1 N GLY F 399 O ALA F 478
SHEET 1 AC 5 LEU F 420 ASP F 427 0
SHEET 2 AC 5 LYS F 430 GLU F 436 -1 O LYS F 430 N ASP F 427
SHEET 3 AC 5 TYR F 442 ILE F 446 -1 O ILE F 446 N TYR F 433
SHEET 4 AC 5 VAL F 453 THR F 457 -1 O GLN F 454 N ARG F 445
SHEET 5 AC 5 ARG F 472 ASN F 473 -1 O ARG F 472 N TYR F 455
SHEET 1 AD 2 ILE F 635 ALA F 636 0
SHEET 2 AD 2 ALA F 641 TYR F 642 -1 O ALA F 641 N ALA F 636
SHEET 1 AE 2 ILE O 27 THR O 28 0
SHEET 2 AE 2 THR O 62 ILE O 63 -1 O ILE O 63 N ILE O 27
SHEET 1 AF 2 TYR O 99 ILE O 100 0
SHEET 2 AF 2 VAL O 136 ASN O 137 -1 O VAL O 136 N ILE O 100
SHEET 1 AG 2 ILE P 27 THR P 28 0
SHEET 2 AG 2 THR P 62 ILE P 63 -1 O ILE P 63 N ILE P 27
SHEET 1 AH 2 TYR P 99 ILE P 100 0
SHEET 2 AH 2 VAL P 136 ASN P 137 -1 O VAL P 136 N ILE P 100
SHEET 1 AI 2 ILE Q 27 THR Q 28 0
SHEET 2 AI 2 THR Q 62 ILE Q 63 -1 O ILE Q 63 N ILE Q 27
SHEET 1 AJ 2 TYR Q 99 ILE Q 100 0
SHEET 2 AJ 2 VAL Q 136 ASN Q 137 -1 O VAL Q 136 N ILE Q 100
SHEET 1 AK 2 ILE R 27 THR R 28 0
SHEET 2 AK 2 THR R 62 ILE R 63 -1 O ILE R 63 N ILE R 27
SHEET 1 AL 2 TYR R 99 ILE R 100 0
SHEET 2 AL 2 VAL R 136 ASN R 137 -1 O VAL R 136 N ILE R 100
SHEET 1 AM 2 ILE S 27 THR S 28 0
SHEET 2 AM 2 THR S 62 ILE S 63 -1 O ILE S 63 N ILE S 27
SHEET 1 AN 2 TYR S 99 ILE S 100 0
SHEET 2 AN 2 VAL S 136 ASN S 137 -1 O VAL S 136 N ILE S 100
SHEET 1 AO 2 ILE T 27 THR T 28 0
SHEET 2 AO 2 THR T 62 ILE T 63 -1 O ILE T 63 N ILE T 27
SHEET 1 AP 2 TYR T 99 ILE T 100 0
SHEET 2 AP 2 VAL T 136 ASN T 137 -1 O VAL T 136 N ILE T 100
LINK OD2 ASP A 491 MG MG A 900 1555 1555 2.71
LINK OD1 ASP A 491 MG MG A 900 1555 1555 2.12
LINK OD2 ASP A 493 MG MG A 900 1555 1555 2.62
LINK NE2 HIS A 577 MG MG A 900 1555 1555 2.52
LINK OD2 ASP B 491 MG MG B 901 1555 1555 2.80
LINK OD1 ASP B 491 MG MG B 901 1555 1555 2.21
LINK OD2 ASP B 493 MG MG B 901 1555 1555 2.72
LINK NE2 HIS B 577 MG MG B 901 1555 1555 2.50
LINK MG MG B 901 O1P CMP B 902 1555 1555 3.13
LINK OD1 ASP C 491 MG MG C 902 1555 1555 2.11
LINK OD2 ASP C 491 MG MG C 902 1555 1555 2.64
LINK OD2 ASP C 493 MG MG C 902 1555 1555 2.64
LINK NE2 HIS C 577 MG MG C 902 1555 1555 2.61
LINK MG MG C 902 O1P CMP C 903 1555 1555 3.10
LINK OD2 ASP D 491 MG MG D 903 1555 1555 2.79
LINK OD1 ASP D 491 MG MG D 903 1555 1555 2.20
LINK OD2 ASP D 493 MG MG D 903 1555 1555 2.78
LINK NE2 HIS D 577 MG MG D 903 1555 1555 2.59
LINK MG MG D 903 O1P CMP D 904 1555 1555 3.12
LINK OD1 ASP E 491 MG MG E 904 1555 1555 2.18
LINK OD2 ASP E 491 MG MG E 904 1555 1555 2.70
LINK OD2 ASP E 493 MG MG E 904 1555 1555 2.67
LINK NE2 HIS E 577 MG MG E 904 1555 1555 2.58
LINK MG MG E 904 O1P CMP E 905 1555 1555 3.08
LINK OD1 ASP F 491 MG MG F 905 1555 1555 2.20
LINK OD2 ASP F 491 MG MG F 905 1555 1555 2.64
LINK OD2 ASP F 493 MG MG F 905 1555 1555 2.63
LINK NE2 HIS F 577 MG MG F 905 1555 1555 2.65
LINK MG MG F 905 O1P CMP F 906 1555 1555 3.09
LINK OD2 ASP O 20 CA CA O 701 1555 1555 2.36
LINK OD2 ASP O 22 CA CA O 701 1555 1555 2.63
LINK OD1 ASP O 22 CA CA O 701 1555 1555 2.30
LINK OD1 ASP O 24 CA CA O 701 1555 1555 2.28
LINK OD2 ASP O 24 CA CA O 701 1555 1555 3.16
LINK O THR O 26 CA CA O 701 1555 1555 2.19
LINK OD1 ASP O 93 CA CA O 802 1555 1555 3.08
LINK OD1 ASP O 95 CA CA O 802 1555 1555 2.26
LINK OD2 ASP O 95 CA CA O 802 1555 1555 3.09
LINK ND2 ASN O 97 CA CA O 802 1555 1555 2.37
LINK OD1 ASN O 97 CA CA O 802 1555 1555 2.27
LINK O TYR O 99 CA CA O 802 1555 1555 2.40
LINK OE1 GLU O 104 CA CA O 802 1555 1555 1.99
LINK OE2 GLU O 104 CA CA O 802 1555 1555 3.37
LINK OD2 ASP O 129 CA CA O 801 1555 1555 2.28
LINK OD1 ASP O 131 CA CA O 801 1555 1555 2.53
LINK OD1 ASP O 133 CA CA O 801 1555 1555 1.96
LINK O GLN O 135 CA CA O 801 1555 1555 2.11
LINK OE1 GLU O 140 CA CA O 801 1555 1555 2.02
LINK OD2 ASP P 20 CA CA P 703 1555 1555 2.58
LINK OD2 ASP P 22 CA CA P 703 1555 1555 2.58
LINK OD1 ASP P 22 CA CA P 703 1555 1555 2.38
LINK OD1 ASP P 24 CA CA P 703 1555 1555 2.29
LINK OD2 ASP P 24 CA CA P 703 1555 1555 3.06
LINK O THR P 26 CA CA P 703 1555 1555 2.12
LINK OD1 ASP P 93 CA CA P 804 1555 1555 2.98
LINK OD1 ASP P 95 CA CA P 804 1555 1555 2.21
LINK OD2 ASP P 95 CA CA P 804 1555 1555 3.11
LINK OD1 ASN P 97 CA CA P 804 1555 1555 2.32
LINK ND2 ASN P 97 CA CA P 804 1555 1555 2.32
LINK O TYR P 99 CA CA P 804 1555 1555 2.38
LINK OE1 GLU P 104 CA CA P 804 1555 1555 2.01
LINK OE2 GLU P 104 CA CA P 804 1555 1555 3.32
LINK OD2 ASP P 129 CA CA P 803 1555 1555 2.30
LINK OD1 ASP P 131 CA CA P 803 1555 1555 2.58
LINK OD1 ASP P 133 CA CA P 803 1555 1555 1.96
LINK O GLN P 135 CA CA P 803 1555 1555 2.07
LINK OE1 GLU P 140 CA CA P 803 1555 1555 2.04
LINK OD2 ASP Q 20 CA CA Q 705 1555 1555 2.48
LINK OD1 ASP Q 22 CA CA Q 705 1555 1555 2.36
LINK OD2 ASP Q 22 CA CA Q 705 1555 1555 2.61
LINK OD1 ASP Q 24 CA CA Q 705 1555 1555 2.28
LINK OD2 ASP Q 24 CA CA Q 705 1555 1555 3.10
LINK O THR Q 26 CA CA Q 705 1555 1555 2.13
LINK OD1 ASP Q 93 CA CA Q 806 1555 1555 2.72
LINK OD1 ASP Q 95 CA CA Q 806 1555 1555 2.19
LINK OD2 ASP Q 95 CA CA Q 806 1555 1555 3.22
LINK ND2 ASN Q 97 CA CA Q 806 1555 1555 2.26
LINK OD1 ASN Q 97 CA CA Q 806 1555 1555 2.50
LINK O TYR Q 99 CA CA Q 806 1555 1555 2.27
LINK OE2 GLU Q 104 CA CA Q 806 1555 1555 3.26
LINK OE1 GLU Q 104 CA CA Q 806 1555 1555 2.00
LINK OD2 ASP Q 129 CA CA Q 805 1555 1555 2.34
LINK OD1 ASP Q 131 CA CA Q 805 1555 1555 2.56
LINK OD1 ASP Q 133 CA CA Q 805 1555 1555 1.98
LINK O GLN Q 135 CA CA Q 805 1555 1555 2.11
LINK OE1 GLU Q 140 CA CA Q 805 1555 1555 1.98
LINK OD2 ASP R 20 CA CA R 707 1555 1555 2.55
LINK OD2 ASP R 22 CA CA R 707 1555 1555 2.50
LINK OD1 ASP R 22 CA CA R 707 1555 1555 2.33
LINK OD2 ASP R 24 CA CA R 707 1555 1555 3.01
LINK OD1 ASP R 24 CA CA R 707 1555 1555 2.26
LINK O THR R 26 CA CA R 707 1555 1555 2.19
LINK OD1 ASP R 93 CA CA R 808 1555 1555 3.01
LINK OD1 ASP R 95 CA CA R 808 1555 1555 2.17
LINK OD2 ASP R 95 CA CA R 808 1555 1555 3.05
LINK OD1 ASN R 97 CA CA R 808 1555 1555 2.30
LINK ND2 ASN R 97 CA CA R 808 1555 1555 2.36
LINK O TYR R 99 CA CA R 808 1555 1555 2.45
LINK OE1 GLU R 104 CA CA R 808 1555 1555 2.00
LINK OE2 GLU R 104 CA CA R 808 1555 1555 3.30
LINK OD2 ASP R 129 CA CA R 807 1555 1555 2.27
LINK OD1 ASP R 131 CA CA R 807 1555 1555 2.48
LINK OD1 ASP R 133 CA CA R 807 1555 1555 1.97
LINK O GLN R 135 CA CA R 807 1555 1555 2.16
LINK OE1 GLU R 140 CA CA R 807 1555 1555 2.00
LINK OD2 ASP S 20 CA CA S 709 1555 1555 2.43
LINK OD2 ASP S 22 CA CA S 709 1555 1555 2.67
LINK OD1 ASP S 22 CA CA S 709 1555 1555 2.44
LINK OD2 ASP S 24 CA CA S 709 1555 1555 3.08
LINK OD1 ASP S 24 CA CA S 709 1555 1555 2.20
LINK O THR S 26 CA CA S 709 1555 1555 2.08
LINK OD1 ASP S 93 CA CA S 810 1555 1555 3.20
LINK OD2 ASP S 95 CA CA S 810 1555 1555 3.16
LINK OD1 ASP S 95 CA CA S 810 1555 1555 2.39
LINK OD1 ASN S 97 CA CA S 810 1555 1555 2.23
LINK ND2 ASN S 97 CA CA S 810 1555 1555 2.43
LINK O TYR S 99 CA CA S 810 1555 1555 2.38
LINK OE1 GLU S 104 CA CA S 810 1555 1555 1.99
LINK OD2 ASP S 129 CA CA S 809 1555 1555 2.32
LINK OD1 ASP S 131 CA CA S 809 1555 1555 2.54
LINK OD1 ASP S 133 CA CA S 809 1555 1555 1.96
LINK O GLN S 135 CA CA S 809 1555 1555 2.13
LINK OE1 GLU S 140 CA CA S 809 1555 1555 2.01
LINK OD2 ASP T 20 CA CA T 711 1555 1555 2.42
LINK OD2 ASP T 22 CA CA T 711 1555 1555 2.61
LINK OD1 ASP T 22 CA CA T 711 1555 1555 2.37
LINK OD1 ASP T 24 CA CA T 711 1555 1555 2.21
LINK OD2 ASP T 24 CA CA T 711 1555 1555 3.06
LINK O THR T 26 CA CA T 711 1555 1555 2.15
LINK OD1 ASP T 93 CA CA T 812 1555 1555 3.11
LINK OD2 ASP T 95 CA CA T 812 1555 1555 3.06
LINK OD1 ASP T 95 CA CA T 812 1555 1555 2.23
LINK ND2 ASN T 97 CA CA T 812 1555 1555 2.38
LINK OD1 ASN T 97 CA CA T 812 1555 1555 2.23
LINK O TYR T 99 CA CA T 812 1555 1555 2.47
LINK OE2 GLU T 104 CA CA T 812 1555 1555 3.36
LINK OE1 GLU T 104 CA CA T 812 1555 1555 2.02
LINK OD2 ASP T 129 CA CA T 811 1555 1555 2.30
LINK OD1 ASP T 131 CA CA T 811 1555 1555 2.54
LINK OD1 ASP T 133 CA CA T 811 1555 1555 1.98
LINK O GLN T 135 CA CA T 811 1555 1555 2.11
LINK OE1 GLU T 140 CA CA T 811 1555 1555 2.01
SITE 1 AC1 5 LYS A 346 ASP A 491 ASP A 493 HIS A 577
SITE 2 AC1 5 CMP A 901
SITE 1 AC2 5 LYS B 346 ASP B 491 ASP B 493 HIS B 577
SITE 2 AC2 5 CMP B 902
SITE 1 AC3 5 LYS C 346 ASP C 491 ASP C 493 HIS C 577
SITE 2 AC3 5 CMP C 903
SITE 1 AC4 5 LYS D 346 ASP D 491 ASP D 493 HIS D 577
SITE 2 AC4 5 CMP D 904
SITE 1 AC5 5 LYS E 346 ASP E 491 ASP E 493 HIS E 577
SITE 2 AC5 5 CMP E 905
SITE 1 AC6 5 LYS F 346 ASP F 491 ASP F 493 HIS F 577
SITE 2 AC6 5 CMP F 906
SITE 1 AC7 4 ASP O 20 ASP O 22 ASP O 24 THR O 26
SITE 1 AC8 5 ASP O 129 ASP O 131 ASP O 133 GLN O 135
SITE 2 AC8 5 GLU O 140
SITE 1 AC9 5 ASP O 93 ASP O 95 ASN O 97 TYR O 99
SITE 2 AC9 5 GLU O 104
SITE 1 BC1 4 ASP P 20 ASP P 22 ASP P 24 THR P 26
SITE 1 BC2 5 ASP P 129 ASP P 131 ASP P 133 GLN P 135
SITE 2 BC2 5 GLU P 140
SITE 1 BC3 5 ASP P 93 ASP P 95 ASN P 97 TYR P 99
SITE 2 BC3 5 GLU P 104
SITE 1 BC4 4 ASP Q 20 ASP Q 22 ASP Q 24 THR Q 26
SITE 1 BC5 5 ASP Q 129 ASP Q 131 ASP Q 133 GLN Q 135
SITE 2 BC5 5 GLU Q 140
SITE 1 BC6 5 ASP Q 93 ASP Q 95 ASN Q 97 TYR Q 99
SITE 2 BC6 5 GLU Q 104
SITE 1 BC7 4 ASP R 20 ASP R 22 ASP R 24 THR R 26
SITE 1 BC8 5 ASP R 129 ASP R 131 ASP R 133 GLN R 135
SITE 2 BC8 5 GLU R 140
SITE 1 BC9 5 ASP R 93 ASP R 95 ASN R 97 TYR R 99
SITE 2 BC9 5 GLU R 104
SITE 1 CC1 4 ASP S 20 ASP S 22 ASP S 24 THR S 26
SITE 1 CC2 5 ASP S 129 ASP S 131 ASP S 133 GLN S 135
SITE 2 CC2 5 GLU S 140
SITE 1 CC3 5 ASP S 93 ASP S 95 ASN S 97 TYR S 99
SITE 2 CC3 5 GLU S 104
SITE 1 CC4 4 ASP T 20 ASP T 22 ASP T 24 THR T 26
SITE 1 CC5 5 ASP T 129 ASP T 131 ASP T 133 GLN T 135
SITE 2 CC5 5 GLU T 140
SITE 1 CC6 5 ASP T 93 ASP T 95 ASN T 97 TYR T 99
SITE 2 CC6 5 GLU T 104
SITE 1 CC7 9 ARG A 329 LEU A 348 GLY A 547 THR A 548
SITE 2 CC7 9 GLY A 578 THR A 579 GLU A 580 ASN A 583
SITE 3 CC7 9 MG A 900
SITE 1 CC8 9 ARG B 329 LEU B 348 GLY B 547 THR B 548
SITE 2 CC8 9 GLY B 578 THR B 579 GLU B 580 ASN B 583
SITE 3 CC8 9 MG B 901
SITE 1 CC9 9 ARG C 329 LEU C 348 GLY C 547 THR C 548
SITE 2 CC9 9 GLY C 578 THR C 579 GLU C 580 ASN C 583
SITE 3 CC9 9 MG C 902
SITE 1 DC1 9 ARG D 329 LEU D 348 GLY D 547 THR D 548
SITE 2 DC1 9 GLY D 578 THR D 579 GLU D 580 ASN D 583
SITE 3 DC1 9 MG D 903
SITE 1 DC2 9 ARG E 329 LEU E 348 GLY E 547 THR E 548
SITE 2 DC2 9 GLY E 578 THR E 579 GLU E 580 ASN E 583
SITE 3 DC2 9 MG E 904
SITE 1 DC3 9 ARG F 329 LEU F 348 GLY F 547 THR F 548
SITE 2 DC3 9 GLY F 578 THR F 579 GLU F 580 ASN F 583
SITE 3 DC3 9 MG F 905
CRYST1 320.501 185.044 142.454 90.00 90.22 90.00 C 1 2 1 24
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 0.003120 0.000000 0.000012 0.00000
SCALE2 0.000000 0.005404 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007020 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
