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HEADER HYDROLASE 14-JUN-99 1QII
TITLE SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME POINTS
TITLE 2 (POINT F) CAUSED BY INTENSE SYNCHROTRON RADIATION TO
TITLE 3 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 VARIANT: G2 FORM;
SOURCE 5 ORGAN: ELECTRIC ORGAN;
SOURCE 6 TISSUE: ELECTROPLAQUE
KEYWDS RADIATION DAMAGE, TIME SERIES, DISULFIDE BOND, SERINE
KEYWDS 2 HYDROLASE, ALPHA/BETA HYDROLASE, NEUROTRANSMITTER CLEAVAGE,
KEYWDS 3 CATALYTIC TRIAD, GLYCOSYLATED PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KRYGER,M.WEIK,R.B.G.RAVELLI
REVDAT 1 28-JAN-00 1QII 0
JRNL AUTH M.WEIK,R.B.G.RAVELLI,G.KRYGER,S.MCSWEENEY,
JRNL AUTH 2 M.L.RAVES,M.HAREL,P.GROS,I.SILMAN,J.KROON,
JRNL AUTH 3 J.L.SUSSMAN
JRNL TITL SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE TO
JRNL TITL 2 PROTEINS BY SYNCHROTRON RADIATION
JRNL REF PROC.NAT.ACAD.SCI.USA V. 97 623 2000
JRNL REFN ASTM PNASA6 US ISSN 0027-8424
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 2227180.61000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 29353
REMARK 3
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) : 0.198
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1421
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2727
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.06000
REMARK 3 B22 (A**2) : 5.06000
REMARK 3 B33 (A**2) : -10.11000
REMARK 3 B12 (A**2) : 4.13000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.400
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) : 0.34
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.85
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) : 3.32 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.14 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.92 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.92 ; 2.500
REMARK 3
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 39.12
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_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.PARAM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED. ONLY
REMARK 3 PARTIAL REFINEMENT DONE. ALL SIX CYSTEINE RESIDUES TAKING
REMARK 3 PART IN INTRACHAIN DISULFIDE LINKAGES,CYS 67-CYS 94, CYS
REMARK 3 402- CYS 521 AND CYS 254-CYS 265, WERE MODELED AND
REMARK 3 REFINED AS ALANINE RESIDUES.
REMARK 4
REMARK 4 1QII COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 7
REMARK 7 TCACHE IS A GLYCOPROTEIN OF MR = 65,000, WHICH CONTAINS
REMARK 7 THREE INTRACHAIN DISULFIDE BONDS. IN THE COURSE OF
REMARK 7 CRYOGENIC DATA COLLECTION ON TRIGONAL CRYSTALS OF TCACHE ON
REMARK 7 THE UNDULATOR BEAMLINE, ID14-EH4, AT THE ESRF IN GRENOBLE,
REMARK 7 IN PREPARATION FOR TIME-RESOLVED STUDIES, WE COLLECTED A
REMARK 7 SERIES OF NINE HIGH-QUALITY COMPLETE DATA SETS ON THE SAME
REMARK 7 CRYSTAL. DATA COLLECTION UTILIZED THE UNATTENUATED BEAM,
REMARK 7 AND THE DURATION PER DATA SET WAS CA. 19 MIN, FOR 3 H IN
REMARK 7 TOTAL, AT 100K. ELECTRON DENSITY MAPS WERE OBTAINED FOR
REMARK 7 EACH DATA SET BY ROUTINE REFINEMENT, STARTING FROM THE SAME
REMARK 7 MODEL OF NATIVE TCACHE. FOR RESULTS, SEE:
REMARK 7 HTTP://SGJS3.WEIZMANN.AC.IL/~KRYGER/RADIATION_DAMAGE
REMARK 7 (LOWER CASE!)
REMARK 8
REMARK 8 THIS ENTRY IS THE 6TH TIME POINT (6 OF 9). SEE HTTP://
REMARK 8 SGJS3.WEIZMANN.AC.IL/~KRYGER/RADIATION_DAMAGE (LOWER CASE!)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-1999.
REMARK 100 THE RCSB ID CODE IS RCSB001189.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-1999
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-EH4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC 2X2 QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29417
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 36.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 2.080
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: CNS_SOLVE 0.5
REMARK 200 STARTING MODEL: PDB ENTRY 1VXR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 200, 0.3 M MES
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.99800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.99600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.99600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.99800
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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 137.99400
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 ASP A 1
REMARK 465 ASP A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 536
REMARK 465 CYS A 537
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 CYS A 67 SG
REMARK 470 CYS A 94 SG
REMARK 470 CYS A 254 SG
REMARK 470 CYS A 265 SG
REMARK 470 CYS A 402 SG
REMARK 470 CYS A 521 SG
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 ASN A 183 N - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP A 285 N - CA - C ANGL. DEV. =-14.9 DEGREES
REMARK 500 GLY A 328 N - CA - C ANGL. DEV. = 8.9 DEGREES
REMARK 500 GLY A 335 N - CA - C ANGL. DEV. = 11.1 DEGREES
REMARK 500 ILE A 439 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 THR A 479 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 TRP A 492 N - CA - C ANGL. DEV. = -9.1 DEGREES
REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 8.7 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 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
REMARK 500 SER A 200 54.25 -119.45
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 1225 DISTANCE = 5.48 ANGSTROMS
REMARK 525 0 HOH 1230 DISTANCE = 5.02 ANGSTROMS
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR-DETERMINED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR-DETERMINED.
REMARK 700 TAKEN FROM PDB ENTRY 2ACE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 SITE_DESCRIPTION:
REMARK 800 CATALYTIC TRIAD.
REMARK 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QID RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT A
REMARK 900 RELATED ID: 1QIE RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT B
REMARK 900 RELATED ID: 1QIF RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT C
REMARK 900 RELATED ID: 1QIG RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT D
REMARK 900 RELATED ID: 1QIH RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT E
REMARK 900 RELATED ID: 1QII RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT F
REMARK 900 RELATED ID: 1QIJ RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT G
REMARK 900 RELATED ID: 1QIK RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT H
REMARK 900 RELATED ID: 1QIM RELATED DB: PDB
REMARK 900 EXPERIMENTAL TIME POINT I
DBREF 1QII A 1 537 SWS P04058 ACES_TORCA 22 558
SEQRES 1 A 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 A 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 A 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 A 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 A 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 A 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 A 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 A 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 A 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 A 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 A 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 A 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 A 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 A 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 A 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 A 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 A 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 A 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 A 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 A 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 A 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 A 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 A 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 A 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 A 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 A 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 A 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 A 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 A 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 A 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 A 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 A 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 A 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 A 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 A 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 A 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 A 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 A 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 A 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 A 537 ALA THR ALA CYS
FORMUL 2 HOH *297(H2 O1)
HELIX 1 1 GLY A 41 MET A 43 5 3
HELIX 2 2 SER A 79 TRP A 84 1 6
HELIX 3 3 ASP A 128 TYR A 130 5 3
HELIX 4 4 LYS A 133 GLU A 139 1 7
HELIX 5 5 GLY A 151 PHE A 155 1 5
HELIX 6 6 VAL A 168 PHE A 187 1 20
HELIX 7 7 ALA A 201 LEU A 211 1 11
HELIX 8 8 PRO A 213 LEU A 218 1 6
HELIX 9 9 VAL A 238 LEU A 252 1 15
HELIX 10 10 ASP A 259 GLU A 268 1 10
HELIX 11 11 PRO A 271 VAL A 281 1 11
HELIX 12 12 LEU A 305 SER A 311 1 7
HELIX 13 13 SER A 329 GLY A 335 1 7
HELIX 14 14 ARG A 349 SER A 359 1 11
HELIX 15 15 ASP A 365 GLN A 374 1 10
HELIX 16 16 GLY A 384 ASN A 399 1 16
HELIX 17 17 ILE A 401 PHE A 414 1 14
HELIX 18 18 GLU A 434 MET A 436 5 3
HELIX 19 19 ILE A 444 VAL A 447 1 4
HELIX 20 20 LEU A 450 LEU A 452 5 3
HELIX 21 21 LYS A 454 LEU A 456 5 3
HELIX 22 22 ALA A 460 THR A 479 1 10
HELIX 23 23 VAL A 518 ASN A 525 1 8
HELIX 24 24 PHE A 527 ASN A 533 1 7
SHEET 1 A 3 LEU A 6 THR A 10 0
SHEET 2 A 3 GLY A 13 MET A 16 -1 N VAL A 15 O VAL A 8
SHEET 3 A 3 VAL A 57 ALA A 60 1 N TRP A 58 O LYS A 14
SHEET 1 B11 MET A 16 PRO A 21 0
SHEET 2 B11 HIS A 26 PRO A 34 -1 O ALA A 29 N THR A 18
SHEET 3 B11 TYR A 96 PRO A 102 -1 N ILE A 99 O PHE A 30
SHEET 4 B11 VAL A 142 SER A 147 -1 N LEU A 143 O TRP A 100
SHEET 5 B11 THR A 109 TYR A 116 1 N MET A 112 O VAL A 142
SHEET 6 B11 THR A 193 GLU A 199 1 O THR A 195 N VAL A 113
SHEET 7 B11 ARG A 220 SER A 226 1 N ILE A 223 O ILE A 196
SHEET 8 B11 GLN A 318 ASN A 324 1 N GLY A 322 O LEU A 224
SHEET 9 B11 GLY A 417 PHE A 423 1 N TYR A 421 O LEU A 321
SHEET 10 B11 PHE A 502 LEU A 505 1 N ILE A 503 O LEU A 420
SHEET 11 B11 MET A 510 GLN A 514 -1 N HIS A 513 O PHE A 502
CISPEP 1 SER A 103 PRO A 104 0 0.06
SITE 1 CAT 3 SER A 200 GLU A 327 HIS A 440
CRYST1 112.124 112.124 137.994 90.00 90.00 120.00 P 31 2 1 6
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 0.008919 0.005149 0.000000 0.00000
SCALE2 0.000000 0.010298 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007247 0.00000
END |