HEADER LYASE 06-APR-05 1ZAH
TITLE FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MUSCLE-TYPE ALDOLASE;
COMPND 5 EC: 4.1.2.13;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 GENE: ALDOA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-SI (INVITROGEN);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPB14
KEYWDS ALDOLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ST-JEAN,J.LAFRANCE-VANASSE,B.LIOTARD,J.SYGUSCH
REVDAT 5 23-AUG-23 1ZAH 1 REMARK
REVDAT 4 11-OCT-17 1ZAH 1 REMARK
REVDAT 3 24-FEB-09 1ZAH 1 VERSN
REVDAT 2 02-AUG-05 1ZAH 1 JRNL
REVDAT 1 10-MAY-05 1ZAH 0
JRNL AUTH M.ST-JEAN,J.LAFRANCE-VANASSE,B.LIOTARD,J.SYGUSCH
JRNL TITL HIGH RESOLUTION REACTION INTERMEDIATES OF RABBIT MUSCLE
JRNL TITL 2 FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE: SUBSTRATE CLEAVAGE AND
JRNL TITL 3 INDUCED FIT.
JRNL REF J.BIOL.CHEM. V. 280 27262 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15870069
JRNL DOI 10.1074/JBC.M502413200
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 118090
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) : 0.167
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 5925
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11032
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 2427
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.69800
REMARK 3 B22 (A**2) : -8.98400
REMARK 3 B33 (A**2) : 6.28600
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.25800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.267
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.218 ; 0.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.839 ; 0.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.834 ; 0.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.620 ; 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 71.67
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032499.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127047
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.38800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1ADO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM HEPES, PEG 4000, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 51.45800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE HOMOTETRAMER FOUND IN THE
REMARK 300 ASYMMETRIC UNIT
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 600 O HOH D 757 2.17
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 PRO A 344 C - N - CA ANGL. DEV. = 12.9 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 PRO A 5 115.61 -23.06
REMARK 500 PRO A 25 125.33 -39.25
REMARK 500 ASP A 67 -7.93 -50.12
REMARK 500 THR A 259 -30.75 -138.55
REMARK 500 THR A 298 -159.03 -130.90
REMARK 500 CYS A 338 6.29 -69.38
REMARK 500 PRO A 344 -61.38 -20.43
REMARK 500 SER A 345 -76.56 -103.01
REMARK 500 ALA A 348 -61.78 -106.18
REMARK 500 ALA A 350 79.40 74.31
REMARK 500 ALA A 351 122.68 -176.14
REMARK 500 ALA A 352 68.68 -173.07
REMARK 500 GLU A 354 140.83 178.64
REMARK 500 ILE A 358 -75.55 -133.95
REMARK 500 PRO B 5 115.18 -25.39
REMARK 500 PRO B 290 38.99 -69.67
REMARK 500 THR B 298 -159.00 -129.65
REMARK 500 SER B 345 -70.90 -61.79
REMARK 500 GLN B 347 -75.65 -111.49
REMARK 500 ALA B 350 -14.27 -142.57
REMARK 500 GLU B 354 -125.70 -84.97
REMARK 500 PHE B 357 72.65 -114.27
REMARK 500 ILE B 358 -153.06 -88.48
REMARK 500 PRO C 5 114.10 -25.25
REMARK 500 ASP C 67 -6.05 -55.10
REMARK 500 PRO C 188 76.21 -103.39
REMARK 500 PRO C 290 4.14 -65.04
REMARK 500 ALA C 304 -9.62 -59.44
REMARK 500 SER C 345 55.58 -104.74
REMARK 500 ALA C 348 35.00 -160.06
REMARK 500 ALA C 350 -57.10 -159.86
REMARK 500 SER C 353 97.22 58.41
REMARK 500 GLU C 354 -82.94 -118.43
REMARK 500 LEU C 356 -15.06 -161.91
REMARK 500 PRO D 5 116.93 -27.31
REMARK 500 ASP D 67 -8.00 -51.60
REMARK 500 PRO D 290 -2.76 -58.14
REMARK 500 THR D 298 -155.76 -131.77
REMARK 500 SER D 345 147.66 167.46
REMARK 500 GLN D 347 158.78 -48.28
REMARK 500 ALA D 348 89.22 66.06
REMARK 500 ALA D 362 -56.71 -165.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 213 0.07 SIDE CHAIN
REMARK 500 TYR B 213 0.07 SIDE CHAIN
REMARK 500 TYR D 213 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZAI RELATED DB: PDB
REMARK 900 RELATED ID: 1ZAJ RELATED DB: PDB
REMARK 900 RELATED ID: 1ZAL RELATED DB: PDB
DBREF 1ZAH A 1 363 UNP P00883 ALDOA_RABIT 1 363
DBREF 1ZAH B 1 363 UNP P00883 ALDOA_RABIT 1 363
DBREF 1ZAH C 1 363 UNP P00883 ALDOA_RABIT 1 363
DBREF 1ZAH D 1 363 UNP P00883 ALDOA_RABIT 1 363
SEQRES 1 A 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 A 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 A 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 A 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 A 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 A 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 A 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 A 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 A 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 A 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 A 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 A 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 A 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 A 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 A 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 A 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 A 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 A 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 A 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 A 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 A 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 A 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 A 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 A 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 A 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 A 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 A 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 A 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
SEQRES 1 B 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 B 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 B 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 B 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 B 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 B 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 B 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 B 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 B 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 B 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 B 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 B 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 B 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 B 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 B 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 B 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 B 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 B 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 B 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 B 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 B 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 B 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 B 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 B 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 B 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 B 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 B 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 B 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
SEQRES 1 C 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 C 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 C 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 C 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 C 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 C 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 C 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 C 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 C 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 C 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 C 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 C 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 C 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 C 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 C 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 C 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 C 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 C 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 C 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 C 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 C 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 C 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 C 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 C 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 C 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 C 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 C 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 C 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
SEQRES 1 D 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 D 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 D 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 D 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 D 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 D 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 D 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 D 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 D 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 D 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 D 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 D 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 D 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 D 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 D 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 D 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 D 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 D 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 D 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 D 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 D 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 D 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 D 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 D 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 D 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 D 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 D 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 D 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
FORMUL 5 HOH *2427(H2 O)
HELIX 1 1 THR A 8 VAL A 23 1 16
HELIX 2 2 SER A 35 SER A 45 1 11
HELIX 3 3 THR A 51 THR A 64 1 14
HELIX 4 4 ASP A 66 ASN A 70 5 5
HELIX 5 5 PHE A 79 TYR A 84 1 6
HELIX 6 6 PRO A 92 LYS A 100 1 9
HELIX 7 7 GLY A 129 ASP A 140 1 12
HELIX 8 8 SER A 159 ASN A 180 1 22
HELIX 9 9 ASP A 197 HIS A 219 1 23
HELIX 10 10 TYR A 222 THR A 226 5 5
HELIX 11 11 SER A 244 ARG A 258 1 15
HELIX 12 12 SER A 275 CYS A 289 1 15
HELIX 13 13 GLY A 302 GLY A 314 1 13
HELIX 14 14 LYS A 316 GLU A 318 5 3
HELIX 15 15 ASN A 319 CYS A 338 1 20
HELIX 16 16 THR B 8 VAL B 23 1 16
HELIX 17 17 SER B 35 SER B 45 1 11
HELIX 18 18 THR B 51 THR B 64 1 14
HELIX 19 19 ASP B 66 ASN B 70 5 5
HELIX 20 20 PHE B 79 TYR B 84 1 6
HELIX 21 21 PRO B 92 LYS B 100 1 9
HELIX 22 22 GLY B 129 ASP B 140 1 12
HELIX 23 23 SER B 159 ASN B 180 1 22
HELIX 24 24 ASP B 197 HIS B 219 1 23
HELIX 25 25 TYR B 222 GLY B 225 5 4
HELIX 26 26 SER B 244 ARG B 258 1 15
HELIX 27 27 SER B 275 CYS B 289 1 15
HELIX 28 28 GLY B 302 GLY B 314 1 13
HELIX 29 29 LYS B 316 GLU B 318 5 3
HELIX 30 30 ASN B 319 CYS B 338 1 20
HELIX 31 31 SER B 359 TYR B 363 5 5
HELIX 32 32 THR C 8 VAL C 23 1 16
HELIX 33 33 SER C 35 SER C 45 1 11
HELIX 34 34 THR C 51 THR C 64 1 14
HELIX 35 35 ASP C 66 ASN C 70 5 5
HELIX 36 36 PHE C 79 TYR C 84 1 6
HELIX 37 37 PRO C 92 LYS C 100 1 9
HELIX 38 38 GLY C 129 ASP C 140 1 12
HELIX 39 39 SER C 159 ASN C 180 1 22
HELIX 40 40 ASP C 197 HIS C 219 1 23
HELIX 41 41 TYR C 222 GLY C 225 5 4
HELIX 42 42 SER C 244 ARG C 258 1 15
HELIX 43 43 SER C 275 CYS C 289 1 15
HELIX 44 44 GLY C 302 GLY C 314 1 13
HELIX 45 45 LYS C 316 GLU C 318 5 3
HELIX 46 46 ASN C 319 CYS C 338 1 20
HELIX 47 47 SER C 359 TYR C 363 5 5
HELIX 48 48 THR D 8 VAL D 23 1 16
HELIX 49 49 SER D 35 SER D 45 1 11
HELIX 50 50 THR D 51 THR D 64 1 14
HELIX 51 51 ASP D 66 ASN D 70 5 5
HELIX 52 52 PHE D 79 TYR D 84 1 6
HELIX 53 53 PRO D 92 LYS D 100 1 9
HELIX 54 54 GLY D 129 ASP D 140 1 12
HELIX 55 55 SER D 159 ASN D 180 1 22
HELIX 56 56 ASP D 197 HIS D 219 1 23
HELIX 57 57 TYR D 222 GLY D 225 5 4
HELIX 58 58 SER D 244 ARG D 258 1 15
HELIX 59 59 SER D 275 CYS D 289 1 15
HELIX 60 60 GLY D 302 GLY D 314 1 13
HELIX 61 61 LYS D 316 GLU D 318 5 3
HELIX 62 62 ASN D 319 CYS D 338 1 20
HELIX 63 63 GLY D 349 SER D 353 5 5
SHEET 1 A 9 GLY A 28 ALA A 32 0
SHEET 2 A 9 ILE A 73 LEU A 78 1 O ILE A 77 N LEU A 30
SHEET 3 A 9 VAL A 103 LYS A 107 1 O GLY A 105 N VAL A 76
SHEET 4 A 9 PHE A 144 LEU A 151 1 O PHE A 144 N ILE A 106
SHEET 5 A 9 VAL A 183 ILE A 190 1 O GLU A 189 N LEU A 151
SHEET 6 A 9 LEU A 227 LEU A 228 1 O LEU A 227 N VAL A 186
SHEET 7 A 9 GLY A 266 PHE A 269 1 O THR A 268 N LEU A 228
SHEET 8 A 9 ALA A 296 TYR A 301 1 O THR A 298 N VAL A 267
SHEET 9 A 9 GLY A 28 ALA A 32 1 N ILE A 29 O PHE A 299
SHEET 1 B 2 VAL A 112 PRO A 114 0
SHEET 2 B 2 THR A 122 THR A 124 -1 O THR A 123 N VAL A 113
SHEET 1 C 9 GLY B 28 ALA B 32 0
SHEET 2 C 9 ILE B 73 LEU B 78 1 O ILE B 77 N LEU B 30
SHEET 3 C 9 VAL B 103 LYS B 107 1 O GLY B 105 N VAL B 76
SHEET 4 C 9 PHE B 144 LEU B 151 1 O PHE B 144 N ILE B 106
SHEET 5 C 9 VAL B 183 ILE B 190 1 O GLU B 187 N CYS B 149
SHEET 6 C 9 LEU B 227 LEU B 228 1 O LEU B 227 N VAL B 186
SHEET 7 C 9 GLY B 266 PHE B 269 1 O THR B 268 N LEU B 228
SHEET 8 C 9 ALA B 296 TYR B 301 1 O THR B 298 N VAL B 267
SHEET 9 C 9 GLY B 28 ALA B 32 1 N ILE B 29 O PHE B 299
SHEET 1 D 2 VAL B 112 PRO B 114 0
SHEET 2 D 2 THR B 122 THR B 124 -1 O THR B 123 N VAL B 113
SHEET 1 E 9 GLY C 28 ALA C 32 0
SHEET 2 E 9 ILE C 73 LEU C 78 1 O ILE C 77 N LEU C 30
SHEET 3 E 9 VAL C 103 LYS C 107 1 O GLY C 105 N VAL C 76
SHEET 4 E 9 PHE C 144 LEU C 151 1 O LYS C 146 N ILE C 106
SHEET 5 E 9 VAL C 183 ILE C 190 1 O GLU C 187 N CYS C 149
SHEET 6 E 9 LEU C 227 LEU C 228 1 O LEU C 227 N VAL C 186
SHEET 7 E 9 GLY C 266 PHE C 269 1 O THR C 268 N LEU C 228
SHEET 8 E 9 ALA C 296 TYR C 301 1 O THR C 298 N VAL C 267
SHEET 9 E 9 GLY C 28 ALA C 32 1 N ILE C 29 O PHE C 299
SHEET 1 F 2 VAL C 112 PRO C 114 0
SHEET 2 F 2 THR C 122 THR C 124 -1 O THR C 123 N VAL C 113
SHEET 1 G 9 GLY D 28 ALA D 32 0
SHEET 2 G 9 ILE D 73 LEU D 78 1 O GLY D 74 N GLY D 28
SHEET 3 G 9 VAL D 103 LYS D 107 1 O GLY D 105 N VAL D 76
SHEET 4 G 9 PHE D 144 LEU D 151 1 O PHE D 144 N ILE D 106
SHEET 5 G 9 VAL D 183 ILE D 190 1 O GLU D 189 N LEU D 151
SHEET 6 G 9 LEU D 227 LEU D 228 1 O LEU D 227 N VAL D 186
SHEET 7 G 9 GLY D 266 PHE D 269 1 O THR D 268 N LEU D 228
SHEET 8 G 9 ALA D 296 TYR D 301 1 O ALA D 296 N VAL D 267
SHEET 9 G 9 GLY D 28 ALA D 32 1 N ALA D 31 O TYR D 301
SHEET 1 H 2 VAL D 112 PRO D 114 0
SHEET 2 H 2 THR D 122 THR D 124 -1 O THR D 123 N VAL D 113
CISPEP 1 THR A 157 PRO A 158 0 -0.47
CISPEP 2 THR B 157 PRO B 158 0 -0.47
CISPEP 3 THR C 157 PRO C 158 0 -0.02
CISPEP 4 THR D 157 PRO D 158 0 -0.06
CRYST1 83.096 102.916 84.663 90.00 98.36 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012030 0.000000 0.001770 0.00000
SCALE2 0.000000 0.009720 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011940 0.00000
(ATOM LINES ARE NOT SHOWN.)
END