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HEADER HYDROLASE 12-JAN-19 6QGS
TITLE CRYSTAL STRUCTURE OF APT1 BOUND TO PALMITIC ACID.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PROTEIN THIOESTERASE 1;
COMPND 3 CHAIN: B, D, A, C, E, F;
COMPND 4 SYNONYM: HAPT1,LYSOPHOSPHOLIPASE 1,LYSOPHOSPHOLIPASE I,LYSOPLA I;
COMPND 5 EC: 3.1.2.-;
COMPND 6 ENGINEERED: 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 6QGS 1 JRNL
REVDAT 2 17-MAR-21 6QGS 1 JRNL
REVDAT 1 05-FEB-20 6QGS 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. 2.76 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) : 2.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 73550
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3664
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 49.9559 - 8.1508 1.00 2680 138 0.1701 0.1794
REMARK 3 2 8.1508 - 6.4740 1.00 2705 149 0.1773 0.2040
REMARK 3 3 6.4740 - 5.6569 1.00 2714 138 0.1766 0.1887
REMARK 3 4 5.6569 - 5.1403 1.00 2690 136 0.1740 0.2170
REMARK 3 5 5.1403 - 4.7722 1.00 2671 144 0.1574 0.1696
REMARK 3 6 4.7722 - 4.4910 1.00 2705 139 0.1505 0.2071
REMARK 3 7 4.4910 - 4.2662 1.00 2683 143 0.1433 0.1598
REMARK 3 8 4.2662 - 4.0806 1.00 2700 145 0.1582 0.2237
REMARK 3 9 4.0806 - 3.9236 1.00 2714 143 0.1650 0.2109
REMARK 3 10 3.9236 - 3.7882 1.00 2713 145 0.1784 0.2270
REMARK 3 11 3.7882 - 3.6698 1.00 2677 143 0.1721 0.2371
REMARK 3 12 3.6698 - 3.5649 1.00 2688 137 0.1762 0.2194
REMARK 3 13 3.5649 - 3.4711 1.00 2732 142 0.1842 0.3077
REMARK 3 14 3.4711 - 3.3864 1.00 2643 134 0.2068 0.2376
REMARK 3 15 3.3864 - 3.3095 1.00 2740 136 0.2038 0.2506
REMARK 3 16 3.3095 - 3.2391 1.00 2684 143 0.2125 0.2841
REMARK 3 17 3.2391 - 3.1743 1.00 2714 141 0.2027 0.3086
REMARK 3 18 3.1743 - 3.1144 1.00 2671 142 0.2128 0.2427
REMARK 3 19 3.1144 - 3.0588 1.00 2723 146 0.2093 0.2718
REMARK 3 20 3.0588 - 3.0069 1.00 2660 137 0.2175 0.2908
REMARK 3 21 3.0069 - 2.9584 1.00 2712 146 0.2028 0.2733
REMARK 3 22 2.9584 - 2.9129 1.00 2681 143 0.2095 0.2703
REMARK 3 23 2.9129 - 2.8701 1.00 2745 145 0.2045 0.2452
REMARK 3 24 2.8701 - 2.8297 1.00 2626 138 0.2276 0.2779
REMARK 3 25 2.8297 - 2.7914 1.00 2749 144 0.2528 0.3336
REMARK 3 26 2.7914 - 2.7552 0.92 2466 127 0.3154 0.3762
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.860
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 10275
REMARK 3 ANGLE : 0.549 13958
REMARK 3 CHIRALITY : 0.043 1595
REMARK 3 PLANARITY : 0.004 1802
REMARK 3 DIHEDRAL : 5.045 6221
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 6QGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-13
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) : 0.82656
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73690
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.755
REMARK 200 RESOLUTION RANGE LOW (A) : 49.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 14.00
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
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 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 (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% OF POLYETHYLENE GLYCOL (PEG) 8000,
REMARK 280 0.2 M POTASSIUM BROMIDE, 01.M SODIUM ACETATE AT PH 5.5,10%W/V
REMARK 280 PEG1000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 220.97300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 40.83000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 40.83000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 110.48650
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 40.83000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 40.83000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 331.45950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 40.83000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.83000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 110.48650
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 40.83000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.83000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 331.45950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 220.97300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: 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 350
REMARK 350 BIOMOLECULE: 3
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: 4
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 ASP B 230
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 ARG D 0
REMARK 465 MET D 1
REMARK 465 CYS 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 465 THR D 8
REMARK 465 ASP D 230
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 ARG A 0
REMARK 465 MET A 1
REMARK 465 CYS 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 THR A 8
REMARK 465 ASP A 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 SER C 7
REMARK 465 THR C 8
REMARK 465 ASP C 230
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 ARG E 0
REMARK 465 MET E 1
REMARK 465 CYS E 2
REMARK 465 GLY E 3
REMARK 465 ASN E 4
REMARK 465 ASN E 5
REMARK 465 MET E 6
REMARK 465 SER E 7
REMARK 465 THR E 8
REMARK 465 ASP E 230
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 ARG F 0
REMARK 465 MET F 1
REMARK 465 CYS F 2
REMARK 465 GLY F 3
REMARK 465 ASN F 4
REMARK 465 ASN F 5
REMARK 465 MET F 6
REMARK 465 SER F 7
REMARK 465 THR F 8
REMARK 465 ASP F 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 322 O HOH C 343 1.87
REMARK 500 OE1 GLN C 154 O HOH C 301 1.91
REMARK 500 O HOH A 406 O HOH A 436 1.95
REMARK 500 OD1 ASN A 64 O HOH A 401 1.96
REMARK 500 O ALA C 160 O HOH C 302 2.03
REMARK 500 O HOH B 341 O HOH B 344 2.03
REMARK 500 O HOH D 522 O HOH D 524 2.03
REMARK 500 O THR C 33 O HOH C 303 2.05
REMARK 500 OE2 GLU D 214 O HOH D 501 2.06
REMARK 500 OD1 ASN F 64 O HOH F 301 2.07
REMARK 500 O ASP F 217 O HOH F 302 2.10
REMARK 500 O HOH A 435 O HOH A 437 2.14
REMARK 500 NH1 ARG A 59 O HOH A 402 2.16
REMARK 500 O ASP D 74 O HOH D 502 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 ASN B 64 52.61 -111.32
REMARK 500 SER B 119 -130.62 56.89
REMARK 500 CYS B 144 -158.39 -121.57
REMARK 500 ASN B 161 71.26 -116.57
REMARK 500 MET B 207 -139.95 -108.40
REMARK 500 SER D 119 -118.89 59.92
REMARK 500 CYS D 144 -165.81 -128.35
REMARK 500 PRO D 153 -163.16 -76.36
REMARK 500 MET D 207 -145.30 -104.29
REMARK 500 ARG A 18 -92.30 -141.17
REMARK 500 SER A 119 -119.41 53.63
REMARK 500 CYS A 144 -154.20 -132.75
REMARK 500 ASN A 161 45.34 -94.47
REMARK 500 MET A 207 -137.10 -95.50
REMARK 500 SER A 209 -157.17 -158.93
REMARK 500 ASN C 64 53.82 -103.74
REMARK 500 ASN C 66 18.96 57.95
REMARK 500 ASP C 85 86.48 -64.99
REMARK 500 SER C 119 -126.14 60.42
REMARK 500 CYS C 144 -153.57 -120.05
REMARK 500 ASN C 161 42.16 -108.13
REMARK 500 MET C 207 -147.23 -98.77
REMARK 500 SER C 209 -155.84 -160.83
REMARK 500 ARG E 18 -158.09 -102.32
REMARK 500 ASN E 66 18.12 59.86
REMARK 500 ASP E 85 101.71 -57.71
REMARK 500 ILE E 108 109.25 -57.58
REMARK 500 SER E 119 -111.89 55.78
REMARK 500 ALA E 160 -51.52 -126.98
REMARK 500 ASN E 161 39.83 -83.83
REMARK 500 LEU E 192 -50.79 -137.53
REMARK 500 MET E 207 -145.49 -101.83
REMARK 500 ASN F 111 0.93 -65.42
REMARK 500 SER F 119 -118.21 59.51
REMARK 500 CYS F 144 -156.99 -125.79
REMARK 500 MET F 207 -138.37 -98.86
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 D 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6QGQ RELATED DB: PDB
REMARK 900 RELATED ID: 6QGO RELATED DB: PDB
REMARK 900 RELATED ID: 6QGN RELATED DB: PDB
DBREF 6QGS B 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGS D 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGS A 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGS C 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGS E 1 230 UNP O75608 LYPA1_HUMAN 1 230
DBREF 6QGS F 1 230 UNP O75608 LYPA1_HUMAN 1 230
SEQADV 6QGS GLY B -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGS SER B -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGS ARG B 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGS GLY D -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGS SER D -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGS ARG D 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGS GLY A -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGS SER A -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGS ARG A 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGS GLY C -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGS SER C -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGS ARG C 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGS GLY E -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGS SER E -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGS ARG E 0 UNP O75608 EXPRESSION TAG
SEQADV 6QGS GLY F -2 UNP O75608 EXPRESSION TAG
SEQADV 6QGS SER F -1 UNP O75608 EXPRESSION TAG
SEQADV 6QGS ARG F 0 UNP O75608 EXPRESSION TAG
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 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 D 233 GLY SER ARG MET CYS 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
SEQRES 1 A 233 GLY SER ARG MET CYS 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 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 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 E 233 GLY SER ARG MET CYS GLY ASN ASN MET SER THR PRO LEU
SEQRES 2 E 233 PRO ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA
SEQRES 3 E 233 VAL ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY
SEQRES 4 E 233 TRP ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE
SEQRES 5 E 233 LYS TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR
SEQRES 6 E 233 LEU ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE
SEQRES 7 E 233 ILE GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY
SEQRES 8 E 233 ILE LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP
SEQRES 9 E 233 GLN GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE
SEQRES 10 E 233 LEU GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR
SEQRES 11 E 233 THR ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR
SEQRES 12 E 233 ALA LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO
SEQRES 13 E 233 GLN GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE
SEQRES 14 E 233 LEU GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU
SEQRES 15 E 233 MET PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU
SEQRES 16 E 233 VAL ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY
SEQRES 17 E 233 MET MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL
SEQRES 18 E 233 LYS GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
SEQRES 1 F 233 GLY SER ARG MET CYS GLY ASN ASN MET SER THR PRO LEU
SEQRES 2 F 233 PRO ALA ILE VAL PRO ALA ALA ARG LYS ALA THR ALA ALA
SEQRES 3 F 233 VAL ILE PHE LEU HIS GLY LEU GLY ASP THR GLY HIS GLY
SEQRES 4 F 233 TRP ALA GLU ALA PHE ALA GLY ILE ARG SER SER HIS ILE
SEQRES 5 F 233 LYS TYR ILE CYS PRO HIS ALA PRO VAL ARG PRO VAL THR
SEQRES 6 F 233 LEU ASN MET ASN VAL ALA MET PRO SER TRP PHE ASP ILE
SEQRES 7 F 233 ILE GLY LEU SER PRO ASP SER GLN GLU ASP GLU SER GLY
SEQRES 8 F 233 ILE LYS GLN ALA ALA GLU ASN ILE LYS ALA LEU ILE ASP
SEQRES 9 F 233 GLN GLU VAL LYS ASN GLY ILE PRO SER ASN ARG ILE ILE
SEQRES 10 F 233 LEU GLY GLY PHE SER GLN GLY GLY ALA LEU SER LEU TYR
SEQRES 11 F 233 THR ALA LEU THR THR GLN GLN LYS LEU ALA GLY VAL THR
SEQRES 12 F 233 ALA LEU SER CYS TRP LEU PRO LEU ARG ALA SER PHE PRO
SEQRES 13 F 233 GLN GLY PRO ILE GLY GLY ALA ASN ARG ASP ILE SER ILE
SEQRES 14 F 233 LEU GLN CYS HIS GLY ASP CYS ASP PRO LEU VAL PRO LEU
SEQRES 15 F 233 MET PHE GLY SER LEU THR VAL GLU LYS LEU LYS THR LEU
SEQRES 16 F 233 VAL ASN PRO ALA ASN VAL THR PHE LYS THR TYR GLU GLY
SEQRES 17 F 233 MET MET HIS SER SER CYS GLN GLN GLU MET MET ASP VAL
SEQRES 18 F 233 LYS GLN PHE ILE ASP LYS LEU LEU PRO PRO ILE ASP
HET PLM D 400 18
HET PLM A 301 18
HET CL A 302 1
HETNAM PLM PALMITIC ACID
HETNAM CL CHLORIDE ION
FORMUL 7 PLM 2(C16 H32 O2)
FORMUL 9 CL CL 1-
FORMUL 10 HOH *196(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 LYS B 105 1 21
HELIX 4 AA4 PRO B 109 ASN B 111 5 3
HELIX 5 AA5 SER 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 THR D 33 ILE D 44 1 12
HELIX 11 AB2 THR D 62 MET D 65 5 4
HELIX 12 AB3 ASP D 85 ASN D 106 1 22
HELIX 13 AB4 PRO D 109 ASN D 111 5 3
HELIX 14 AB5 SER D 119 THR D 132 1 14
HELIX 15 AB6 LEU D 148 PHE D 152 5 5
HELIX 16 AB7 GLY D 159 ILE D 164 5 6
HELIX 17 AB8 PRO D 178 VAL D 193 1 16
HELIX 18 AB9 ASN D 194 ALA D 196 5 3
HELIX 19 AC1 CYS D 211 LEU D 226 1 16
HELIX 20 AC2 THR A 33 GLY A 43 1 11
HELIX 21 AC3 ASP A 85 GLY A 107 1 23
HELIX 22 AC4 PRO A 109 ASN A 111 5 3
HELIX 23 AC5 SER A 119 THR A 132 1 14
HELIX 24 AC6 LEU A 148 PHE A 152 5 5
HELIX 25 AC7 PRO A 178 VAL A 193 1 16
HELIX 26 AC8 ASN A 194 ALA A 196 5 3
HELIX 27 AC9 CYS A 211 LEU A 226 1 16
HELIX 28 AD1 GLY C 34 GLY C 43 1 10
HELIX 29 AD2 ASP C 85 ASN C 106 1 22
HELIX 30 AD3 PRO C 109 ASN C 111 5 3
HELIX 31 AD4 SER C 119 LEU C 130 1 12
HELIX 32 AD5 LEU C 148 PHE C 152 5 5
HELIX 33 AD6 PRO C 178 VAL C 193 1 16
HELIX 34 AD7 ASN C 194 ALA C 196 5 3
HELIX 35 AD8 CYS C 211 LEU C 226 1 16
HELIX 36 AD9 GLY E 34 GLY E 43 1 10
HELIX 37 AE1 ASP E 85 ASN E 106 1 22
HELIX 38 AE2 PRO E 109 ASN E 111 5 3
HELIX 39 AE3 SER E 119 THR E 132 1 14
HELIX 40 AE4 LEU E 148 PHE E 152 5 5
HELIX 41 AE5 PRO E 178 THR E 191 1 14
HELIX 42 AE6 ASN E 194 ALA E 196 5 3
HELIX 43 AE7 CYS E 211 LEU E 226 1 16
HELIX 44 AE8 THR F 33 GLY F 43 1 11
HELIX 45 AE9 ASP F 85 LYS F 105 1 21
HELIX 46 AF1 PRO F 109 ASN F 111 5 3
HELIX 47 AF2 SER F 119 THR F 132 1 14
HELIX 48 AF3 LEU F 148 PHE F 152 5 5
HELIX 49 AF4 PRO F 178 VAL F 193 1 16
HELIX 50 AF5 ASN F 194 ALA F 196 5 3
HELIX 51 AF6 CYS F 211 LEU F 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 GLY B 116 N ILE B 25
SHEET 5 AA1 7 GLY B 138 LEU B 142 1 O LEU B 142 N GLY B 117
SHEET 6 AA1 7 SER B 165 GLY B 171 1 O LEU B 167 N VAL B 139
SHEET 7 AA1 7 VAL B 198 TYR B 203 1 O LYS B 201 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 6 ILE D 49 ILE D 52 0
SHEET 2 AA3 6 ALA D 22 LEU D 27 1 N VAL D 24 O ILE D 52
SHEET 3 AA3 6 ILE D 113 PHE D 118 1 O ILE D 114 N ILE D 25
SHEET 4 AA3 6 GLY D 138 LEU D 142 1 O LEU D 142 N GLY D 117
SHEET 5 AA3 6 SER D 165 GLY D 171 1 O LEU D 167 N VAL D 139
SHEET 6 AA3 6 VAL D 198 TYR D 203 1 O LYS D 201 N GLN D 168
SHEET 1 AA4 2 VAL D 58 PRO D 60 0
SHEET 2 AA4 2 ALA D 68 PRO D 70 -1 O MET D 69 N ARG D 59
SHEET 1 AA5 7 ALA A 12 VAL A 14 0
SHEET 2 AA5 7 ILE A 49 CYS A 53 -1 O CYS A 53 N ALA A 12
SHEET 3 AA5 7 ALA A 22 LEU A 27 1 N VAL A 24 O ILE A 52
SHEET 4 AA5 7 ILE A 113 PHE A 118 1 O GLY A 116 N ILE A 25
SHEET 5 AA5 7 GLY A 138 LEU A 142 1 O LEU A 142 N GLY A 117
SHEET 6 AA5 7 SER A 165 GLY A 171 1 O LEU A 167 N ALA A 141
SHEET 7 AA5 7 VAL A 198 TYR A 203 1 O THR A 199 N ILE A 166
SHEET 1 AA6 2 VAL A 58 PRO A 60 0
SHEET 2 AA6 2 ALA A 68 PRO A 70 -1 O MET A 69 N ARG A 59
SHEET 1 AA7 7 ALA C 12 VAL C 14 0
SHEET 2 AA7 7 ILE C 49 CYS C 53 -1 O CYS C 53 N ALA C 12
SHEET 3 AA7 7 ALA C 22 LEU C 27 1 N VAL C 24 O ILE C 52
SHEET 4 AA7 7 ILE C 113 PHE C 118 1 O ILE C 114 N ILE C 25
SHEET 5 AA7 7 GLY C 138 LEU C 142 1 O GLY C 138 N LEU C 115
SHEET 6 AA7 7 SER C 165 GLY C 171 1 O LEU C 167 N VAL C 139
SHEET 7 AA7 7 VAL C 198 TYR C 203 1 O LYS C 201 N GLN C 168
SHEET 1 AA8 2 VAL C 58 VAL C 61 0
SHEET 2 AA8 2 VAL C 67 PRO C 70 -1 O MET C 69 N ARG C 59
SHEET 1 AA9 7 ALA E 12 VAL E 14 0
SHEET 2 AA9 7 ILE E 49 CYS E 53 -1 O CYS E 53 N ALA E 12
SHEET 3 AA9 7 ALA E 22 LEU E 27 1 N VAL E 24 O ILE E 52
SHEET 4 AA9 7 ILE E 113 PHE E 118 1 O GLY E 116 N ILE E 25
SHEET 5 AA9 7 GLY E 138 LEU E 142 1 O LEU E 142 N GLY E 117
SHEET 6 AA9 7 SER E 165 GLY E 171 1 O LEU E 167 N ALA E 141
SHEET 7 AA9 7 VAL E 198 TYR E 203 1 O THR E 199 N GLN E 168
SHEET 1 AB1 2 VAL E 58 PRO E 60 0
SHEET 2 AB1 2 ALA E 68 PRO E 70 -1 O MET E 69 N ARG E 59
SHEET 1 AB2 7 ALA F 12 VAL F 14 0
SHEET 2 AB2 7 ILE F 49 CYS F 53 -1 O TYR F 51 N VAL F 14
SHEET 3 AB2 7 ALA F 22 LEU F 27 1 N VAL F 24 O ILE F 52
SHEET 4 AB2 7 ILE F 113 PHE F 118 1 O GLY F 116 N ILE F 25
SHEET 5 AB2 7 GLY F 138 LEU F 142 1 O LEU F 142 N GLY F 117
SHEET 6 AB2 7 SER F 165 GLY F 171 1 O LEU F 167 N ALA F 141
SHEET 7 AB2 7 VAL F 198 TYR F 203 1 O THR F 199 N GLN F 168
SHEET 1 AB3 2 VAL F 58 PRO F 60 0
SHEET 2 AB3 2 ALA F 68 PRO F 70 -1 O MET F 69 N ARG F 59
SITE 1 AC1 8 LEU D 30 LEU D 78 SER D 119 GLN D 120
SITE 2 AC1 8 TRP D 145 LEU D 184 HIS D 208 ASN E 64
SITE 1 AC2 11 LEU A 30 GLY A 77 SER A 79 SER A 119
SITE 2 AC2 11 GLN A 120 TRP A 145 ARG A 149 VAL A 177
SITE 3 AC2 11 PHE A 181 LEU A 184 THR A 185
SITE 1 AC3 1 ALA A 16
CRYST1 81.660 81.660 441.946 90.00 90.00 90.00 P 41 21 2 48
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 0.012246 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012246 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002263 0.00000
TER 1693 ILE B 229
TER 3357 ILE D 229
TER 5021 ILE A 229
TER 6685 ILE C 229
TER 8349 ILE E 229
TER 10013 ILE F 229
MASTER 433 0 3 51 53 0 6 610240 6 36 108
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