HEADER MEMBRANE PROTEIN 20-OCT-16 5H36
TITLE CRYSTAL STRUCTURES OF THE TRIC TRIMERIC INTRACELLULAR CATION CHANNEL
TITLE 2 ORTHOLOGUE FROM RHODOBACTER SPHAEROIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN TRIC;
COMPND 3 CHAIN: E, A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-204;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES (STRAIN ATCC 17023 /
SOURCE 3 2.4.1 / NCIB 8253 / DSM 158);
SOURCE 4 ORGANISM_TAXID: 272943;
SOURCE 5 STRAIN: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
SOURCE 6 GENE: RSP_3856;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ION CHANNELS, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.KASUYA,M.HIRAIZUMI,M.HATTORI,O.NUREKI
REVDAT 2 20-MAR-24 5H36 1 REMARK
REVDAT 1 11-JAN-17 5H36 0
JRNL AUTH G.KASUYA,M.HIRAIZUMI,A.D.MATURANA,K.KUMAZAKI,Y.FUJIWARA,
JRNL AUTH 2 K.LIU,Y.NAKADA-NAKURA,S.IWATA,K.TSUKADA,T.KOMORI,S.UEMURA,
JRNL AUTH 3 Y.GOTO,T.NAKANE,M.TAKEMOTO,H.E.KATO,K.YAMASHITA,M.WADA,
JRNL AUTH 4 K.ITO,R.ISHITANI,M.HATTORI,O.NUREKI
JRNL TITL CRYSTAL STRUCTURES OF THE TRIC TRIMERIC INTRACELLULAR CATION
JRNL TITL 2 CHANNEL ORTHOLOGUES
JRNL REF CELL RES. V. 26 1288 2016
JRNL REFN ISSN 1748-7838
JRNL PMID 27909292
JRNL DOI 10.1038/CR.2016.140
REMARK 2
REMARK 2 RESOLUTION. 3.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 3.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 9730
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.263
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.940
REMARK 3 FREE R VALUE TEST SET COUNT : 967
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 43.4056 - 6.5451 0.90 1290 145 0.2585 0.2699
REMARK 3 2 6.5451 - 5.1978 0.90 1290 142 0.2661 0.2534
REMARK 3 3 5.1978 - 4.5416 0.90 1301 140 0.2659 0.2434
REMARK 3 4 4.5416 - 4.1267 0.90 1287 143 0.2628 0.2973
REMARK 3 5 4.1267 - 3.8311 0.90 1296 143 0.2615 0.3167
REMARK 3 6 3.8311 - 3.6053 0.90 1283 142 0.2466 0.3288
REMARK 3 7 3.6053 - 3.4249 0.70 1001 112 0.2535 0.3134
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.530
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 : 0.004 2880
REMARK 3 ANGLE : 0.960 3919
REMARK 3 CHIRALITY : 0.031 474
REMARK 3 PLANARITY : 0.003 487
REMARK 3 DIHEDRAL : 14.692 950
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 5H36 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1300001922.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-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 : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9730
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.409
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-32% (V/V) PEG 400, 20-70MM LI2SO4,
REMARK 280 20-70MM NA2SO4, 50MM TRIS-HCL, PH 8.0, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 78.00500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 45.03621
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.45667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 78.00500
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 45.03621
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 27.45667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 78.00500
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 45.03621
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 27.45667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.07242
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 54.91333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 90.07242
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 54.91333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 90.07242
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 54.91333
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 MET E 1
REMARK 465 PHE E 2
REMARK 465 SER E 197
REMARK 465 LEU E 198
REMARK 465 PRO E 199
REMARK 465 ARG E 200
REMARK 465 TYR E 201
REMARK 465 ARG E 202
REMARK 465 ALA E 203
REMARK 465 ARG E 204
REMARK 465 LEU E 205
REMARK 465 GLU E 206
REMARK 465 SER E 207
REMARK 465 SER E 208
REMARK 465 GLY E 209
REMARK 465 GLU E 210
REMARK 465 ASN E 211
REMARK 465 LEU E 212
REMARK 465 TYR E 213
REMARK 465 PHE E 214
REMARK 465 GLN E 215
REMARK 465 MET A 1
REMARK 465 PHE A 2
REMARK 465 GLN A 3
REMARK 465 SER A 197
REMARK 465 LEU A 198
REMARK 465 PRO A 199
REMARK 465 ARG A 200
REMARK 465 TYR A 201
REMARK 465 ARG A 202
REMARK 465 ALA A 203
REMARK 465 ARG A 204
REMARK 465 LEU A 205
REMARK 465 GLU A 206
REMARK 465 SER A 207
REMARK 465 SER A 208
REMARK 465 GLY A 209
REMARK 465 GLU A 210
REMARK 465 ASN A 211
REMARK 465 LEU A 212
REMARK 465 TYR A 213
REMARK 465 PHE A 214
REMARK 465 GLN A 215
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 HIS E 83 CG ND1 CD2 CE1 NE2
REMARK 470 SER E 87 OG
REMARK 470 ARG E 90 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 174 CG CD OE1 OE2
REMARK 470 LEU E 196 CG CD1 CD2
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 83 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 113 CG CD OE1 NE2
REMARK 470 THR A 114 OG1 CG2
REMARK 470 ASP A 167 CG OD1 OD2
REMARK 470 LEU A 192 CD1 CD2
REMARK 470 VAL A 193 CG2
REMARK 470 TRP A 194 CD1 CD2 NE1 CE2 CE3 CZ2 CZ3
REMARK 470 TRP A 194 CH2
REMARK 470 LEU A 196 CG CD1 CD2
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 OD2 ASP A 10 NH1 ARG A 110 2.13
REMARK 500 O PHE E 17 OG1 THR E 20 2.18
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 GLU E 150 -5.26 -146.05
REMARK 500 GLU A 150 -2.77 -147.25
REMARK 500 PRO A 172 -160.36 -76.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PX4 E 301
REMARK 610 PX4 A 301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PX4 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5H35 RELATED DB: PDB
DBREF 5H36 E 1 204 UNP Q3HKN0 Q3HKN0_RHOS4 1 204
DBREF 5H36 A 1 204 UNP Q3HKN0 Q3HKN0_RHOS4 1 204
SEQADV 5H36 LEU E 205 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLU E 206 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 SER E 207 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 SER E 208 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLY E 209 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLU E 210 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 ASN E 211 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 LEU E 212 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 TYR E 213 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 PHE E 214 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLN E 215 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 LEU A 205 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLU A 206 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 SER A 207 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 SER A 208 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLY A 209 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLU A 210 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 ASN A 211 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 LEU A 212 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 TYR A 213 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 PHE A 214 UNP Q3HKN0 EXPRESSION TAG
SEQADV 5H36 GLN A 215 UNP Q3HKN0 EXPRESSION TAG
SEQRES 1 E 215 MET PHE GLN THR VAL THR ILE LEU LEU ASP TRP PHE GLY
SEQRES 2 E 215 LEU CYS ILE PHE THR VAL THR GLY ALA LEU VAL ALA SER
SEQRES 3 E 215 ARG LYS GLU MET ASP ILE ALA GLY PHE VAL LEU LEU GLY
SEQRES 4 E 215 ALA VAL THR GLY VAL GLY GLY GLY THR ILE ARG ASP LEU
SEQRES 5 E 215 VAL LEU GLY ARG THR PRO VAL PHE TRP VAL GLU GLU PRO
SEQRES 6 E 215 ALA TYR VAL LEU ALA CYS LEU GLY VAL ALA VAL PHE THR
SEQRES 7 E 215 PHE PHE PHE ALA HIS ILE PRO GLN SER ARG TYR ARG PHE
SEQRES 8 E 215 LEU LEU TRP LEU ASP ALA VAL GLY LEU SER LEU PHE ALA
SEQRES 9 E 215 VAL THR GLY ALA GLU ARG ALA LEU GLN THR GLY ALA GLY
SEQRES 10 E 215 PRO VAL ILE ALA ILE ALA MET GLY VAL ALA THR ALA THR
SEQRES 11 E 215 PHE GLY GLY ILE LEU ARG ASP LEU LEU GLY GLY GLU SER
SEQRES 12 E 215 PRO VAL ILE LEU ARG ARG GLU ILE TYR ILE THR ALA ALA
SEQRES 13 E 215 LEU LEU GLY ALA ALA ALA PHE VAL ALA LEU ASP ALA PHE
SEQRES 14 E 215 GLY ALA PRO ARG GLU LEU ALA LEU GLY ALA GLY PHE ALA
SEQRES 15 E 215 ALA ALA PHE LEU SER ARG ALA ALA GLY LEU VAL TRP GLY
SEQRES 16 E 215 LEU SER LEU PRO ARG TYR ARG ALA ARG LEU GLU SER SER
SEQRES 17 E 215 GLY GLU ASN LEU TYR PHE GLN
SEQRES 1 A 215 MET PHE GLN THR VAL THR ILE LEU LEU ASP TRP PHE GLY
SEQRES 2 A 215 LEU CYS ILE PHE THR VAL THR GLY ALA LEU VAL ALA SER
SEQRES 3 A 215 ARG LYS GLU MET ASP ILE ALA GLY PHE VAL LEU LEU GLY
SEQRES 4 A 215 ALA VAL THR GLY VAL GLY GLY GLY THR ILE ARG ASP LEU
SEQRES 5 A 215 VAL LEU GLY ARG THR PRO VAL PHE TRP VAL GLU GLU PRO
SEQRES 6 A 215 ALA TYR VAL LEU ALA CYS LEU GLY VAL ALA VAL PHE THR
SEQRES 7 A 215 PHE PHE PHE ALA HIS ILE PRO GLN SER ARG TYR ARG PHE
SEQRES 8 A 215 LEU LEU TRP LEU ASP ALA VAL GLY LEU SER LEU PHE ALA
SEQRES 9 A 215 VAL THR GLY ALA GLU ARG ALA LEU GLN THR GLY ALA GLY
SEQRES 10 A 215 PRO VAL ILE ALA ILE ALA MET GLY VAL ALA THR ALA THR
SEQRES 11 A 215 PHE GLY GLY ILE LEU ARG ASP LEU LEU GLY GLY GLU SER
SEQRES 12 A 215 PRO VAL ILE LEU ARG ARG GLU ILE TYR ILE THR ALA ALA
SEQRES 13 A 215 LEU LEU GLY ALA ALA ALA PHE VAL ALA LEU ASP ALA PHE
SEQRES 14 A 215 GLY ALA PRO ARG GLU LEU ALA LEU GLY ALA GLY PHE ALA
SEQRES 15 A 215 ALA ALA PHE LEU SER ARG ALA ALA GLY LEU VAL TRP GLY
SEQRES 16 A 215 LEU SER LEU PRO ARG TYR ARG ALA ARG LEU GLU SER SER
SEQRES 17 A 215 GLY GLU ASN LEU TYR PHE GLN
HET PX4 E 301 14
HET PX4 A 301 14
HETNAM PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
FORMUL 3 PX4 2(C36 H73 N O8 P 1+)
HELIX 1 AA1 THR E 4 LYS E 28 1 25
HELIX 2 AA2 ASP E 31 GLY E 55 1 25
HELIX 3 AA3 VAL E 59 GLU E 64 1 6
HELIX 4 AA4 PRO E 65 ALA E 82 1 18
HELIX 5 AA5 SER E 87 GLN E 113 1 27
HELIX 6 AA6 GLY E 117 GLY E 141 1 25
HELIX 7 AA7 PRO E 144 ARG E 148 5 5
HELIX 8 AA8 ILE E 151 PHE E 169 1 19
HELIX 9 AA9 PRO E 172 GLY E 195 1 24
HELIX 10 AB1 VAL A 5 LYS A 28 1 24
HELIX 11 AB2 ASP A 31 GLY A 55 1 25
HELIX 12 AB3 VAL A 59 GLU A 64 1 6
HELIX 13 AB4 PRO A 65 ALA A 82 1 18
HELIX 14 AB5 SER A 87 THR A 114 1 28
HELIX 15 AB6 GLY A 117 GLY A 141 1 25
HELIX 16 AB7 PRO A 144 ARG A 148 5 5
HELIX 17 AB8 ILE A 151 PHE A 169 1 19
HELIX 18 AB9 PRO A 172 LEU A 192 1 21
CISPEP 1 THR E 57 PRO E 58 0 -1.02
CISPEP 2 GLN E 86 SER E 87 0 5.90
CISPEP 3 ARG E 149 GLU E 150 0 5.31
CISPEP 4 THR A 57 PRO A 58 0 -0.86
CISPEP 5 GLN A 86 SER A 87 0 5.38
CISPEP 6 THR A 114 GLY A 115 0 -3.11
CISPEP 7 ARG A 149 GLU A 150 0 3.70
CISPEP 8 ALA A 171 PRO A 172 0 -4.79
SITE 1 AC1 5 VAL E 36 ALA E 40 THR E 48 PHE E 131
SITE 2 AC1 5 LEU E 135
SITE 1 AC2 2 VAL A 36 ALA A 40
CRYST1 156.010 156.010 82.370 90.00 90.00 120.00 H 3 18
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 0.006410 0.003701 0.000000 0.00000
SCALE2 0.000000 0.007401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012140 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
