HEADER LIPID BINDING PROTEIN 24-OCT-16 5H3G
TITLE CRYSTAL STRUCTURE OF ORYZA SATIVA ACYL-COA-BINDING PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACYL-COA BINDING PROTEIN (ACBP);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYL-COA-BINDING PROTEIN 1,OS08G0162800 PROTEIN,CDNA
COMPND 5 CLONE:001-027-C02,FULL INSERT SEQUENCE,CDNA CLONE:J033115J15;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYZA SATIVA JAPONICA GROUP;
SOURCE 3 ORGANISM_COMMON: RICE;
SOURCE 4 ORGANISM_TAXID: 39947;
SOURCE 5 GENE: P0577B11.140, OJ9990_A01.106, OS08G0162800, OSJ_26146;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACYL-COA-BINDING DOMAIN, RICE, ORYZA SATIVA, ACB, LIPID BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.K.W.KONG,W.H.Y.CHAN
REVDAT 2 08-NOV-23 5H3G 1 REMARK
REVDAT 1 17-MAY-17 5H3G 0
JRNL AUTH Z.-H.GUO,W.H.Y.CHAN,G.K.W.KONG,Q.HAO,M.-L.CHYE
JRNL TITL THE FIRST PLANT ACYL-COA-BINDING PROTEIN STRUCTURES: THE
JRNL TITL 2 CLOSE HOMOLOGUES OSACBP1 AND OSACBP2 FROM RICE
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 73 438 2017
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 28471368
JRNL DOI 10.1107/S2059798317004193
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 15626
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 790
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 39.3691 - 2.9077 0.97 2726 137 0.1651 0.2157
REMARK 3 2 2.9077 - 2.3080 1.00 2677 134 0.1892 0.2343
REMARK 3 3 2.3080 - 2.0163 0.99 2626 153 0.1906 0.2297
REMARK 3 4 2.0163 - 1.8319 0.99 2637 126 0.2236 0.2219
REMARK 3 5 1.8319 - 1.7006 0.98 2580 136 0.2436 0.3012
REMARK 3 6 1.7006 - 1.6003 0.61 1590 104 0.2538 0.2908
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.66
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 : 0.005 793
REMARK 3 ANGLE : 0.771 1069
REMARK 3 CHIRALITY : 0.041 115
REMARK 3 PLANARITY : 0.004 136
REMARK 3 DIHEDRAL : 14.078 498
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND (RESID -1:16 OR RESID 102:102 OR RESID
REMARK 3 105:106) )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1256 23.7197 0.9470
REMARK 3 T TENSOR
REMARK 3 T11: 0.1518 T22: 0.2696
REMARK 3 T33: 0.1255 T12: -0.0479
REMARK 3 T13: 0.0002 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 4.0419 L22: 2.7744
REMARK 3 L33: 5.4044 L12: -1.6964
REMARK 3 L13: 3.4334 L23: -1.8988
REMARK 3 S TENSOR
REMARK 3 S11: -0.0553 S12: 0.3983 S13: 0.2046
REMARK 3 S21: -0.0670 S22: -0.0083 S23: -0.1945
REMARK 3 S31: -0.4188 S32: 0.2072 S33: 0.0023
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND (RESID 17:38 OR RESID 319:338) )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0948 9.9036 6.0037
REMARK 3 T TENSOR
REMARK 3 T11: 0.0206 T22: 0.2550
REMARK 3 T33: 0.1187 T12: -0.0094
REMARK 3 T13: 0.0073 T23: -0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 1.6680 L22: 1.0730
REMARK 3 L33: 2.0485 L12: 0.2595
REMARK 3 L13: 0.6971 L23: 0.1863
REMARK 3 S TENSOR
REMARK 3 S11: 0.0488 S12: 0.0550 S13: -0.0722
REMARK 3 S21: 0.0573 S22: -0.0772 S23: -0.0894
REMARK 3 S31: 0.1833 S32: -0.0830 S33: 0.0367
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND (RESID 39:67 OR RESID 202:318) )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.398 3.901 -0.583
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.3200
REMARK 3 T33: 0.1309 T12: -0.0007
REMARK 3 T13: -0.0311 T23: -0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 1.2835 L22: 3.4104
REMARK 3 L33: 0.9786 L12: -0.9961
REMARK 3 L13: 0.3131 L23: -1.0093
REMARK 3 S TENSOR
REMARK 3 S11: 0.1141 S12: 0.2116 S13: -0.1028
REMARK 3 S21: -0.5477 S22: -0.1981 S23: 0.2434
REMARK 3 S31: 0.3059 S32: 0.0015 S33: 0.0284
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND (RESID 68:91 OR RESID 107:107) )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5994 18.6072 7.9084
REMARK 3 T TENSOR
REMARK 3 T11: -0.0017 T22: 0.3427
REMARK 3 T33: 0.1463 T12: 0.0126
REMARK 3 T13: 0.0121 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 1.4399 L22: 1.1144
REMARK 3 L33: 0.4789 L12: 0.1947
REMARK 3 L13: 0.6973 L23: -0.2921
REMARK 3 S TENSOR
REMARK 3 S11: 0.1269 S12: 0.2812 S13: -0.0246
REMARK 3 S21: 0.1603 S22: -0.0368 S23: 0.1535
REMARK 3 S31: -0.0704 S32: -0.4198 S33: 0.0201
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 5H3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9900
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20012
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 39.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 21.67
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 2.64200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 2FJ9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRIC ACID, 2.6M NACL, PH 3.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 40.48000
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 20.24000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 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 20.24000
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 40.48000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 267 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 306 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 338 LIES ON A SPECIAL POSITION.
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 TRP A -2
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 271 O HOH A 301 2.06
REMARK 500 O HOH A 238 O HOH A 301 2.10
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 OG SER A 73 OG SER A 73 4555 2.12
REMARK 500 O HOH A 226 O HOH A 270 2654 2.13
REMARK 500 O HOH A 275 O HOH A 299 4545 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 338 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 339 DISTANCE = 7.17 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 107
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H3I RELATED DB: PDB
DBREF 5H3G A 1 91 UNP Q84SC3 Q84SC3_ORYSJ 1 91
SEQADV 5H3G TRP A -2 UNP Q84SC3 EXPRESSION TAG
SEQADV 5H3G GLY A -1 UNP Q84SC3 EXPRESSION TAG
SEQADV 5H3G SER A 0 UNP Q84SC3 EXPRESSION TAG
SEQRES 1 A 94 TRP GLY SER MET GLY LEU GLN GLU ASP PHE GLU GLN TYR
SEQRES 2 A 94 ALA GLU LYS ALA LYS THR LEU PRO GLU SER THR SER ASN
SEQRES 3 A 94 GLU ASN LYS LEU ILE LEU TYR GLY LEU TYR LYS GLN ALA
SEQRES 4 A 94 THR VAL GLY ASP VAL ASN THR ALA ARG PRO GLY ILE PHE
SEQRES 5 A 94 ALA GLN ARG ASP ARG ALA LYS TRP ASP ALA TRP LYS ALA
SEQRES 6 A 94 VAL GLU GLY LYS SER LYS GLU GLU ALA MET SER ASP TYR
SEQRES 7 A 94 ILE THR LYS VAL LYS GLN LEU LEU GLU GLU ALA ALA ALA
SEQRES 8 A 94 ALA ALA SER
HET CL A 101 1
HET CL A 102 1
HET CL A 103 1
HET GOL A 104 6
HET GOL A 105 6
HET GOL A 106 6
HET GOL A 107 6
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CL 3(CL 1-)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *139(H2 O)
HELIX 1 AA1 SER A 0 LYS A 15 1 16
HELIX 2 AA2 SER A 22 GLY A 39 1 18
HELIX 3 AA3 ASP A 53 ALA A 62 1 10
HELIX 4 AA4 SER A 67 ALA A 90 1 24
SITE 1 AC1 5 SER A 22 ASN A 23 ASP A 53 ARG A 54
SITE 2 AC1 5 ALA A 55
SITE 1 AC2 3 MET A 1 TYR A 10 LYS A 80
SITE 1 AC3 3 LYS A 13 LYS A 34 LYS A 80
SITE 1 AC4 3 THR A 77 LYS A 80 GLU A 84
SITE 1 AC5 6 THR A 16 PRO A 18 HOH A 201 HOH A 204
SITE 2 AC5 6 HOH A 230 HOH A 253
SITE 1 AC6 4 GLY A -1 LYS A 80 GOL A 107 HOH A 266
SITE 1 AC7 8 GLY A -1 SER A 67 LYS A 68 GOL A 106
SITE 2 AC7 8 HOH A 207 HOH A 208 HOH A 238 HOH A 257
CRYST1 59.680 59.680 60.720 90.00 90.00 120.00 P 32 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 0.016756 0.009674 0.000000 0.00000
SCALE2 0.000000 0.019348 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
