HEADER LIPID BINDING PROTEIN 25-JUL-05 2AF9
TITLE CRYSTAL STRUCTURE ANALYSIS OF GM2-ACTIVATOR PROTEIN COMPLEXED WITH
TITLE 2 PHOSPHATIDYLCHOLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GANGLIOSIDE GM2 ACTIVATOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GM2-AP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER, BRAIN, NEURONS;
SOURCE 6 GENE: GM2A;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET16B (NOVAGEN)
KEYWDS LIPID-PROTEIN COMPLEX, LIPID ACYL CHAIN STACKING, LIPID BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.WRIGHT,L.Z.MI,S.LEE,F.RASTINEJAD
REVDAT 3 23-AUG-23 2AF9 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2AF9 1 VERSN
REVDAT 1 25-OCT-05 2AF9 0
JRNL AUTH C.S.WRIGHT,L.Z.MI,S.LEE,F.RASTINEJAD
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF
JRNL TITL 2 PHOSPHATIDYLCHOLINE-GM2-ACTIVATOR PRODUCT COMPLEXES:
JRNL TITL 3 EVIDENCE FOR HYDROLASE ACTIVITY.
JRNL REF BIOCHEMISTRY V. 44 13510 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16216074
JRNL DOI 10.1021/BI050668W
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.S.WRIGHT,S.C.LI,F.RASTINEJAD
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN GM2- ACTIVATOR PROTEIN WITH A
REMARK 1 TITL 2 NOVEL BETA-CUP TOPOLOGY
REMARK 1 REF J.MOL.BIOL. V. 304 411 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 11090283
REMARK 1 DOI 10.1006/JMBI.2000.4225
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.S.WRIGHT,Q.ZHAO,F.RASTINEJAD
REMARK 1 TITL STRUCTURE ANALYSIS OF LIPID COMPLEXES OF GM2-ACTIVATOR
REMARK 1 TITL 2 PROTEIN
REMARK 1 REF J.MOL.BIOL. V. 331 951 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 12909021
REMARK 1 DOI 10.1016/S0022-2836(03)00794-0
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.S.WRIGHT,L.Z.MI,F.RASTINEJAD
REMARK 1 TITL EVIDENCE FOR LIPID PACKAGING IN THE CRYSTAL STRUCTURE OF THE
REMARK 1 TITL 2 GM2-ACTIVATOR COMPLEX WITH PLATELET ACTIVATING FACTOR
REMARK 1 REF J.MOL.BIOL. V. 342 585 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1020095.170
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 12607
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) : 0.222
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1020
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1994
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 169
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1235
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 115
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 0.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.02
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.02
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.110
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.990 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.870 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 9.750 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.380 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 85.19
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : SOLVENT_REP.PARAM
REMARK 3 PARAMETER FILE 4 : LPC_OLA_MYR_LAU_EPE.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : SOLVENT.TOP
REMARK 3 TOPOLOGY FILE 4 : LPC_OLA_MYR_LAU_EPE.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97943
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13297
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.29200
REMARK 200 R SYM FOR SHELL (I) : 0.29200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1PUB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISO-PROPANOL, HEPES, PH 5.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K
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 19.56000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.10500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.99000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.10500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.56000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.99000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 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 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 HIS A -1
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 MET A 0 CG SD CE
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 THR A 90 CB OG1 CG2
REMARK 480 LYS A 110 CD CE NZ
REMARK 480 GLU A 111 CG CD OE1 OE2
REMARK 480 ASP A 125 CG OD1 OD2
REMARK 480 LEU A 126 CG CD1 CD2
REMARK 480 GLU A 127 CB CG CD OE1 OE2
REMARK 480 LYS A 160 NZ
REMARK 480 ILE A 162 CB CG1 CG2 CD1 OXT
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 O HOH A 3651 O HOH A 3679 3655 2.05
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 TYR A 71 -1.05 77.58
REMARK 500 CYS A 105 25.08 -143.77
REMARK 500 LEU A 126 -17.99 65.01
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 OLA A 3629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 3045
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAO A 1364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAO A 1365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 1510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 1511
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TJJ RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH PLATELET ACTIVATING FACTOR (PAF)
REMARK 900 RELATED ID: 1PUB RELATED DB: PDB
REMARK 900 APO-PROTEIN STRUCTURE OF CRYTALS GROWN AT PH 5.5
REMARK 900 RELATED ID: 1PU5 RELATED DB: PDB
REMARK 900 SAME PROTEIN CO-CRYSTALLIZED WITH GM2 GANGLIOSIDE
REMARK 900 RELATED ID: 1G13 RELATED DB: PDB
REMARK 900 APO-PROTEIN STRUCTURE OF CRYSTALS GROWN AT PH 7.9
DBREF 2AF9 A 1 162 UNP P17900 SAP3_HUMAN 32 193
SEQADV 2AF9 HIS A -1 UNP P17900 CLONING ARTIFACT
SEQADV 2AF9 MET A 0 UNP P17900 CLONING ARTIFACT
SEQRES 1 A 164 HIS MET SER SER PHE SER TRP ASP ASN CYS ASP GLU GLY
SEQRES 2 A 164 LYS ASP PRO ALA VAL ILE ARG SER LEU THR LEU GLU PRO
SEQRES 3 A 164 ASP PRO ILE VAL VAL PRO GLY ASN VAL THR LEU SER VAL
SEQRES 4 A 164 VAL GLY SER THR SER VAL PRO LEU SER SER PRO LEU LYS
SEQRES 5 A 164 VAL ASP LEU VAL LEU GLU LYS GLU VAL ALA GLY LEU TRP
SEQRES 6 A 164 ILE LYS ILE PRO CYS THR ASP TYR ILE GLY SER CYS THR
SEQRES 7 A 164 PHE GLU HIS PHE CYS ASP VAL LEU ASP MET LEU ILE PRO
SEQRES 8 A 164 THR GLY GLU PRO CYS PRO GLU PRO LEU ARG THR TYR GLY
SEQRES 9 A 164 LEU PRO CYS HIS CYS PRO PHE LYS GLU GLY THR TYR SER
SEQRES 10 A 164 LEU PRO LYS SER GLU PHE VAL VAL PRO ASP LEU GLU LEU
SEQRES 11 A 164 PRO SER TRP LEU THR THR GLY ASN TYR ARG ILE GLU SER
SEQRES 12 A 164 VAL LEU SER SER SER GLY LYS ARG LEU GLY CYS ILE LYS
SEQRES 13 A 164 ILE ALA ALA SER LEU LYS GLY ILE
HET OLA A3629 20
HET MYR A3045 16
HET DAO A1364 14
HET DAO A1365 14
HET IPA A1510 4
HET IPA A1511 4
HETNAM OLA OLEIC ACID
HETNAM MYR MYRISTIC ACID
HETNAM DAO LAURIC ACID
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 OLA C18 H34 O2
FORMUL 3 MYR C14 H28 O2
FORMUL 4 DAO 2(C12 H24 O2)
FORMUL 6 IPA 2(C3 H8 O)
FORMUL 8 HOH *115(H2 O)
HELIX 1 1 ASP A 9 LYS A 12 5 4
HELIX 2 2 HIS A 79 ILE A 88 1 10
HELIX 3 3 PRO A 129 THR A 134 1 6
SHEET 1 A 5 SER A 4 ASN A 7 0
SHEET 2 A 5 LYS A 148 GLY A 161 -1 O LYS A 154 N ASP A 6
SHEET 3 A 5 GLY A 135 SER A 145 -1 N ILE A 139 O ILE A 155
SHEET 4 A 5 LYS A 50 VAL A 59 -1 N LYS A 50 O SER A 144
SHEET 5 A 5 LEU A 62 LYS A 65 -1 O ILE A 64 N LYS A 57
SHEET 1 B 5 ILE A 27 VAL A 29 0
SHEET 2 B 5 LYS A 148 GLY A 161 1 O LYS A 160 N VAL A 29
SHEET 3 B 5 GLY A 135 SER A 145 -1 N ILE A 139 O ILE A 155
SHEET 4 B 5 LYS A 50 VAL A 59 -1 N LYS A 50 O SER A 144
SHEET 5 B 5 THR A 76 PHE A 77 -1 O PHE A 77 N VAL A 51
SHEET 1 C 3 ALA A 15 GLU A 23 0
SHEET 2 C 3 GLY A 31 THR A 41 -1 O VAL A 38 N ARG A 18
SHEET 3 C 3 GLY A 112 VAL A 123 -1 O TYR A 114 N GLY A 39
SSBOND 1 CYS A 8 CYS A 152 1555 1555 2.04
SSBOND 2 CYS A 68 CYS A 75 1555 1555 2.04
SSBOND 3 CYS A 81 CYS A 107 1555 1555 2.03
SSBOND 4 CYS A 94 CYS A 105 1555 1555 2.03
CISPEP 1 GLU A 23 PRO A 24 0 -0.16
CISPEP 2 ASP A 25 PRO A 26 0 0.03
CISPEP 3 VAL A 29 PRO A 30 0 -0.12
CISPEP 4 SER A 47 PRO A 48 0 0.13
CISPEP 5 GLU A 96 PRO A 97 0 -0.10
CISPEP 6 CYS A 107 PRO A 108 0 -0.01
SITE 1 AC1 10 ALA A 15 PHE A 109 TYR A 114 SER A 141
SITE 2 AC1 10 LEU A 143 GLY A 151 CYS A 152 ILE A 153
SITE 3 AC1 10 DAO A1364 HOH A3732
SITE 1 AC2 4 ILE A 27 VAL A 33 LEU A 128 THR A 133
SITE 1 AC3 8 VAL A 51 PHE A 80 PHE A 109 ILE A 139
SITE 2 AC3 8 SER A 141 ILE A 153 ILE A 155 OLA A3629
SITE 1 AC4 6 LYS A 57 LEU A 132 TYR A 137 ILE A 155
SITE 2 AC4 6 ALA A 157 LEU A 159
SITE 1 AC5 2 IPA A1511 HOH A3742
SITE 1 AC6 3 LEU A 22 ILE A 155 IPA A1510
CRYST1 39.120 41.980 114.210 90.00 90.00 90.00 P 21 21 21 4
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 0.025562 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023821 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008756 0.00000
(ATOM LINES ARE NOT SHOWN.)
END