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HEADER HYDROLASE 29-NOV-20 7B38
TITLE TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH MG+2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;
SOURCE 3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;
SOURCE 4 ORGANISM_TAXID: 7787;
SOURCE 5 VARIANT: G2 FORM;
SOURCE 6 ORGAN: ELECTRIC ORGAN;
SOURCE 7 TISSUE: ELECTROPLAQUE
KEYWDS ACETYLCHOLINESTERASE; ASSAM; DIFFERENTIAL SCANNING CALORIMETRY;
KEYWDS 2 DIVALENT METAL ION; ELECTRON PARAMAGNETIC RESONANCE; THERMAL
KEYWDS 3 INACTIVATION; TORPEDO; 4D MOTIF, HYDROLASE, 3.1.1.7
EXPDTA X-RAY DIFFRACTION
AUTHOR I.SILMAN,V.L.SHNYROV,Y.ASHANI,E.ROTH,A.NICOLAS,J.L.SUSSMAN,L.WEINER
REVDAT 1 17-MAR-21 7B38 0
JRNL AUTH I.SILMAN,V.L.SHNYROV,Y.ASHANI,E.ROTH,A.NICOLAS,J.L.SUSSMAN,
JRNL AUTH 2 L.WEINER
JRNL TITL TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IS STABILIZED BY
JRNL TITL 2 BINDING OF A DIVALENT METAL ION TO A NOVEL AND VERSATILE 4D
JRNL TITL 3 MOTIF
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.DVIR,H.L.JIANG,D.M.WONG,M.HAREL,M.CHETRIT,X.C.HE,G.Y.JIN,
REMARK 1 AUTH 2 G.L.YU,X.C.TANG,I.SILMAN,D.L.BAI,J.L.SUSSMAN
REMARK 1 TITL X-RAY STRUCTURES OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
REMARK 1 TITL 2 COMPLEXED WITH (+)-HUPERZINE A AND (-)-HUPERZINE B:
REMARK 1 TITL 3 STRUCTURAL EVIDENCE FOR AN ACTIVE SITE REARRANGEMENT.
REMARK 1 REF BIOCHEMISTRY V. 41 10810 2002
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 12196020
REMARK 1 DOI 10.1021/BI020151+
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,L.TOKER,
REMARK 1 AUTH 2 I.SILMAN
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM TORPEDO
REMARK 1 TITL 2 CALIFORNICA: A PROTOTYPIC ACETYLCHOLINE-BINDING PROTEIN.
REMARK 1 REF SCIENCE V. 253 872 1991
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 1678899
REMARK 1 DOI 10.1126/SCIENCE.1678899
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 66943
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : 4.92%
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 3292
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2635
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2996
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.3443
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4200
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 127
REMARK 3 SOLVENT ATOMS : 397
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.213
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.11
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7B38 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-20.
REMARK 100 THE DEPOSITION ID IS D_1292112564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 155
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO V1.0
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK V1.0
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69953
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 34.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
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 : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT V1.0
REMARK 200 STARTING MODEL: 1EA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXING 2 UL OF PROTEIN (10-13 MG/ML IN
REMARK 280 0.1 M NACL/0.1 M 2-MORPHOLINOETHANESULFONIC ACID (MES)/0.02%
REMARK 280 SODIUM AZIDE, PH 5.8) WITH 2 UL OF PRECIPITANT SOLUTION (0.2 M
REMARK 280 MAGNESIUM ACETATE/10-15% (V/V) POLYETHYLENE GLYCOL (PEG) 5000
REMARK 280 MONOMETHYL ETHER, 0.1 M MES, PH 6.5), THUS YIELDING CRYSTALS OF
REMARK 280 THE MG+2/TCACHE COMPLEX, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 47.58400
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 23.79200
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 23.79200
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 47.58400
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
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 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 71.37600
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 SER A 4 CB OG
REMARK 470 LEU A 7 CD1 CD2
REMARK 470 ASN A 9 OD1 ND2
REMARK 470 LYS A 14 CD CE NZ
REMARK 470 MET A 16 CE
REMARK 470 LYS A 52 CD CE NZ
REMARK 470 GLU A 89 CD OE1 OE2
REMARK 470 LYS A 107 CG CD CE NZ
REMARK 470 GLU A 140 CD OE1 OE2
REMARK 470 LYS A 192 CG CD CE NZ
REMARK 470 LYS A 413 CE NZ
REMARK 470 GLU A 434 OE1 OE2
REMARK 470 LYS A 454 CE NZ
REMARK 470 LYS A 478 CD CE NZ
REMARK 470 GLU A 484 OE1 OE2
REMARK 470 GLN A 488 CG CD OE1 NE2
REMARK 470 GLU A 489 OE1 OE2
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 SER A 25 -156.22 -141.32
REMARK 500 PHE A 45 -16.65 86.40
REMARK 500 SER A 200 -122.47 55.89
REMARK 500 GLU A 299 -74.56 -117.58
REMARK 500 THR A 317 -159.67 -154.15
REMARK 500 ASP A 380 52.15 -168.02
REMARK 500 VAL A 400 -60.89 -128.34
REMARK 500 HIS A 486 70.40 -153.82
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 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 181 NE2
REMARK 620 2 GLU A 268 OE1 16.5
REMARK 620 3 GLU A 268 OE2 15.2 2.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 619 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 268 OE2
REMARK 620 2 HOH A1004 O 147.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 326 OD1
REMARK 620 2 ASP A 392 OD2 93.0
REMARK 620 3 HOH A 813 O 92.8 87.5
REMARK 620 4 HOH A 873 O 169.8 96.9 90.1
REMARK 620 5 HOH A 903 O 89.1 97.5 174.5 87.2
REMARK 620 6 HOH A 957 O 91.0 173.7 87.4 79.3 87.4
REMARK 620 N 1 2 3 4 5
DBREF 7B38 A 4 535 UNP P04058 ACES_TETCF 25 556
SEQRES 1 A 532 SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET
SEQRES 2 A 532 GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA
SEQRES 3 A 532 PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN
SEQRES 4 A 532 MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER
SEQRES 5 A 532 GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN
SEQRES 6 A 532 GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER
SEQRES 7 A 532 GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS
SEQRES 8 A 532 LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS
SEQRES 9 A 532 SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE
SEQRES 10 A 532 TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS
SEQRES 11 A 532 TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU
SEQRES 12 A 532 SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS
SEQRES 13 A 532 GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP
SEQRES 14 A 532 GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN
SEQRES 15 A 532 PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY
SEQRES 16 A 532 GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU
SEQRES 17 A 532 SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU
SEQRES 18 A 532 GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER
SEQRES 19 A 532 VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG
SEQRES 20 A 532 ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE
SEQRES 21 A 532 HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP
SEQRES 22 A 532 VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG
SEQRES 23 A 532 PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO
SEQRES 24 A 532 THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS
SEQRES 25 A 532 LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY
SEQRES 26 A 532 SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS
SEQRES 27 A 532 ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER
SEQRES 28 A 532 GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY
SEQRES 29 A 532 LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP
SEQRES 30 A 532 ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP
SEQRES 31 A 532 ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS
SEQRES 32 A 532 PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR
SEQRES 33 A 532 LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP
SEQRES 34 A 532 PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU
SEQRES 35 A 532 PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR
SEQRES 36 A 532 THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS
SEQRES 37 A 532 TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU
SEQRES 38 A 532 PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR
SEQRES 39 A 532 LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET
SEQRES 40 A 532 LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE
SEQRES 41 A 532 TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR
HET NAG B 1 14
HET FUC B 2 10
HET MG A 601 1
HET ZN A 602 1
HET NAG A 603 14
HET NAG A 604 14
HET PGE A 605 10
HET GOL A 606 6
HET EDO A 607 4
HET PEG A 608 7
HET EDO A 609 4
HET EDO A 610 10
HET GOL A 611 6
HET PEG A 612 7
HET EDO A 613 4
HET EDO A 614 4
HET EDO A 615 10
HET GOL A 616 6
HET EDO A 617 4
HET MG A 618 1
HET MG A 619 1
HET MG A 620 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 2 FUC C6 H12 O5
FORMUL 3 MG 4(MG 2+)
FORMUL 4 ZN ZN 2+
FORMUL 7 PGE C6 H14 O4
FORMUL 8 GOL 3(C3 H8 O3)
FORMUL 9 EDO 7(C2 H6 O2)
FORMUL 10 PEG 2(C4 H10 O3)
FORMUL 23 HOH *397(H2 O)
HELIX 1 AA1 VAL A 40 ARG A 44 5 5
HELIX 2 AA2 PHE A 78 MET A 83 1 6
HELIX 3 AA3 LEU A 127 ASN A 131 5 5
HELIX 4 AA4 GLY A 132 GLU A 140 1 9
HELIX 5 AA5 GLY A 151 LEU A 156 1 6
HELIX 6 AA6 ASN A 167 ILE A 184 1 18
HELIX 7 AA7 GLN A 185 PHE A 187 5 3
HELIX 8 AA8 SER A 200 SER A 212 1 13
HELIX 9 AA9 SER A 212 ASP A 217 1 6
HELIX 10 AB1 SER A 237 LEU A 252 1 16
HELIX 11 AB2 SER A 258 LYS A 269 1 12
HELIX 12 AB3 LYS A 270 GLU A 278 1 9
HELIX 13 AB4 TRP A 279 LEU A 282 5 4
HELIX 14 AB5 SER A 304 GLY A 312 1 9
HELIX 15 AB6 GLY A 328 ALA A 336 1 9
HELIX 16 AB7 SER A 348 VAL A 360 1 13
HELIX 17 AB8 ASN A 364 THR A 376 1 13
HELIX 18 AB9 ASN A 383 VAL A 400 1 18
HELIX 19 AC1 VAL A 400 LYS A 413 1 14
HELIX 20 AC2 PRO A 433 GLY A 437 5 5
HELIX 21 AC3 GLU A 443 PHE A 448 1 6
HELIX 22 AC4 GLY A 449 ASN A 457 5 9
HELIX 23 AC5 THR A 459 GLY A 480 1 22
HELIX 24 AC6 ARG A 517 GLN A 526 1 10
HELIX 25 AC7 GLN A 526 THR A 535 1 10
SHEET 1 AA1 3 LEU A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 MET A 16 -1 O GLY A 13 N THR A 10
SHEET 3 AA1 3 VAL A 57 ASN A 59 1 O TRP A 58 N MET A 16
SHEET 1 AA211 THR A 18 VAL A 22 0
SHEET 2 AA211 SER A 25 PRO A 34 -1 O ALA A 29 N THR A 18
SHEET 3 AA211 TYR A 96 VAL A 101 -1 O ILE A 99 N PHE A 30
SHEET 4 AA211 VAL A 142 SER A 145 -1 O LEU A 143 N TRP A 100
SHEET 5 AA211 THR A 109 ILE A 115 1 N MET A 112 O VAL A 144
SHEET 6 AA211 GLY A 189 GLU A 199 1 O ASP A 190 N THR A 109
SHEET 7 AA211 ARG A 221 GLN A 225 1 O GLN A 225 N GLY A 198
SHEET 8 AA211 GLN A 318 ASN A 324 1 O LEU A 320 N LEU A 224
SHEET 9 AA211 GLY A 417 PHE A 423 1 O PHE A 423 N VAL A 323
SHEET 10 AA211 LYS A 501 LEU A 505 1 O LEU A 505 N PHE A 422
SHEET 11 AA211 VAL A 512 GLN A 514 -1 O HIS A 513 N PHE A 502
SSBOND 1 CYS A 67 CYS A 94 1555 1555 2.09
SSBOND 2 CYS A 254 CYS A 265 1555 1555 2.07
SSBOND 3 CYS A 402 CYS A 521 1555 1555 2.08
LINK ND2 ASN A 59 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 416 C1 NAG A 603 1555 1555 1.45
LINK ND2 ASN A 457 C1 NAG A 604 1555 1555 1.44
LINK O6 NAG B 1 C1 FUC B 2 1555 1555 1.37
LINK OE2 GLU A 139 MG MG A 618 1555 1555 2.64
LINK NE2 HIS A 181 ZN ZN A 602 1555 3665 2.44
LINK OE1 GLU A 268 ZN ZN A 602 1555 1555 2.36
LINK OE2 GLU A 268 ZN ZN A 602 1555 1555 1.92
LINK OE2 GLU A 268 MG MG A 619 1555 1555 2.41
LINK OD1 ASP A 326 MG MG A 601 1555 1555 2.01
LINK OD2 ASP A 392 MG MG A 601 1555 1555 1.97
LINK O HIS A 486 MG MG A 620 1555 4556 2.11
LINK MG MG A 601 O HOH A 813 1555 1555 2.07
LINK MG MG A 601 O HOH A 873 1555 1555 2.14
LINK MG MG A 601 O HOH A 903 1555 1555 2.07
LINK MG MG A 601 O HOH A 957 1555 1555 2.20
LINK MG MG A 619 O HOH A1004 1555 2654 2.43
CISPEP 1 SER A 103 PRO A 104 0 3.64
CRYST1 138.217 138.217 71.376 90.00 90.00 120.00 P 32 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 0.007235 0.004177 0.000000 0.00000
SCALE2 0.000000 0.008354 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014010 0.00000
TER 4207 THR A 535
MASTER 352 0 22 25 14 0 0 6 4724 1 157 41
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