HEADER OXIDOREDUCTASE 27-JUL-00 1E5L
TITLE APO SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SACCHAROPINE REDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SACCHAROPNE DEHYDROGENASE (GLUTAMATE FORMING), ALPHA-
COMPND 5 AMINOADIPATE-DELTA-SEMIALDEHYDE-GLUTAMATE REDUCTASE;
COMPND 6 EC: 1.5.1.10;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MAGNAPORTHE GRISEA;
SOURCE 3 ORGANISM_COMMON: RICE BLAST FUNGUS;
SOURCE 4 ORGANISM_TAXID: 148305;
SOURCE 5 GENE: LYS3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: FM5/PDB45;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PDB45
KEYWDS OXIDOREDUCTASE, SACCHAROPINE REDUCTASE, LYSINE BIOSYNTHESIS, ALPHA-
KEYWDS 2 AMINOADIPATE PATHWAY
EXPDTA X-RAY DIFFRACTION
AUTHOR E.JOHANSSON,J.J.STEFFENS,Y.LINDQVIST,G.SCHNEIDER
REVDAT 5 13-DEC-23 1E5L 1 REMARK
REVDAT 4 17-JAN-18 1E5L 1 REMARK
REVDAT 3 24-FEB-09 1E5L 1 VERSN
REVDAT 2 18-JUL-03 1E5L 1 JRNL REMARK
REVDAT 1 27-NOV-00 1E5L 0
JRNL AUTH E.JOHANSSON,J.J.STEFFENS,Y.LINDQVIST,G.SCHNEIDER
JRNL TITL CRYSTAL STRUCTURE OF SACCHAROPINE REDUCTASE FROM MAGNAPORTHE
JRNL TITL 2 GRISEA, AN ENZYME OF THE ALPHA-AMINOADIPATE PATHWAY OF
JRNL TITL 3 LYSINE BIOSYNTHESIS
JRNL REF STRUCTURE V. 8 1037 2000
JRNL REFN ISSN 0969-2126
JRNL PMID 11080625
JRNL DOI 10.1016/S0969-2126(00)00512-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.JOHANSSON,J.J.STEFFENS,M.EMPTAGE,Y.LINDQVIST,G.SCHNEIDER
REMARK 1 TITL CLONING, EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF
REMARK 1 TITL 2 SACCHAROPINE REDUCTASE FROM MAGNAPORTHE GRISEA, AN ENZYME OF
REMARK 1 TITL 3 THE ALPHA-AMINOADIPATE PATHWAY OF LYSINE BIOSYNTHESIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 662 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 10771443
REMARK 1 DOI 10.1107/S0907444900003735
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : MAXIMUM LIKELIHOOD TARGET USING AMPLITUDES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2970901.790
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 39933
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) : 0.222
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1961
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5804
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 310
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6884
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 171
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.54000
REMARK 3 B22 (A**2) : -3.01000
REMARK 3 B33 (A**2) : -5.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MLF REFINEMENT TARGET
REMARK 4
REMARK 4 1E5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1290005196.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.104
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1FF9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8 MG/ML PROTEIN, 11-14 % (W/W)
REMARK 280 PEG6000, 0.1 M CITRIC ACID PH 4.0, 0.1 % BETA-OCTYLGLUCOSIDE, 1
REMARK 280 MM DTT, PH 4.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.97000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.97000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.66500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.66500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 97.97000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.66500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.50000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 97.97000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.66500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.50000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
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 B 332 C - N - CA ANGL. DEV. = 9.9 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 THR A 3 126.13 -35.03
REMARK 500 SER A 11 7.49 -151.76
REMARK 500 ALA A 44 108.07 -46.48
REMARK 500 ASP A 126 101.37 -160.81
REMARK 500 TRP A 174 -157.98 -151.55
REMARK 500 LEU A 183 6.49 -68.90
REMARK 500 ALA A 207 74.18 -69.03
REMARK 500 ILE A 212 -65.81 -137.21
REMARK 500 LEU A 272 32.19 -95.31
REMARK 500 ALA A 275 83.04 -57.69
REMARK 500 SER A 289 -94.98 -70.71
REMARK 500 ILE A 324 0.29 -65.17
REMARK 500 PRO A 332 113.47 -31.99
REMARK 500 GLU A 352 132.66 -26.80
REMARK 500 SER B 11 89.87 -157.25
REMARK 500 ASP B 59 -72.16 -46.74
REMARK 500 ASN B 121 -169.28 -122.74
REMARK 500 SER B 175 108.28 -48.83
REMARK 500 ALA B 182 8.32 -62.94
REMARK 500 VAL B 195 96.44 -69.53
REMARK 500 PRO B 201 17.44 -54.77
REMARK 500 GLU B 202 -6.80 -158.44
REMARK 500 ALA B 207 86.72 -67.59
REMARK 500 ILE B 212 -63.77 -133.50
REMARK 500 ALA B 275 64.92 -59.70
REMARK 500 PRO B 332 129.86 -38.61
REMARK 500 ARG B 333 28.34 -146.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DESCRIBED IN JOHANSSON ET AL.(2000) ACTA CRYST. D56 662-664
DBREF 1E5L A 1 450 PDB 1E5L 1E5L 1 450
DBREF 1E5L B 1 450 PDB 1E5L 1E5L 1 450
SEQRES 1 A 450 MET ALA THR LYS SER VAL LEU MET LEU GLY SER GLY PHE
SEQRES 2 A 450 VAL THR ARG PRO THR LEU ASP VAL LEU THR ASP SER GLY
SEQRES 3 A 450 ILE LYS VAL THR VAL ALA CYS ARG THR LEU GLU SER ALA
SEQRES 4 A 450 LYS LYS LEU SER ALA GLY VAL GLN HIS SER THR PRO ILE
SEQRES 5 A 450 SER LEU ASP VAL ASN ASP ASP ALA ALA LEU ASP ALA GLU
SEQRES 6 A 450 VAL ALA LYS HIS ASP LEU VAL ILE SER LEU ILE PRO TYR
SEQRES 7 A 450 THR PHE HIS ALA THR VAL ILE LYS SER ALA ILE ARG GLN
SEQRES 8 A 450 LYS LYS HIS VAL VAL THR THR SER TYR VAL SER PRO ALA
SEQRES 9 A 450 MET MET GLU LEU ASP GLN ALA ALA LYS ASP ALA GLY ILE
SEQRES 10 A 450 THR VAL MET ASN GLU ILE GLY LEU ASP PRO GLY ILE ASP
SEQRES 11 A 450 HIS LEU TYR ALA ILE LYS THR ILE GLU GLU VAL HIS ALA
SEQRES 12 A 450 ALA GLY GLY LYS ILE LYS THR PHE LEU SER TYR CYS GLY
SEQRES 13 A 450 GLY LEU PRO ALA PRO GLU SER SER ASP ASN PRO LEU GLY
SEQRES 14 A 450 TYR LYS PHE SER TRP SER SER ARG GLY VAL LEU LEU ALA
SEQRES 15 A 450 LEU ARG ASN ALA ALA SER PHE TYR LYS ASP GLY LYS VAL
SEQRES 16 A 450 THR ASN VAL ALA GLY PRO GLU LEU MET ALA THR ALA LYS
SEQRES 17 A 450 PRO TYR PHE ILE TYR PRO GLY PHE ALA PHE VAL ALA TYR
SEQRES 18 A 450 PRO ASN ARG ASP SER THR PRO TYR LYS GLU ARG TYR GLN
SEQRES 19 A 450 ILE PRO GLU ALA ASP ASN ILE VAL ARG GLY THR LEU ARG
SEQRES 20 A 450 TYR GLN GLY PHE PRO GLN PHE ILE LYS VAL LEU VAL ASP
SEQRES 21 A 450 ILE GLY PHE LEU SER ASP GLU GLU GLN PRO PHE LEU LYS
SEQRES 22 A 450 GLU ALA ILE PRO TRP LYS GLU ALA THR GLN LYS ILE VAL
SEQRES 23 A 450 LYS ALA SER SER ALA SER GLU GLN ASP ILE VAL SER THR
SEQRES 24 A 450 ILE VAL SER ASN ALA THR PHE GLU SER THR GLU GLU GLN
SEQRES 25 A 450 LYS ARG ILE VAL ALA GLY LEU LYS TRP LEU GLY ILE PHE
SEQRES 26 A 450 SER ASP LYS LYS ILE THR PRO ARG GLY ASN ALA LEU ASP
SEQRES 27 A 450 THR LEU CYS ALA THR LEU GLU GLU LYS MET GLN PHE GLU
SEQRES 28 A 450 GLU GLY GLU ARG ASP LEU VAL MET LEU GLN HIS LYS PHE
SEQRES 29 A 450 GLU ILE GLU ASN LYS ASP GLY SER ARG GLU THR ARG THR
SEQRES 30 A 450 SER SER LEU CYS GLU TYR GLY ALA PRO ILE GLY SER GLY
SEQRES 31 A 450 GLY TYR SER ALA MET ALA LYS LEU VAL GLY VAL PRO CYS
SEQRES 32 A 450 ALA VAL ALA VAL LYS PHE VAL LEU ASP GLY THR ILE SER
SEQRES 33 A 450 ASP ARG GLY VAL LEU ALA PRO MET ASN SER LYS ILE ASN
SEQRES 34 A 450 ASP PRO LEU MET LYS GLU LEU LYS GLU LYS TYR GLY ILE
SEQRES 35 A 450 GLU CYS LYS GLU LYS VAL VAL ALA
SEQRES 1 B 450 MET ALA THR LYS SER VAL LEU MET LEU GLY SER GLY PHE
SEQRES 2 B 450 VAL THR ARG PRO THR LEU ASP VAL LEU THR ASP SER GLY
SEQRES 3 B 450 ILE LYS VAL THR VAL ALA CYS ARG THR LEU GLU SER ALA
SEQRES 4 B 450 LYS LYS LEU SER ALA GLY VAL GLN HIS SER THR PRO ILE
SEQRES 5 B 450 SER LEU ASP VAL ASN ASP ASP ALA ALA LEU ASP ALA GLU
SEQRES 6 B 450 VAL ALA LYS HIS ASP LEU VAL ILE SER LEU ILE PRO TYR
SEQRES 7 B 450 THR PHE HIS ALA THR VAL ILE LYS SER ALA ILE ARG GLN
SEQRES 8 B 450 LYS LYS HIS VAL VAL THR THR SER TYR VAL SER PRO ALA
SEQRES 9 B 450 MET MET GLU LEU ASP GLN ALA ALA LYS ASP ALA GLY ILE
SEQRES 10 B 450 THR VAL MET ASN GLU ILE GLY LEU ASP PRO GLY ILE ASP
SEQRES 11 B 450 HIS LEU TYR ALA ILE LYS THR ILE GLU GLU VAL HIS ALA
SEQRES 12 B 450 ALA GLY GLY LYS ILE LYS THR PHE LEU SER TYR CYS GLY
SEQRES 13 B 450 GLY LEU PRO ALA PRO GLU SER SER ASP ASN PRO LEU GLY
SEQRES 14 B 450 TYR LYS PHE SER TRP SER SER ARG GLY VAL LEU LEU ALA
SEQRES 15 B 450 LEU ARG ASN ALA ALA SER PHE TYR LYS ASP GLY LYS VAL
SEQRES 16 B 450 THR ASN VAL ALA GLY PRO GLU LEU MET ALA THR ALA LYS
SEQRES 17 B 450 PRO TYR PHE ILE TYR PRO GLY PHE ALA PHE VAL ALA TYR
SEQRES 18 B 450 PRO ASN ARG ASP SER THR PRO TYR LYS GLU ARG TYR GLN
SEQRES 19 B 450 ILE PRO GLU ALA ASP ASN ILE VAL ARG GLY THR LEU ARG
SEQRES 20 B 450 TYR GLN GLY PHE PRO GLN PHE ILE LYS VAL LEU VAL ASP
SEQRES 21 B 450 ILE GLY PHE LEU SER ASP GLU GLU GLN PRO PHE LEU LYS
SEQRES 22 B 450 GLU ALA ILE PRO TRP LYS GLU ALA THR GLN LYS ILE VAL
SEQRES 23 B 450 LYS ALA SER SER ALA SER GLU GLN ASP ILE VAL SER THR
SEQRES 24 B 450 ILE VAL SER ASN ALA THR PHE GLU SER THR GLU GLU GLN
SEQRES 25 B 450 LYS ARG ILE VAL ALA GLY LEU LYS TRP LEU GLY ILE PHE
SEQRES 26 B 450 SER ASP LYS LYS ILE THR PRO ARG GLY ASN ALA LEU ASP
SEQRES 27 B 450 THR LEU CYS ALA THR LEU GLU GLU LYS MET GLN PHE GLU
SEQRES 28 B 450 GLU GLY GLU ARG ASP LEU VAL MET LEU GLN HIS LYS PHE
SEQRES 29 B 450 GLU ILE GLU ASN LYS ASP GLY SER ARG GLU THR ARG THR
SEQRES 30 B 450 SER SER LEU CYS GLU TYR GLY ALA PRO ILE GLY SER GLY
SEQRES 31 B 450 GLY TYR SER ALA MET ALA LYS LEU VAL GLY VAL PRO CYS
SEQRES 32 B 450 ALA VAL ALA VAL LYS PHE VAL LEU ASP GLY THR ILE SER
SEQRES 33 B 450 ASP ARG GLY VAL LEU ALA PRO MET ASN SER LYS ILE ASN
SEQRES 34 B 450 ASP PRO LEU MET LYS GLU LEU LYS GLU LYS TYR GLY ILE
SEQRES 35 B 450 GLU CYS LYS GLU LYS VAL VAL ALA
FORMUL 3 HOH *171(H2 O)
HELIX 1 1 VAL A 14 SER A 25 1 12
HELIX 2 2 THR A 35 ALA A 44 1 10
HELIX 3 3 ASP A 58 LYS A 68 1 11
HELIX 4 4 PRO A 77 THR A 79 5 3
HELIX 5 5 PHE A 80 GLN A 91 1 12
HELIX 6 6 SER A 102 LEU A 108 1 7
HELIX 7 7 LEU A 108 ALA A 115 1 8
HELIX 8 8 GLY A 128 GLY A 145 1 18
HELIX 9 9 PRO A 161 SER A 164 5 4
HELIX 10 10 LEU A 181 ASN A 185 5 5
HELIX 11 11 ALA A 199 LEU A 203 5 5
HELIX 12 12 LEU A 203 ALA A 207 5 5
HELIX 13 13 PRO A 228 TYR A 233 1 6
HELIX 14 14 GLY A 250 ILE A 261 1 12
HELIX 15 15 PRO A 270 GLU A 274 5 5
HELIX 16 16 PRO A 277 LYS A 287 1 11
HELIX 17 17 SER A 292 ALA A 304 1 13
HELIX 18 18 SER A 308 GLY A 323 1 16
HELIX 19 19 ASN A 335 MET A 348 1 14
HELIX 20 20 SER A 393 ASP A 412 1 20
HELIX 21 21 ASN A 425 LYS A 439 1 15
HELIX 22 22 SER B 11 PHE B 13 5 3
HELIX 23 23 VAL B 14 SER B 25 1 12
HELIX 24 24 THR B 35 LEU B 42 1 8
HELIX 25 25 ASP B 58 ALA B 67 1 10
HELIX 26 26 ALA B 82 GLN B 91 1 10
HELIX 27 27 SER B 102 LEU B 108 1 7
HELIX 28 28 LEU B 108 ALA B 115 1 8
HELIX 29 29 GLY B 128 ALA B 144 1 17
HELIX 30 30 PRO B 161 SER B 164 5 4
HELIX 31 31 SER B 175 ALA B 182 1 8
HELIX 32 32 ALA B 199 PRO B 201 5 3
HELIX 33 33 GLU B 202 ALA B 207 1 6
HELIX 34 34 PRO B 228 TYR B 233 1 6
HELIX 35 35 GLY B 250 ILE B 261 1 12
HELIX 36 36 GLN B 269 LYS B 273 5 5
HELIX 37 37 PRO B 277 LYS B 287 1 11
HELIX 38 38 SER B 292 ALA B 304 1 13
HELIX 39 39 SER B 308 GLY B 323 1 16
HELIX 40 40 ASN B 335 MET B 348 1 14
HELIX 41 41 SER B 393 ASP B 412 1 20
HELIX 42 42 ASN B 425 GLY B 441 1 17
SHEET 1 A 5 HIS A 94 THR A 97 0
SHEET 2 A 5 LEU A 71 SER A 74 1 N VAL A 72 O HIS A 94
SHEET 3 A 5 SER A 5 LEU A 9 1 N LEU A 7 O LEU A 71
SHEET 4 A 5 LYS A 28 CYS A 33 1 N LYS A 28 O VAL A 6
SHEET 5 A 5 SER A 49 SER A 53 1 N THR A 50 O VAL A 29
SHEET 1 B 2 THR A 118 MET A 120 0
SHEET 2 B 2 GLY A 419 LEU A 421 1 N GLY A 419 O VAL A 119
SHEET 1 C 6 PHE A 218 PRO A 222 0
SHEET 2 C 6 ASN A 240 TYR A 248 -1 N ARG A 247 O VAL A 219
SHEET 3 C 6 LYS A 147 PRO A 159 1 N PHE A 151 O ASN A 240
SHEET 4 C 6 ASP A 356 GLU A 367 -1 N GLU A 367 O LYS A 147
SHEET 5 C 6 ARG A 373 TYR A 383 -1 N GLU A 382 O VAL A 358
SHEET 6 C 6 LYS A 445 VAL A 448 -1 N LYS A 447 O THR A 377
SHEET 1 D 2 ALA A 187 LYS A 191 0
SHEET 2 D 2 LYS A 194 VAL A 198 -1 N VAL A 198 O ALA A 187
SHEET 1 E 4 LYS B 28 ALA B 32 0
SHEET 2 E 4 SER B 5 LEU B 9 1 N VAL B 6 O LYS B 28
SHEET 3 E 4 LEU B 71 SER B 74 1 N LEU B 71 O LEU B 7
SHEET 4 E 4 HIS B 94 THR B 97 1 N HIS B 94 O VAL B 72
SHEET 1 F 2 THR B 118 MET B 120 0
SHEET 2 F 2 GLY B 419 LEU B 421 1 N GLY B 419 O VAL B 119
SHEET 1 G 6 PHE B 218 PRO B 222 0
SHEET 2 G 6 ASN B 240 TYR B 248 -1 N ARG B 247 O VAL B 219
SHEET 3 G 6 LYS B 147 PRO B 159 1 N PHE B 151 O ASN B 240
SHEET 4 G 6 ASP B 356 GLU B 367 -1 N GLU B 367 O LYS B 147
SHEET 5 G 6 ARG B 373 TYR B 383 -1 N GLU B 382 O VAL B 358
SHEET 6 G 6 LYS B 445 VAL B 449 -1 N VAL B 449 O THR B 375
SHEET 1 H 2 ALA B 187 LYS B 191 0
SHEET 2 H 2 LYS B 194 VAL B 198 -1 N VAL B 198 O ALA B 187
CISPEP 1 ASP A 126 PRO A 127 0 0.45
CISPEP 2 ASP B 126 PRO B 127 0 0.36
CRYST1 89.330 119.000 195.940 90.00 90.00 90.00 C 2 2 21 16
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 0.011194 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005104 0.00000
MTRIX1 1 -0.562430 0.351270 0.748520 8.62276 1
MTRIX2 1 0.337690 -0.728750 0.595730 -27.46522 1
MTRIX3 1 0.754740 0.587830 0.291250 34.30939 1
(ATOM LINES ARE NOT SHOWN.)
END
