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HEADER HYDROLASE 12-JAN-19 6QGN
TITLE CRYSTAL STRUCTURE OF APT1 BOUND TO 2-BROMOPALMITATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PROTEIN THIOESTERASE 1;
COMPND 3 CHAIN: A, B, C, D;
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 2-BROMOPALMITATE DEPALMITOYLATION,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.MARCAIDA,M.AUDAGNOTTO,S.HO,F.POJER,G.VAN DER GOOT,M.DAL PERARO
REVDAT 3 31-MAR-21 6QGN 1 JRNL
REVDAT 2 17-MAR-21 6QGN 1 JRNL
REVDAT 1 05-FEB-20 6QGN 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. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 66823
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160
REMARK 3 FREE R VALUE TEST SET COUNT : 3446
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 46.4382 - 6.1335 1.00 2737 166 0.2105 0.2210
REMARK 3 2 6.1335 - 4.8701 1.00 2609 159 0.2211 0.2585
REMARK 3 3 4.8701 - 4.2549 1.00 2594 142 0.1997 0.2135
REMARK 3 4 4.2549 - 3.8661 1.00 2585 136 0.2169 0.2549
REMARK 3 5 3.8661 - 3.5891 1.00 2577 128 0.2295 0.2714
REMARK 3 6 3.5891 - 3.3776 1.00 2535 157 0.2351 0.2608
REMARK 3 7 3.3776 - 3.2085 1.00 2569 110 0.2407 0.3112
REMARK 3 8 3.2085 - 3.0688 1.00 2529 151 0.2480 0.2938
REMARK 3 9 3.0688 - 2.9507 1.00 2535 122 0.2443 0.2748
REMARK 3 10 2.9507 - 2.8489 1.00 2542 152 0.2434 0.3215
REMARK 3 11 2.8489 - 2.7598 1.00 2528 140 0.2357 0.3003
REMARK 3 12 2.7598 - 2.6810 1.00 2494 141 0.2324 0.2611
REMARK 3 13 2.6810 - 2.6104 1.00 2542 122 0.2423 0.3120
REMARK 3 14 2.6104 - 2.5467 1.00 2537 122 0.2386 0.3080
REMARK 3 15 2.5467 - 2.4888 1.00 2523 139 0.2413 0.3093
REMARK 3 16 2.4888 - 2.4358 1.00 2507 142 0.2380 0.2841
REMARK 3 17 2.4358 - 2.3871 1.00 2518 140 0.2351 0.3261
REMARK 3 18 2.3871 - 2.3421 1.00 2516 125 0.2230 0.2840
REMARK 3 19 2.3421 - 2.3003 1.00 2529 131 0.2320 0.2655
REMARK 3 20 2.3003 - 2.2613 1.00 2462 144 0.2351 0.3300
REMARK 3 21 2.2613 - 2.2248 1.00 2565 118 0.2443 0.3360
REMARK 3 22 2.2248 - 2.1906 1.00 2504 115 0.2469 0.3190
REMARK 3 23 2.1906 - 2.1583 1.00 2509 160 0.2432 0.3018
REMARK 3 24 2.1583 - 2.1279 1.00 2504 132 0.2455 0.2996
REMARK 3 25 2.1279 - 2.0992 0.94 2327 152 0.2751 0.3279
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.170
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 : 0.007 6962
REMARK 3 ANGLE : 0.830 9453
REMARK 3 CHIRALITY : 0.049 1078
REMARK 3 PLANARITY : 0.006 1222
REMARK 3 DIHEDRAL : 7.684 5014
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 6QGN 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_1292100040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-18
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) : 0.91971
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66902
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 46.427
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.200
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: 5SYM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: D1 MORPHEUS (MOLECULAR DIMENSIONS) 0.1
REMARK 280 M IMIDAZOLE, 0.1 M MES MONOHYDRATE, 20% V/V PEG 500 MME, 10% W/V
REMARK 280 PEG 2000, 20 MM 1,6-HEXANEDIOL, 20 MM 1-BUTANOL, 20 MM 1,2-
REMARK 280 PROPANEDIOL, 20 MM 2- PROPANOL, 20 MM 1,4-BUTANEDIOL, 20 MM 1,3-
REMARK 280 PROPANEDIOL, PH 6.5., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+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 29.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.35650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.80800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.35650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.80800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 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
REMARK 350 BIOMOLECULE: 2
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: 3
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 A -2
REMARK 465 SER A -1
REMARK 465 ARG A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ASN A 4
REMARK 465 ASN A 5
REMARK 465 MET A 6
REMARK 465 SER A 7
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 ARG B 0
REMARK 465 MET B 1
REMARK 465 SER 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 GLY C -2
REMARK 465 SER C -1
REMARK 465 ARG C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 ASN C 4
REMARK 465 ASN C 5
REMARK 465 MET C 6
REMARK 465 SER C 7
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 ARG D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLY D 3
REMARK 465 ASN D 4
REMARK 465 ASN D 5
REMARK 465 MET D 6
REMARK 465 SER D 7
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 A 409 O HOH A 496 2.13
REMARK 500 OG SER C 183 OD1 ASP D 81 2.15
REMARK 500 O HOH A 505 O HOH A 508 2.18
REMARK 500
REMARK 500 REMARK: NULL
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. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED 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 NH1 ARG A 18 O GLU C 39 3445 2.17
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 ALA A 17 -70.31 -48.56
REMARK 500 SER A 119 -121.94 53.59
REMARK 500 SER A 143 65.12 34.28
REMARK 500 MET A 207 -145.64 -103.50
REMARK 500 SER A 209 -166.27 -160.96
REMARK 500 ARG B 18 -130.93 -109.63
REMARK 500 ASN B 64 70.97 -113.22
REMARK 500 MET B 65 57.87 26.69
REMARK 500 SER B 71 128.31 -171.98
REMARK 500 SER B 119 -128.28 60.09
REMARK 500 CYS B 144 -158.94 -139.05
REMARK 500 MET B 207 -144.49 -100.40
REMARK 500 SER B 209 -173.09 -178.40
REMARK 500 LEU B 226 58.49 -118.83
REMARK 500 ASN C 64 68.19 -112.98
REMARK 500 ASN C 111 2.12 -69.02
REMARK 500 SER C 119 -120.22 52.48
REMARK 500 CYS C 144 -158.41 -141.85
REMARK 500 MET C 207 -141.33 -101.30
REMARK 500 SER C 209 -148.95 -160.65
REMARK 500 ARG D 18 -106.28 -122.79
REMARK 500 ASN D 64 69.73 -112.72
REMARK 500 SER D 71 135.50 -172.46
REMARK 500 ASN D 111 6.89 -64.87
REMARK 500 SER D 119 -128.12 59.69
REMARK 500 GLN D 154 52.41 -100.44
REMARK 500 PRO D 156 134.49 -37.73
REMARK 500 MET D 207 -140.39 -104.89
REMARK 500 SER D 209 -159.01 -172.83
REMARK 500 LEU D 226 56.18 -116.39
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 J1W A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1W B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1W C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1W D 301
DBREF 6QGN A 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGN B 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGN C 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGN D 1 230 UNP O75608 LYPA1_HUMAN 1 230
SEQADV 6QGN GLY A -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER A -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGN ARG A 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER A 2 UNP O75608 CYS 2 ENGINEERED MUTATION
SEQADV 6QGN GLY B -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER B -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGN ARG B 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER B 2 UNP O75608 CYS 2 ENGINEERED MUTATION
SEQADV 6QGN GLY C -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER C -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGN ARG C 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER C 2 UNP O75608 CYS 2 ENGINEERED MUTATION
SEQADV 6QGN GLY D -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER D -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGN ARG D 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGN SER D 2 UNP O75608 CYS 2 ENGINEERED MUTATION
SEQRES 1 A 233 GLY SER ARG MET SER GLY ASN ASN MET SER THR PRO LEU
SEQRES 2 A 233 PRO ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA
SEQRES 3 A 233 VAL ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY
SEQRES 4 A 233 TRP ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE
SEQRES 5 A 233 LYS TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR
SEQRES 6 A 233 LEU ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE
SEQRES 7 A 233 ILE GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY
SEQRES 8 A 233 ILE LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP
SEQRES 9 A 233 GLN GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE
SEQRES 10 A 233 LEU GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR
SEQRES 11 A 233 THR ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR
SEQRES 12 A 233 ALA LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO
SEQRES 13 A 233 GLN GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE
SEQRES 14 A 233 LEU GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU
SEQRES 15 A 233 MET PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU
SEQRES 16 A 233 VAL ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY
SEQRES 17 A 233 MET MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL
SEQRES 18 A 233 LYS GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
SEQRES 1 B 233 GLY SER ARG MET SER 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 SER 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 SER 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 SER 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
SEQRES 1 D 233 GLY SER ARG MET SER GLY ASN ASN MET SER THR PRO LEU
SEQRES 2 D 233 PRO ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA
SEQRES 3 D 233 VAL ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY
SEQRES 4 D 233 TRP ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE
SEQRES 5 D 233 LYS TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR
SEQRES 6 D 233 LEU ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE
SEQRES 7 D 233 ILE GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY
SEQRES 8 D 233 ILE LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP
SEQRES 9 D 233 GLN GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE
SEQRES 10 D 233 LEU GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR
SEQRES 11 D 233 THR ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR
SEQRES 12 D 233 ALA LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO
SEQRES 13 D 233 GLN GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE
SEQRES 14 D 233 LEU GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU
SEQRES 15 D 233 MET PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU
SEQRES 16 D 233 VAL ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY
SEQRES 17 D 233 MET MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL
SEQRES 18 D 233 LYS GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
HET J1W A 301 49
HET J1W B 301 49
HET J1W C 301 49
HET J1W D 301 49
HETNAM J1W 2-BROMOPALMITIC ACID
FORMUL 5 J1W 4(C16 H31 BR O2)
FORMUL 9 HOH *438(H2 O)
HELIX 1 AA1 GLY A 34 GLY A 43 1 10
HELIX 2 AA2 ASP A 85 GLY A 107 1 23
HELIX 3 AA3 PRO A 109 ASN A 111 5 3
HELIX 4 AA4 SER A 119 THR A 132 1 14
HELIX 5 AA5 LEU A 148 PHE A 152 5 5
HELIX 6 AA6 PRO A 178 VAL A 193 1 16
HELIX 7 AA7 ASN A 194 ALA A 196 5 3
HELIX 8 AA8 CYS A 211 LEU A 226 1 16
HELIX 9 AA9 GLY B 34 GLY B 43 1 10
HELIX 10 AB1 THR B 62 MET B 65 5 4
HELIX 11 AB2 ASP B 85 LYS B 105 1 21
HELIX 12 AB3 PRO B 109 ASN B 111 5 3
HELIX 13 AB4 SER B 119 THR B 132 1 14
HELIX 14 AB5 LEU B 148 PHE B 152 5 5
HELIX 15 AB6 PRO B 178 VAL B 193 1 16
HELIX 16 AB7 ASN B 194 ALA B 196 5 3
HELIX 17 AB8 CYS B 211 LEU B 226 1 16
HELIX 18 AB9 GLY C 34 ILE C 44 1 11
HELIX 19 AC1 THR C 62 MET C 65 5 4
HELIX 20 AC2 ASP C 85 LYS C 105 1 21
HELIX 21 AC3 PRO C 109 ASN C 111 5 3
HELIX 22 AC4 SER C 119 LEU C 130 1 12
HELIX 23 AC5 LEU C 148 PHE C 152 5 5
HELIX 24 AC6 PRO C 178 VAL C 193 1 16
HELIX 25 AC7 ASN C 194 ALA C 196 5 3
HELIX 26 AC8 CYS C 211 LEU C 226 1 16
HELIX 27 AC9 GLY D 34 ARG D 45 1 12
HELIX 28 AD1 ASP D 85 ASN D 106 1 22
HELIX 29 AD2 PRO D 109 ASN D 111 5 3
HELIX 30 AD3 SER D 119 THR D 132 1 14
HELIX 31 AD4 LEU D 148 PHE D 152 5 5
HELIX 32 AD5 PRO D 178 VAL D 193 1 16
HELIX 33 AD6 ASN D 194 ALA D 196 5 3
HELIX 34 AD7 CYS D 211 LEU D 226 1 16
SHEET 1 AA1 7 ALA A 12 VAL A 14 0
SHEET 2 AA1 7 ILE A 49 CYS A 53 -1 O TYR A 51 N VAL A 14
SHEET 3 AA1 7 ALA A 22 LEU A 27 1 N VAL A 24 O ILE A 52
SHEET 4 AA1 7 ILE A 113 PHE A 118 1 O ILE A 114 N ILE A 25
SHEET 5 AA1 7 GLY A 138 LEU A 142 1 O LEU A 142 N GLY A 117
SHEET 6 AA1 7 ILE A 166 GLY A 171 1 O LEU A 167 N ALA A 141
SHEET 7 AA1 7 VAL A 198 TYR A 203 1 O THR A 199 N GLN A 168
SHEET 1 AA2 2 VAL A 58 PRO A 60 0
SHEET 2 AA2 2 ALA A 68 PRO A 70 -1 O MET A 69 N ARG A 59
SHEET 1 AA3 7 ALA B 12 VAL B 14 0
SHEET 2 AA3 7 ILE B 49 CYS B 53 -1 O TYR B 51 N VAL B 14
SHEET 3 AA3 7 ALA B 22 LEU B 27 1 N VAL B 24 O ILE B 52
SHEET 4 AA3 7 ILE B 113 PHE B 118 1 O ILE B 114 N ILE B 25
SHEET 5 AA3 7 GLY B 138 LEU B 142 1 O LEU B 142 N GLY B 117
SHEET 6 AA3 7 ILE B 166 GLY B 171 1 O LEU B 167 N VAL B 139
SHEET 7 AA3 7 VAL B 198 TYR B 203 1 O THR B 199 N GLN B 168
SHEET 1 AA4 2 VAL B 58 PRO B 60 0
SHEET 2 AA4 2 ALA B 68 PRO B 70 -1 O MET B 69 N ARG B 59
SHEET 1 AA5 7 ALA C 12 VAL C 14 0
SHEET 2 AA5 7 ILE C 49 CYS C 53 -1 O CYS C 53 N ALA C 12
SHEET 3 AA5 7 ALA C 22 LEU C 27 1 N VAL C 24 O ILE C 52
SHEET 4 AA5 7 ILE C 113 PHE C 118 1 O PHE C 118 N LEU C 27
SHEET 5 AA5 7 GLY C 138 LEU C 142 1 O LEU C 142 N GLY C 117
SHEET 6 AA5 7 ILE C 166 GLY C 171 1 O LEU C 167 N ALA C 141
SHEET 7 AA5 7 VAL C 198 TYR C 203 1 O THR C 199 N ILE C 166
SHEET 1 AA6 2 VAL C 58 PRO C 60 0
SHEET 2 AA6 2 ALA C 68 PRO C 70 -1 O MET C 69 N ARG C 59
SHEET 1 AA7 7 ALA D 12 VAL D 14 0
SHEET 2 AA7 7 ILE D 49 CYS D 53 -1 O TYR D 51 N VAL D 14
SHEET 3 AA7 7 ALA D 22 LEU D 27 1 N VAL D 24 O ILE D 52
SHEET 4 AA7 7 ILE D 113 PHE D 118 1 O ILE D 114 N ILE D 25
SHEET 5 AA7 7 GLY D 138 LEU D 142 1 O LEU D 142 N GLY D 117
SHEET 6 AA7 7 ILE D 166 GLY D 171 1 O LEU D 167 N VAL D 139
SHEET 7 AA7 7 VAL D 198 TYR D 203 1 O THR D 199 N ILE D 166
SHEET 1 AA8 2 VAL D 58 VAL D 61 0
SHEET 2 AA8 2 VAL D 67 PRO D 70 -1 O MET D 69 N ARG D 59
SITE 1 AC1 11 LEU A 30 ILE A 75 LEU A 78 SER A 119
SITE 2 AC1 11 GLN A 120 TRP A 145 LEU A 176 PHE A 181
SITE 3 AC1 11 LEU A 184 THR A 185 HOH A 417
SITE 1 AC2 11 LEU B 30 ILE B 75 LEU B 78 SER B 119
SITE 2 AC2 11 GLN B 120 TRP B 145 ARG B 149 LEU B 176
SITE 3 AC2 11 PHE B 181 LEU B 184 HIS B 208
SITE 1 AC3 11 LEU C 30 ILE C 75 LEU C 78 SER C 119
SITE 2 AC3 11 GLN C 120 TRP C 145 PHE C 181 LEU C 184
SITE 3 AC3 11 THR C 185 HIS C 208 HOH C 420
SITE 1 AC4 11 LEU D 30 ILE D 75 LEU D 78 SER D 119
SITE 2 AC4 11 GLN D 120 TRP D 145 ARG D 149 VAL D 177
SITE 3 AC4 11 PHE D 181 THR D 185 HIS D 208
CRYST1 58.900 109.616 174.713 90.00 90.00 90.00 P 21 21 21 16
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 0.016978 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009123 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005724 0.00000
TER 1697 ASP A 230
TER 3624 ASP B 230
TER 5313 ASP C 230
TER 7006 ASP D 230
MASTER 378 0 4 34 36 0 12 6 7226 4 196 72
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