HEADER OXIDOREDUCTASE 03-SEP-16 5GV7
TITLE STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE REFINED WITH THE MULTIPOLAR
TITLE 2 ATOMIC MODEL AT 0.80 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADH-CYTOCHROME B5 REDUCTASE 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOCHROME B5 REDUCTASE,DIAPHORASE-1;
COMPND 5 EC: 1.6.2.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: CYB5R3, DIA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, ELECTRON TRANSFER, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAKABA,K.TAKEDA,K.MIKI
REVDAT 3 08-NOV-23 5GV7 1 REMARK
REVDAT 2 19-JUL-17 5GV7 1 REMARK
REVDAT 1 05-APR-17 5GV7 0
JRNL AUTH K.TAKABA,K.TAKEDA,M.KOSUGI,T.TAMADA,K.MIKI
JRNL TITL DISTRIBUTION OF VALENCE ELECTRONS OF THE FLAVIN COFACTOR IN
JRNL TITL 2 NADH-CYTOCHROME B5 REDUCTASE.
JRNL REF SCI REP V. 7 43162 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28225078
JRNL DOI 10.1038/SREP43162
REMARK 2
REMARK 2 RESOLUTION. 0.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM SELECTION
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.122
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.144
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 15874
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2149
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 77
REMARK 3 SOLVENT ATOMS : 616
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 ANGLE DISTANCES (A) : NULL
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : NULL
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE MODEL WAS FINALLY REFINED WITH
REMARK 3 ASPHERICAL ATOMIC MODEL BY USING MOPRO PROGRAM.
REMARK 4
REMARK 4 5GV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001516.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 40
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.65
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 314475
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.800
REMARK 200 RESOLUTION RANGE LOW (A) : 29.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1NDH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, DTT, K-PHOS BUFFER, PH 7.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K
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 24.33200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.60450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.08850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.60450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.33200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.08850
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 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 LYS A1134 CG CD CE NZ
REMARK 470 LYS A1135 CG CD CE NZ
REMARK 470 LYS A1266 CG CD CE NZ
REMARK 470 GLU A1267 CG CD OE1 OE2
REMARK 470 ARG A1268 CG CD NE CZ NH1 NH2
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 C ILE A 1140 H LYS A 1141 1.49
REMARK 500 C ILE A 1140 H LYS A 1141 1.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLY A1118 CA GLY A1118 C 0.109
REMARK 500 ARG A1163 CA ARG A1163 C 0.170
REMARK 500 GLU A1227 CD GLU A1227 OE1 0.074
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A1017 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A1029 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A1030 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A1030 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A1063 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A1063 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A1212 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A1261 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 PRO A1265 C - N - CA ANGL. DEV. = 9.2 DEGREES
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 PRO A1214 -160.88 -77.38
REMARK 500 TYR A1219 -147.92 -116.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A1065 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO A1214 -15.75
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 A2003 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A2004 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A2005 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A2006 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A2007 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A2008 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A2009 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A2010 DISTANCE = 6.52 ANGSTROMS
REMARK 525 HOH A2011 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH A2012 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A2013 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A2014 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A2015 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A2016 DISTANCE = 7.38 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GV8 RELATED DB: PDB
DBREF 5GV7 A 1001 1272 UNP P83686 NB5R3_PIG 1 272
SEQRES 1 A 272 SER THR PRO ALA ILE THR LEU GLU ASN PRO ASP ILE LYS
SEQRES 2 A 272 TYR PRO LEU ARG LEU ILE ASP LYS GLU VAL VAL ASN HIS
SEQRES 3 A 272 ASP THR ARG ARG PHE ARG PHE ALA LEU PRO SER PRO GLU
SEQRES 4 A 272 HIS ILE LEU GLY LEU PRO VAL GLY GLN HIS ILE TYR LEU
SEQRES 5 A 272 SER ALA ARG ILE ASP GLY ASN LEU VAL ILE ARG PRO TYR
SEQRES 6 A 272 THR PRO VAL SER SER ASP ASP ASP LYS GLY PHE VAL ASP
SEQRES 7 A 272 LEU VAL ILE LYS VAL TYR PHE LYS ASP THR HIS PRO LYS
SEQRES 8 A 272 PHE PRO ALA GLY GLY LYS MET SER GLN TYR LEU GLU SER
SEQRES 9 A 272 MET LYS ILE GLY ASP THR ILE GLU PHE ARG GLY PRO ASN
SEQRES 10 A 272 GLY LEU LEU VAL TYR GLN GLY LYS GLY LYS PHE ALA ILE
SEQRES 11 A 272 ARG PRO ASP LYS LYS SER SER PRO VAL ILE LYS THR VAL
SEQRES 12 A 272 LYS SER VAL GLY MET ILE ALA GLY GLY THR GLY ILE THR
SEQRES 13 A 272 PRO MET LEU GLN VAL ILE ARG ALA ILE MET LYS ASP PRO
SEQRES 14 A 272 ASP ASP HIS THR VAL CYS HIS LEU LEU PHE ALA ASN GLN
SEQRES 15 A 272 THR GLU LYS ASP ILE LEU LEU ARG PRO GLU LEU GLU GLU
SEQRES 16 A 272 LEU ARG ASN GLU HIS SER ALA ARG PHE LYS LEU TRP TYR
SEQRES 17 A 272 THR VAL ASP ARG ALA PRO GLU ALA TRP ASP TYR SER GLN
SEQRES 18 A 272 GLY PHE VAL ASN GLU GLU MET ILE ARG ASP HIS LEU PRO
SEQRES 19 A 272 PRO PRO GLU GLU GLU PRO LEU VAL LEU MET CYS GLY PRO
SEQRES 20 A 272 PRO PRO MET ILE GLN TYR ALA CYS LEU PRO ASN LEU GLU
SEQRES 21 A 272 ARG VAL GLY HIS PRO LYS GLU ARG CYS PHE ALA PHE
HET FAD A1301 72
HET GOL A1302 6
HET GOL A1303 12
HET GOL A1304 12
HET GOL A1305 6
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 7 HOH *616(H2 O)
HELIX 1 AA1 GLY A 1096 MET A 1105 1 10
HELIX 2 AA2 GLY A 1154 LYS A 1167 1 14
HELIX 3 AA3 THR A 1183 ILE A 1187 5 5
HELIX 4 AA4 LEU A 1189 SER A 1201 1 13
HELIX 5 AA5 ASN A 1225 LEU A 1233 1 9
HELIX 6 AA6 PRO A 1235 GLU A 1239 5 5
HELIX 7 AA7 PRO A 1247 ALA A 1254 1 8
HELIX 8 AA8 CYS A 1255 GLY A 1263 1 9
HELIX 9 AA9 PRO A 1265 GLU A 1267 5 3
SHEET 1 AA1 6 ASN A1059 TYR A1065 0
SHEET 2 AA1 6 HIS A1049 ILE A1056 -1 N ILE A1056 O ASN A1059
SHEET 3 AA1 6 THR A1110 ASN A1117 -1 O ASN A1117 N HIS A1049
SHEET 4 AA1 6 TYR A1014 ASN A1025 -1 N TYR A1014 O PHE A1113
SHEET 5 AA1 6 THR A1028 ALA A1034 -1 O ARG A1032 N ILE A1019
SHEET 6 AA1 6 PHE A1076 LYS A1082 -1 O LEU A1079 N PHE A1031
SHEET 1 AA2 3 LEU A1120 GLY A1124 0
SHEET 2 AA2 3 LYS A1127 ILE A1130 -1 O ALA A1129 N VAL A1121
SHEET 3 AA2 3 VAL A1139 THR A1142 -1 O LYS A1141 N PHE A1128
SHEET 1 AA3 6 SER A1220 GLN A1221 0
SHEET 2 AA3 6 PHE A1204 VAL A1210 1 N TYR A1208 O SER A1220
SHEET 3 AA3 6 VAL A1174 ASN A1181 1 N LEU A1177 O LYS A1205
SHEET 4 AA3 6 SER A1145 GLY A1151 1 N ALA A1150 O ALA A1180
SHEET 5 AA3 6 LEU A1241 CYS A1245 1 O LEU A1241 N GLY A1147
SHEET 6 AA3 6 CYS A1269 ALA A1271 1 O PHE A1270 N VAL A1242
CISPEP 1 GLY A 1115 PRO A 1116 0 -4.60
SITE 1 AC1 32 ARG A1063 PRO A1064 TYR A1065 THR A1066
SITE 2 AC1 32 VAL A1080 ILE A1081 LYS A1082 TYR A1084
SITE 3 AC1 32 PHE A1085 THR A1088 HIS A1089 PHE A1092
SITE 4 AC1 32 GLY A1095 GLY A1096 LYS A1097 MET A1098
SITE 5 AC1 32 SER A1099 THR A1153 THR A1156 GOL A1304
SITE 6 AC1 32 GOL A1305 HOH A1404 HOH A1417 HOH A1451
SITE 7 AC1 32 HOH A1481 HOH A1528 HOH A1562 HOH A1582
SITE 8 AC1 32 HOH A1596 HOH A1603 HOH A1620 HOH A1740
SITE 1 AC2 8 GLY A1075 PHE A1076 ASP A1170 HOH A1448
SITE 2 AC2 8 HOH A1453 HOH A1555 HOH A1643 HOH A1882
SITE 1 AC3 11 GLY A1151 GLY A1152 ALA A1180 ASN A1181
SITE 2 AC3 11 ASP A1211 PHE A1223 PRO A1247 MET A1250
SITE 3 AC3 11 HOH A1473 HOH A1675 HOH A1728
SITE 1 AC4 12 GLY A1151 THR A1153 GLY A1154 GLY A1246
SITE 2 AC4 12 PRO A1247 FAD A1301 HOH A1417 HOH A1562
SITE 3 AC4 12 HOH A1620 HOH A1668 HOH A1695 HOH A1761
SITE 1 AC5 8 ALA A1094 GLY A1095 LYS A1097 FAD A1301
SITE 2 AC5 8 HOH A1432 HOH A1604 HOH A1921 HOH A1935
CRYST1 48.664 72.177 85.209 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 0.020549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013855 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011736 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
