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HEADER HYDROLASE 12-JAN-19 6QGO
TITLE CRYSTAL STRUCTURE OF APT1 S119A MUTANT BOUND TO PALMITIC ACID.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PROTEIN THIOESTERASE 1;
COMPND 3 CHAIN: B, C;
COMPND 4 SYNONYM: HAPT1,LYSOPHOSPHOLIPASE 1,LYSOPHOSPHOLIPASE I,LYSOPLA I;
COMPND 5 EC: 3.1.2.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LYPLA1, APT1, LPL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACYL-PROTEIN THIOESTERASE, PALMITIC ACID, DEPALMITOYLATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.AUDAGNOTTO,M.J.MARCAIDA,S.HO,F.POJER,G.VAN DER GOOT,M.DAL PERARO
REVDAT 3 31-MAR-21 6QGO 1 JRNL
REVDAT 2 17-MAR-21 6QGO 1 JRNL
REVDAT 1 05-FEB-20 6QGO 0
JRNL AUTH L.ABRAMI,M.AUDAGNOTTO,S.HO,M.J.MARCAIDA,F.S.MESQUITA,
JRNL AUTH 2 M.U.ANWAR,P.A.SANDOZ,G.FONTI,F.POJER,M.DAL PERARO,
JRNL AUTH 3 F.G.VAN DER GOOT
JRNL TITL PALMITOYLATED ACYL PROTEIN THIOESTERASE APT2 DEFORMS
JRNL TITL 2 MEMBRANES TO EXTRACT SUBSTRATE ACYL CHAINS.
JRNL REF NAT.CHEM.BIOL. 2021
JRNL REFN ESSN 1552-4469
JRNL PMID 33707782
JRNL DOI 10.1038/S41589-021-00753-2
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 16797
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 846
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.9522 - 4.7219 1.00 2684 153 0.1652 0.1891
REMARK 3 2 4.7219 - 3.7483 1.00 2668 142 0.1596 0.2189
REMARK 3 3 3.7483 - 3.2746 1.00 2615 172 0.1958 0.2646
REMARK 3 4 3.2746 - 2.9753 1.00 2666 118 0.2220 0.2528
REMARK 3 5 2.9753 - 2.7621 1.00 2692 130 0.2377 0.3299
REMARK 3 6 2.7621 - 2.5992 0.99 2626 131 0.2427 0.3005
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 3432
REMARK 3 ANGLE : 0.641 4662
REMARK 3 CHIRALITY : 0.043 533
REMARK 3 PLANARITY : 0.005 602
REMARK 3 DIHEDRAL : 5.500 2078
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6QGO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16831
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 48.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1FJ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% OF OF POLYETHYLENE GLYCOL (PEG)
REMARK 280 2000, 0.3 M SODIUM ACETATE, 0.1 M SODIUM CACODYLATE PH 6.5;,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
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 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,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 33.34167
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 66.68333
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.34167
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 66.68333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 GLY B -2
REMARK 465 SER B -1
REMARK 465 ARG B 0
REMARK 465 MET B 1
REMARK 465 CYS B 2
REMARK 465 GLY B 3
REMARK 465 ASN B 4
REMARK 465 ASN B 5
REMARK 465 MET B 6
REMARK 465 SER B 7
REMARK 465 THR B 8
REMARK 465 ASP B 230
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 ARG C 0
REMARK 465 MET C 1
REMARK 465 CYS C 2
REMARK 465 GLY C 3
REMARK 465 ASN C 4
REMARK 465 ASN C 5
REMARK 465 MET C 6
REMARK 465 ASP C 230
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 DISTANCE
REMARK 500 O HOH C 317 O HOH C 321 2.19
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 ARG B 18 -156.83 -75.41
REMARK 500 ALA B 119 -119.01 58.24
REMARK 500 CYS B 144 -158.79 -131.70
REMARK 500 MET B 207 -134.76 -99.91
REMARK 500 SER B 209 -149.96 -153.49
REMARK 500 PRO C 9 -176.32 -68.76
REMARK 500 ALA C 20 69.35 39.04
REMARK 500 ALA C 119 -119.63 59.01
REMARK 500 MET C 207 -143.07 -90.93
REMARK 500 SER C 209 -162.79 -163.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6QGN RELATED DB: PDB
DBREF 6QGO B 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGO C 1 230 UNP O75608 LYPA1_HUMAN 1 230
SEQADV 6QGO GLY B -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGO SER B -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGO ARG B 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGO ALA B 119 UNP O75608 SER 119 ENGINEERED MUTATION
SEQADV 6QGO GLY C -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGO SER C -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGO ARG C 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGO ALA C 119 UNP O75608 SER 119 ENGINEERED MUTATION
SEQRES 1 B 233 GLY SER ARG MET CYS GLY ASN ASN MET SER THR PRO LEU
SEQRES 2 B 233 PRO ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA
SEQRES 3 B 233 VAL ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY
SEQRES 4 B 233 TRP ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE
SEQRES 5 B 233 LYS TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR
SEQRES 6 B 233 LEU ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE
SEQRES 7 B 233 ILE GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY
SEQRES 8 B 233 ILE LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP
SEQRES 9 B 233 GLN GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE
SEQRES 10 B 233 LEU GLY GLY PHE ALA GLN GLY GLY ALA LEU SER LEU TYR
SEQRES 11 B 233 THR ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR
SEQRES 12 B 233 ALA LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO
SEQRES 13 B 233 GLN GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE
SEQRES 14 B 233 LEU GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU
SEQRES 15 B 233 MET PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU
SEQRES 16 B 233 VAL ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY
SEQRES 17 B 233 MET MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL
SEQRES 18 B 233 LYS GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
SEQRES 1 C 233 GLY SER ARG MET CYS GLY ASN ASN MET SER THR PRO LEU
SEQRES 2 C 233 PRO ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA
SEQRES 3 C 233 VAL ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY
SEQRES 4 C 233 TRP ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE
SEQRES 5 C 233 LYS TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR
SEQRES 6 C 233 LEU ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE
SEQRES 7 C 233 ILE GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY
SEQRES 8 C 233 ILE LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP
SEQRES 9 C 233 GLN GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE
SEQRES 10 C 233 LEU GLY GLY PHE ALA GLN GLY GLY ALA LEU SER LEU TYR
SEQRES 11 C 233 THR ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR
SEQRES 12 C 233 ALA LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO
SEQRES 13 C 233 GLN GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE
SEQRES 14 C 233 LEU GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU
SEQRES 15 C 233 MET PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU
SEQRES 16 C 233 VAL ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY
SEQRES 17 C 233 MET MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL
SEQRES 18 C 233 LYS GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
HET PLM B 301 18
HETNAM PLM PALMITIC ACID
FORMUL 3 PLM C16 H32 O2
FORMUL 4 HOH *51(H2 O)
HELIX 1 AA1 GLY B 34 GLY B 43 1 10
HELIX 2 AA2 THR B 62 MET B 65 5 4
HELIX 3 AA3 ASP B 85 GLY B 107 1 23
HELIX 4 AA4 PRO B 109 ASN B 111 5 3
HELIX 5 AA5 ALA B 119 LEU B 130 1 12
HELIX 6 AA6 LEU B 148 PHE B 152 5 5
HELIX 7 AA7 PRO B 178 VAL B 193 1 16
HELIX 8 AA8 ASN B 194 ALA B 196 5 3
HELIX 9 AA9 CYS B 211 LEU B 226 1 16
HELIX 10 AB1 GLY C 34 GLY C 43 1 10
HELIX 11 AB2 THR C 62 MET C 65 5 4
HELIX 12 AB3 ASP C 85 ASN C 106 1 22
HELIX 13 AB4 PRO C 109 ASN C 111 5 3
HELIX 14 AB5 ALA C 119 THR C 132 1 14
HELIX 15 AB6 LEU C 148 PHE C 152 5 5
HELIX 16 AB7 PRO C 178 VAL C 193 1 16
HELIX 17 AB8 ASN C 194 ALA C 196 5 3
HELIX 18 AB9 CYS C 211 LEU C 226 1 16
SHEET 1 AA1 7 ALA B 12 VAL B 14 0
SHEET 2 AA1 7 ILE B 49 CYS B 53 -1 O TYR B 51 N VAL B 14
SHEET 3 AA1 7 ALA B 22 LEU B 27 1 N VAL B 24 O ILE B 52
SHEET 4 AA1 7 ILE B 113 PHE B 118 1 O ILE B 114 N ALA B 23
SHEET 5 AA1 7 GLY B 138 LEU B 142 1 O LEU B 142 N GLY B 117
SHEET 6 AA1 7 ILE B 166 GLY B 171 1 O LEU B 167 N VAL B 139
SHEET 7 AA1 7 VAL B 198 TYR B 203 1 O THR B 199 N GLN B 168
SHEET 1 AA2 2 VAL B 58 PRO B 60 0
SHEET 2 AA2 2 ALA B 68 PRO B 70 -1 O MET B 69 N ARG B 59
SHEET 1 AA3 7 ALA C 12 VAL C 14 0
SHEET 2 AA3 7 ILE C 49 CYS C 53 -1 O CYS C 53 N ALA C 12
SHEET 3 AA3 7 ALA C 22 LEU C 27 1 N VAL C 24 O ILE C 52
SHEET 4 AA3 7 ILE C 113 PHE C 118 1 O ILE C 114 N ILE C 25
SHEET 5 AA3 7 GLY C 138 LEU C 142 1 O LEU C 142 N GLY C 117
SHEET 6 AA3 7 ILE C 166 GLY C 171 1 O LEU C 167 N VAL C 139
SHEET 7 AA3 7 VAL C 198 TYR C 203 1 O THR C 199 N GLN C 168
SHEET 1 AA4 2 VAL C 58 PRO C 60 0
SHEET 2 AA4 2 ALA C 68 PRO C 70 -1 O MET C 69 N ARG C 59
SITE 1 AC1 10 LEU B 30 LEU B 78 PRO B 80 ALA B 119
SITE 2 AC1 10 GLN B 120 TRP B 145 ARG B 149 PHE B 181
SITE 3 AC1 10 THR B 185 HIS B 208
CRYST1 97.887 97.887 100.025 90.00 90.00 120.00 P 64 12
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 0.010216 0.005898 0.000000 0.00000
SCALE2 0.000000 0.011796 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009998 0.00000
TER 1663 ILE B 229
TER 3339 ILE C 229
MASTER 282 0 1 18 18 0 3 6 3406 2 18 36
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