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HEADER TRANSPORT PROTEIN 16-SEP-05 2B20
TITLE CRYSTAL STRUCTURE OF ENTEROCHELIN ESTERASE FROM SHIGELLA
TITLE 2 FLEXNERI ENTEROCHELIN ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROCHELIN ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI 2A STR. 2457T;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS ALPHA-BETA-ALPHA-SANDWICH, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,N.MALTSEVA,I.DEMENTIEVA,P.QUARTEY,D.HOLZLE,F.COLLART,
AUTHOR 2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 01-NOV-05 2B20 0
JRNL AUTH Y.KIM,N.MALTSEVA,I.DEMENTIEVA,P.QUARTEY,D.HOLZLE,
JRNL AUTH 2 F.COLLART,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF ENTEROCHELIN ESTERASE FROM
JRNL TITL 2 SHIGELLA FLEXNERI ENTEROCHELIN ESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS,REFMAC 5.2.0005
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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.11
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) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 11946
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 : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 611
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.67
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 841
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 47
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 : 3218
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : -0.91000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : 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 : MASK
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2B20 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-2005.
REMARK 100 THE RCSB ID CODE IS RCSB034576.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC Q315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SBCCOLLECT
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12690
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 20.600
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 16.60
REMARK 200 R MERGE FOR SHELL (I) : 0.96900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL2000_PH, SHELX,SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM/SODIUM TARTRATE, CHES,
REMARK 280 LITIUM SULFATE, PH 9.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,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 126.06250
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.08650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.08650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 189.09375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.08650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.08650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 63.03125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.08650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.08650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 189.09375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.08650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.08650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 63.03125
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 126.06250
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 ASN A 62
REMARK 465 SER A 63
REMARK 465 ALA A 191
REMARK 465 GLU A 192
REMARK 465 ASP A 398
REMARK 465 ARG A 399
REMARK 465 SER A 400
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
REMARK 500 N ILE A 235 O HOH 16 1.95
REMARK 500 NH2 ARG A 369 OD1 ASP A 390 2.02
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 HIS A 60 N - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP A 188 N - CA - C ANGL. DEV. = 10.3 DEGREES
REMARK 500 ALA A 234 N - CA - C ANGL. DEV. =-11.7 DEGREES
REMARK 500 LEU A 335 CA - CB - CG ANGL. DEV. = 10.7 DEGREES
REMARK 500 GLU A 345 N - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 PRO A 346 N - CA - C ANGL. DEV. = -9.1 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 281 -116.05 41.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 345 PRO A 346 -78.51
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC27316 RELATED DB: TARGETDB
DBREF 2B20 A 1 400 GB 30040286 AAP16019 1 400
SEQADV 2B20 SER A -2 GB 30040286 CLONING ARTIFACT
SEQADV 2B20 ASN A -1 GB 30040286 CLONING ARTIFACT
SEQADV 2B20 ALA A 0 GB 30040286 CLONING ARTIFACT
SEQADV 2B20 MSE A 1 GB 30040286 MET 1 MODIFIED RESIDUE
SEQADV 2B20 MSE A 27 GB 30040286 MET 27 MODIFIED RESIDUE
SEQADV 2B20 MSE A 68 GB 30040286 MET 68 MODIFIED RESIDUE
SEQADV 2B20 MSE A 146 GB 30040286 MET 146 MODIFIED RESIDUE
SEQADV 2B20 MSE A 209 GB 30040286 MET 209 MODIFIED RESIDUE
SEQADV 2B20 MSE A 347 GB 30040286 MET 347 MODIFIED RESIDUE
SEQADV 2B20 MSE A 349 GB 30040286 MET 349 MODIFIED RESIDUE
SEQADV 2B20 MSE A 385 GB 30040286 MET 385 MODIFIED RESIDUE
SEQRES 1 A 403 SER ASN ALA MSE THR ALA LEU LYS VAL GLY SER GLU SER
SEQRES 2 A 403 TRP TRP GLN SER LYS HIS GLY PRO GLU TRP GLN ARG LEU
SEQRES 3 A 403 ASN ASP GLU MSE PHE GLU VAL THR PHE TRP TRP ARG ASP
SEQRES 4 A 403 PRO GLN GLY SER GLU GLU TYR SER THR ILE LYS ARG VAL
SEQRES 5 A 403 TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN ASN
SEQRES 6 A 403 SER GLN PRO GLN SER MSE GLN ARG ILE ALA GLY THR ASP
SEQRES 7 A 403 VAL TRP GLN TRP THR THR GLN LEU ASN ALA ASN TRP ARG
SEQRES 8 A 403 GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP ILE
SEQRES 9 A 403 PHE SER ALA PRO SER PRO ASP ARG LEU GLU LEU ARG GLU
SEQRES 10 A 403 GLY TRP ARG LYS LEU LEU PRO GLN ALA ILE ALA ASP PRO
SEQRES 11 A 403 LEU ASN PRO GLN SER TRP LYS GLY GLY LEU GLY HIS ALA
SEQRES 12 A 403 VAL SER ALA LEU GLU MSE PRO GLN ALA PRO LEU GLN PRO
SEQRES 13 A 403 GLY TRP ASP CYS PRO GLN ALA PRO GLU ILE PRO ALA LYS
SEQRES 14 A 403 GLU ILE ILE TRP LYS SER GLU ARG LEU LYS ASN SER ARG
SEQRES 15 A 403 ARG VAL TRP ILE PHE THR THR GLY ASP VAL THR ALA GLU
SEQRES 16 A 403 GLU ARG PRO LEU ALA VAL LEU LEU ASP GLY GLU PHE TRP
SEQRES 17 A 403 ALA GLN SER MSE PRO VAL TRP PRO VAL LEU THR SER LEU
SEQRES 18 A 403 THR HIS ARG GLN GLN LEU PRO PRO ALA VAL TYR VAL LEU
SEQRES 19 A 403 ILE ASP ALA ILE ASP THR THR HIS ARG ALA HIS GLU LEU
SEQRES 20 A 403 PRO CYS ASN ALA ASP PHE TRP LEU ALA VAL GLN GLN GLU
SEQRES 21 A 403 LEU LEU PRO LEU VAL LYS VAL ILE ALA PRO PHE SER ASP
SEQRES 22 A 403 ARG ALA ASP ARG THR VAL VAL ALA GLY GLN SER PHE GLY
SEQRES 23 A 403 GLY LEU SER ALA LEU TYR ALA GLY LEU HIS TRP PRO GLU
SEQRES 24 A 403 ARG PHE GLY CYS VAL LEU SER GLN SER GLY SER TYR TRP
SEQRES 25 A 403 TRP PRO HIS ARG GLY GLY GLN GLN GLU GLY VAL LEU LEU
SEQRES 26 A 403 GLU LYS LEU LYS ALA GLY GLU VAL SER ALA GLU GLY LEU
SEQRES 27 A 403 ARG ILE VAL LEU GLU ALA GLY ILE ARG GLU PRO MSE ILE
SEQRES 28 A 403 MSE ARG ALA ASN GLN ALA LEU TYR ALA GLN LEU HIS PRO
SEQRES 29 A 403 ILE LYS GLU SER ILE PHE TRP ARG GLN VAL ASP GLY GLY
SEQRES 30 A 403 HIS ASP ALA LEU CYS TRP ARG GLY GLY LEU MSE GLN GLY
SEQRES 31 A 403 LEU ILE ASP LEU TRP GLN PRO LEU PHE HIS ASP ARG SER
MODRES 2B20 MSE A 27 MET SELENOMETHIONINE
MODRES 2B20 MSE A 68 MET SELENOMETHIONINE
MODRES 2B20 MSE A 146 MET SELENOMETHIONINE
MODRES 2B20 MSE A 209 MET SELENOMETHIONINE
MODRES 2B20 MSE A 347 MET SELENOMETHIONINE
MODRES 2B20 MSE A 349 MET SELENOMETHIONINE
MODRES 2B20 MSE A 385 MET SELENOMETHIONINE
HET MSE A 27 8
HET MSE A 68 8
HET MSE A 146 8
HET MSE A 209 8
HET MSE A 347 8
HET MSE A 349 8
HET MSE A 385 8
HET TAR 501 10
HETNAM MSE SELENOMETHIONINE
HETNAM TAR D(-)-TARTARIC ACID
FORMUL 1 MSE 7(C5 H11 N1 O2 SE1)
FORMUL 2 TAR C4 H6 O6
FORMUL 3 HOH *50(H2 O1)
HELIX 1 1 SER A 8 SER A 14 1 7
HELIX 2 2 VAL A 56 HIS A 60 5 5
HELIX 3 3 ASP A 108 LEU A 120 1 13
HELIX 4 4 PRO A 121 ALA A 123 5 3
HELIX 5 5 ASP A 201 SER A 208 1 8
HELIX 6 6 VAL A 211 ARG A 221 1 11
HELIX 7 7 ASP A 236 LEU A 244 1 9
HELIX 8 8 ASN A 247 GLU A 257 1 11
HELIX 9 9 GLU A 257 ALA A 266 1 10
HELIX 10 10 ARG A 271 ARG A 274 5 4
HELIX 11 11 SER A 281 TRP A 294 1 14
HELIX 12 12 LEU A 321 ALA A 327 1 7
HELIX 13 13 PRO A 346 GLN A 358 1 13
HELIX 14 14 LEU A 359 HIS A 360 5 2
HELIX 15 15 PRO A 361 GLU A 364 5 4
HELIX 16 16 ASP A 376 TRP A 392 1 17
HELIX 17 17 GLN A 393 PHE A 396 5 4
SHEET 1 A 4 GLU A 19 ARG A 22 0
SHEET 2 A 4 MSE A 27 ARG A 35 -1 O GLU A 29 N GLN A 21
SHEET 3 A 4 VAL A 76 ASN A 84 -1 O TRP A 79 N PHE A 32
SHEET 4 A 4 GLN A 69 ARG A 70 -1 N GLN A 69 O GLN A 78
SHEET 1 B 4 ARG A 48 ILE A 53 0
SHEET 2 B 4 ARG A 88 THR A 96 -1 O THR A 96 N ARG A 48
SHEET 3 B 4 ALA A 140 GLU A 145 -1 O SER A 142 N TYR A 91
SHEET 4 B 4 SER A 132 LYS A 134 -1 N TRP A 133 O VAL A 141
SHEET 1 C 8 LYS A 166 SER A 172 0
SHEET 2 C 8 ASN A 177 THR A 185 -1 O VAL A 181 N ILE A 168
SHEET 3 C 8 VAL A 228 ILE A 232 -1 O TYR A 229 N PHE A 184
SHEET 4 C 8 LEU A 196 LEU A 200 1 N ALA A 197 O VAL A 230
SHEET 5 C 8 VAL A 276 GLN A 280 1 O ALA A 278 N VAL A 198
SHEET 6 C 8 CYS A 300 GLN A 304 1 O CYS A 300 N VAL A 277
SHEET 7 C 8 ARG A 336 GLY A 342 1 O VAL A 338 N VAL A 301
SHEET 8 C 8 ILE A 366 VAL A 371 1 O PHE A 367 N LEU A 339
CISPEP 1 SER A 106 PRO A 107 0 -28.74
CISPEP 2 TRP A 310 PRO A 311 0 -1.81
CRYST1 66.173 66.173 252.125 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015112 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015112 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003966 0.00000
TER 3219 HIS A 397
MASTER 300 0 8 17 16 0 0 6 3278 1 66 31
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