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HEADER HYDROLASE 23-JUN-96 1VOT
TITLE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH
TITLE 2 HUPERZINE A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.7;
COMPND 5 BIOLOGICAL_UNIT: DIMER IN SOLUTION, ACTIVE AS MONOMER;
COMPND 6 OTHER_DETAILS: INTER-MONOMER DISULFIDE BRIDGE
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 HYDROLASE, NEUROTRANSMITTER CLEAVAGE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.RAVES,M.HAREL,I.SILMAN,J.L.SUSSMAN
REVDAT 1 16-JUN-97 1VOT 0
JRNL AUTH M.L.RAVES,M.HAREL,Y.P.PANG,I.SILMAN,A.P.KOZIKOWSKI,
JRNL AUTH 2 J.L.SUSSMAN
JRNL TITL STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH
JRNL TITL 2 THE NOOTROPIC ALKALOID, (-)-HUPERZINE A
JRNL REF NAT.STRUCT.BIOL. V. 4 57 1997
JRNL REFN ASTM NSBIEW US ISSN 1072-8368 2024
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.ASHANI,J.O.PEGGINS III,B.P.DOCTOR
REMARK 1 TITL MECHANISM OF INHIBITION OF CHOLINESTERASES BY
REMARK 1 TITL 2 HUPERZINE A
REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMM. V. 184 719 1992
REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X 0146
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.J.GEIB,W.TUCKMANTEL,A.P.KOZIKOWSKI
REMARK 1 TITL HUPERZINE A--A POTENT ACETYLCHOLINESTERASE
REMARK 1 TITL 2 INHIBITOR OF USE IN THE TREATMENT OF ALZHEIMER'S
REMARK 1 TITL 3 DISEASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.C V. 47 824 1991
REMARK 1 REFN ASTM ACSCEE DK ISSN 0108-2701 0591
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.L.SUSSMAN,M.HAREL,F.FROLOW,C.OEFNER,A.GOLDMAN,
REMARK 1 AUTH 2 L.TOKER,I.SILMAN
REMARK 1 TITL ATOMIC STRUCTURE OF ACETYLCHOLINESTERASE FROM
REMARK 1 TITL 2 TORPEDO CALIFORNICA: A PROTOTYPIC
REMARK 1 TITL 3 ACETYLCHOLINE-BINDING PROTEIN
REMARK 1 REF SCIENCE V. 253 872 1991
REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 0038
REMARK 2
REMARK 2 RESOLUTION. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.5
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 30040
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) : 0.205
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1592
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.3
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3434
REMARK 3 BIN R VALUE (WORKING SET) : 0.300
REMARK 3 BIN FREE R VALUE : 0.367
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 185
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 208
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.62
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 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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.99
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.2
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.46
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 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.50
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VOT COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-1993
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
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 : 44903
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.3
REMARK 200 RESOLUTION RANGE LOW (A) : 40.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.3
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.096
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.7
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.3
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.4
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.575
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.0
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1ACE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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,Z+1/3
REMARK 290 3555 Y-X,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,Y-X,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 -0.866073 0.000000 0.00000
REMARK 290 SMTRY2 2 0.865977 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.45661
REMARK 290 SMTRY1 3 -0.500000 0.866073 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.865977 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 90.91322
REMARK 290 SMTRY1 4 -0.500000 0.866073 0.000000 0.00000
REMARK 290 SMTRY2 4 0.865977 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 90.91322
REMARK 290 SMTRY1 6 -0.500000 -0.866073 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.865977 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.45661
REMARK 290
REMARK 290 REMARK: NULL
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH 774 LIES ON A SPECIAL POSITION.
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 ARG 19 CZ NH1 NH2
REMARK 470 ASN 42 OD1 ND2
REMARK 470 ARG 46 NE CZ NH1 NH2
REMARK 470 LYS 52 CD CE NZ
REMARK 470 GLU 89 CD OE1 OE2
REMARK 470 GLN 162 CG CD OE1 NE2
REMARK 470 ARG 250 NH1 NH2
REMARK 470 ASN 257 CG OD1 ND2
REMARK 470 GLU 268 OE1 OE2
REMARK 470 LYS 270 CD CE NZ
REMARK 470 GLU 299 CD OE1 OE2
REMARK 470 GLU 344 OE1 OE2
REMARK 470 ARG 349 CZ NH1 NH2
REMARK 470 GLU 350 CD OE1 OE2
REMARK 470 LYS 413 CD CE NZ
REMARK 470 GLU 434 OE1 OE2
REMARK 470 LYS 454 CG CD CE NZ
REMARK 470 GLU 455 CG CD OE1 OE2
REMARK 470 LYS 491 CG CD CE NZ
REMARK 470 LYS 498 CG CD CE NZ
REMARK 470 GLU 499 OE1 OE2
REMARK 470 GLU 508 OE1 OE2
REMARK 470 LYS 511 CD CE NZ
REMARK 470 GLN 526 CD OE1 NE2
REMARK 470 ASN 533 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. SOME OF THESE MAY BE ATOMS
REMARK 500 LOCATED ON SPECIAL POSITIONS IN THE CELL. ATOMS WITH
REMARK 500 NON-BLANK ALTERNATE LOCATION INDICATORS ARE NOT INCLUDED
REMARK 500 IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH 774 O HOH 774 4556 0.02
REMARK 500 SG CYS 537 SG CYS 537 4556 2.09
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 HUP 999: MOLECULE IS OPTICALLY PURE, NOT A RACEMATE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 SITE_DESCRIPTION: ACTIVE-SITE CATALYTIC TRIAD.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1VOT SWS P04058 1 - 24 NOT IN ATOMS LIST
REMARK 999 1VOT SWS P04058 559 - 586 NOT IN ATOMS LIST
DBREF 1VOT 4 484 SWS P04058 ACES_TORCA 25 505
DBREF 1VOT 490 537 SWS P04058 ACES_TORCA 511 558
SEQADV 1VOT SWS P04058 PRO 506 GAP IN PDB ENTRY
SEQADV 1VOT SWS P04058 HIS 507 GAP IN PDB ENTRY
SEQADV 1VOT SWS P04058 SER 508 GAP IN PDB ENTRY
SEQADV 1VOT SWS P04058 GLN 509 GAP IN PDB ENTRY
SEQADV 1VOT SWS P04058 GLU 510 GAP IN PDB ENTRY
SEQRES 1 537 ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY
SEQRES 2 537 LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS
SEQRES 3 537 ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO
SEQRES 4 537 VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS
SEQRES 5 537 PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN
SEQRES 6 537 ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE
SEQRES 7 537 SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER
SEQRES 8 537 GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO
SEQRES 9 537 ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY
SEQRES 10 537 GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR
SEQRES 11 537 ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU
SEQRES 12 537 VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 537 ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 537 LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP
SEQRES 15 537 ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR
SEQRES 16 537 ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET
SEQRES 17 537 HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG
SEQRES 18 537 ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA
SEQRES 19 537 SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU
SEQRES 20 537 LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU
SEQRES 21 537 GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU
SEQRES 22 537 LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER
SEQRES 23 537 ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU
SEQRES 24 537 PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY
SEQRES 25 537 ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS
SEQRES 26 537 ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY
SEQRES 27 537 PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP
SEQRES 28 537 PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN
SEQRES 29 537 ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP
SEQRES 30 537 TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY
SEQRES 31 537 LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO
SEQRES 32 537 LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN
SEQRES 33 537 GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN
SEQRES 34 537 LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR
SEQRES 35 537 GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU
SEQRES 36 537 LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG
SEQRES 37 537 ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN
SEQRES 38 537 PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU
SEQRES 39 537 PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR
SEQRES 40 537 GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET
SEQRES 41 537 CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN
SEQRES 42 537 ALA THR ALA CYS
HET HUP 999 18
HETNAM HUP HUPERAINE A
FORMUL 2 HUP C15 H20 N2 O1
FORMUL 3 HOH *208(H2 O1)
HELIX 1 1 GLY 41 MET 43 5 3
HELIX 2 2 SER 79 TRP 84 1 6
HELIX 3 3 ASP 128 TYR 130 5 3
HELIX 4 4 LYS 133 GLU 139 1 7
HELIX 5 5 GLY 151 PHE 155 1 5
HELIX 6 6 VAL 168 PHE 187 1 20
HELIX 7 7 ALA 201 HIS 209 1 9
HELIX 8 8 PRO 213 LEU 218 5 6
HELIX 9 9 VAL 238 LEU 252 1 15
HELIX 10 10 ASP 259 LEU 266 1 8
HELIX 11 11 PRO 271 ASP 276 1 6
HELIX 12 12 GLU 278 VAL 281 5 4
HELIX 13 13 LEU 305 SER 311 1 7
HELIX 14 14 SER 329 GLY 335 1 7
HELIX 15 15 ARG 349 SER 359 1 11
HELIX 16 16 ASP 365 TYR 375 1 11
HELIX 17 17 GLY 384 ASN 399 1 16
HELIX 18 18 ILE 401 LYS 413 1 13
HELIX 19 19 GLU 434 MET 436 5 3
HELIX 20 20 ILE 444 VAL 447 1 4
HELIX 21 21 LEU 450 LEU 452 5 3
HELIX 22 22 LYS 454 LEU 456 5 3
HELIX 23 23 ALA 460 THR 479 1 20
HELIX 24 24 VAL 518 ASN 525 1 8
HELIX 25 25 PHE 527 ALA 534 1 8
SHEET 1 A 3 LEU 7 THR 10 0
SHEET 2 A 3 GLY 13 MET 16 -1 N VAL 15 O VAL 8
SHEET 3 A 3 VAL 57 ASN 59 1 N TRP 58 O LYS 14
SHEET 1 B11 THR 18 VAL 22 0
SHEET 2 B11 SER 25 PHE 30 -1 N ALA 29 O THR 18
SHEET 3 B11 ASN 98 VAL 101 -1 N VAL 101 O SER 28
SHEET 4 B11 VAL 142 SER 145 -1 N SER 145 O ASN 98
SHEET 5 B11 VAL 111 ILE 115 1 N MET 112 O VAL 142
SHEET 6 B11 VAL 194 GLU 199 1 N THR 195 O VAL 111
SHEET 7 B11 ARG 221 GLN 225 1 N ARG 221 O ILE 196
SHEET 8 B11 ILE 319 ASN 324 1 N LEU 320 O ALA 222
SHEET 9 B11 THR 418 PHE 423 1 N TYR 419 O ILE 319
SHEET 10 B11 LYS 501 LEU 505 1 N ILE 503 O PHE 422
SHEET 11 B11 VAL 512 GLN 514 -1 N HIS 513 O PHE 502
SHEET 1 C 2 SER 235 SER 237 0
SHEET 2 C 2 PRO 294 ILE 296 1 N PRO 294 O VAL 236
SSBOND 1 CYS 67 CYS 94
SSBOND 2 CYS 254 CYS 265
SSBOND 3 CYS 402 CYS 521
CISPEP 1 SER 103 PRO 104 0 0.69
SITE 1 ACT 3 SER 200 HIS 440 GLU 327
CRYST1 112.632 112.632 136.378 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 0.008878 0.005126 0.000000 0.00000
SCALE2 0.000000 0.010252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007333 0.00000 |