HEADER SIGNALING PROTEIN 23-MAR-14 4PXF
TITLE CRYSTAL STRUCTURE OF THE ACTIVE G-PROTEIN-COUPLED RECEPTOR OPSIN IN
TITLE 2 COMPLEX WITH THE FINGER-LOOP PEPTIDE DERIVED FROM THE FULL-LENGTH
TITLE 3 ARRESTIN-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHODOPSIN;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: S-ARRESTIN;
COMPND 6 CHAIN: B;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 OTHER_DETAILS: BOVINE EYE;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 9 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 10 ORGANISM_TAXID: 9913
KEYWDS RETINAL PROTEIN, PHOTORECEPTOR, G-PROTEIN COUPLED RECEPTOR,
KEYWDS 2 PHOSPHOPROTEIN, PHOTORECEPTOR PROTEIN, SENSORY TRANSDUCTION,
KEYWDS 3 TRANSDUCER, TRANSMEMBRANE, VISION, SIGNALING PROTEIN, VISUAL
KEYWDS 4 ARRESTIN, DESENSITISATION OF THE VISUAL TRANSDUCTION CASCADE,
KEYWDS 5 BINDING TO ACTICATED AND PHOSPHORYLATED RHODOPSIN, RHODOPSIN, OPSIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SZCZEPEK,P.SCHEERER
REVDAT 3 20-SEP-23 4PXF 1 HETSYN
REVDAT 2 29-JUL-20 4PXF 1 COMPND REMARK HET HETNAM
REVDAT 2 2 1 HETSYN FORMUL LINK SITE
REVDAT 2 3 1 ATOM
REVDAT 1 17-SEP-14 4PXF 0
JRNL AUTH M.SZCZEPEK,F.BEYRIERE,K.P.HOFMANN,M.ELGETI,R.KAZMIN,A.ROSE,
JRNL AUTH 2 F.J.BARTL,D.VON STETTEN,M.HECK,M.E.SOMMER,P.W.HILDEBRAND,
JRNL AUTH 3 P.SCHEERER
JRNL TITL CRYSTAL STRUCTURE OF A COMMON GPCR-BINDING INTERFACE FOR G
JRNL TITL 2 PROTEIN AND ARRESTIN.
JRNL REF NAT COMMUN V. 5 4801 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25205354
JRNL DOI 10.1038/NCOMMS5801
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30511
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 + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1637
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2238
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2635
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 159
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 70.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.17000
REMARK 3 B22 (A**2) : -1.17000
REMARK 3 B33 (A**2) : 3.79000
REMARK 3 B12 (A**2) : -1.17000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2872 ; 0.009 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2702 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3911 ; 1.187 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6211 ; 0.798 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 332 ; 5.104 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;36.438 ;23.421
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 419 ;15.713 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;12.246 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 454 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3080 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 681 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1329 ;13.846 ; 3.493
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1327 ;13.834 ; 3.490
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1657 ;16.286 ; 5.258
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1658 ;16.284 ; 5.258
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1542 ;16.421 ; 4.237
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1542 ;16.412 ; 4.237
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2254 ;19.421 ; 6.147
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3394 ;19.062 ;31.142
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3393 ;19.038 ;31.102
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5571 ; 6.208 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 2 ;40.117 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5497 ;42.816 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 326
REMARK 3 ORIGIN FOR THE GROUP (A): 133.5021 248.1880 38.3901
REMARK 3 T TENSOR
REMARK 3 T11: 0.5966 T22: 0.6075
REMARK 3 T33: 0.3793 T12: 0.0030
REMARK 3 T13: -0.0364 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.2922 L22: 1.0499
REMARK 3 L33: 0.3591 L12: 0.1504
REMARK 3 L13: -0.1493 L23: 0.0503
REMARK 3 S TENSOR
REMARK 3 S11: -0.0085 S12: 0.0247 S13: 0.0738
REMARK 3 S21: -0.0665 S22: -0.0080 S23: 0.0276
REMARK 3 S31: 0.0420 S32: 0.0569 S33: 0.0165
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 71 B 77
REMARK 3 ORIGIN FOR THE GROUP (A): 122.6938 226.4295 39.1501
REMARK 3 T TENSOR
REMARK 3 T11: 0.7873 T22: 0.7445
REMARK 3 T33: 0.8968 T12: -0.1184
REMARK 3 T13: 0.1236 T23: -0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 0.3056 L22: 4.5566
REMARK 3 L33: 1.1300 L12: -1.0004
REMARK 3 L13: 0.5268 L23: -2.2240
REMARK 3 S TENSOR
REMARK 3 S11: -0.1380 S12: -0.1658 S13: -0.0316
REMARK 3 S21: -0.3816 S22: 0.3045 S23: -0.0074
REMARK 3 S31: 0.0938 S32: -0.2005 S33: -0.1664
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 401 A 411
REMARK 3 ORIGIN FOR THE GROUP (A): 146.9902 256.1458 41.5382
REMARK 3 T TENSOR
REMARK 3 T11: 0.5661 T22: 0.5190
REMARK 3 T33: 0.5318 T12: 0.0325
REMARK 3 T13: -0.1350 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 1.0182 L22: 0.1477
REMARK 3 L33: 0.6370 L12: 0.3058
REMARK 3 L13: 0.1307 L23: 0.1958
REMARK 3 S TENSOR
REMARK 3 S11: -0.1535 S12: 0.0835 S13: 0.4692
REMARK 3 S21: -0.0482 S22: 0.0118 S23: 0.2168
REMARK 3 S31: 0.2025 S32: -0.1684 S33: 0.1417
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 511
REMARK 3 ORIGIN FOR THE GROUP (A): 133.1363 251.4432 40.2838
REMARK 3 T TENSOR
REMARK 3 T11: 0.7520 T22: 0.8678
REMARK 3 T33: 0.4436 T12: -0.1793
REMARK 3 T13: -0.0587 T23: 0.1893
REMARK 3 L TENSOR
REMARK 3 L11: 2.4392 L22: 3.5892
REMARK 3 L33: 1.1831 L12: 2.1043
REMARK 3 L13: 0.6801 L23: 1.8437
REMARK 3 S TENSOR
REMARK 3 S11: 0.0899 S12: 0.3198 S13: -0.1382
REMARK 3 S21: 0.1979 S22: -0.0375 S23: -0.3643
REMARK 3 S31: 0.0321 S32: -0.2306 S33: -0.0524
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4PXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : SI(311) MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32166
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 40.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.94400
REMARK 200 R SYM FOR SHELL (I) : 0.00000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 3DQB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2 M (NH4)2SO4 IN 0.1 M 2-(N
REMARK 280 -MORPHOLINO)ETHANESULFONIC ACID (MES), PH 6.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 121.31100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.03894
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.73867
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.31100
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.03894
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.73867
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.31100
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.03894
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.73867
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.31100
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.03894
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.73867
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.31100
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.03894
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.73867
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.31100
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.03894
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.73867
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.07788
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.47733
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.07788
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.47733
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.07788
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 73.47733
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.07788
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.47733
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.07788
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 73.47733
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.07788
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 73.47733
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 110.21600
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 A 1
REMARK 465 PRO A 327
REMARK 465 LEU A 328
REMARK 465 GLY A 329
REMARK 465 ASP A 330
REMARK 465 ASP A 331
REMARK 465 GLU A 332
REMARK 465 ALA A 333
REMARK 465 SER A 334
REMARK 465 THR A 335
REMARK 465 THR A 336
REMARK 465 VAL A 337
REMARK 465 SER A 338
REMARK 465 LYS A 339
REMARK 465 THR A 340
REMARK 465 GLU A 341
REMARK 465 THR A 342
REMARK 465 SER A 343
REMARK 465 GLN A 344
REMARK 465 VAL A 345
REMARK 465 ALA A 346
REMARK 465 PRO A 347
REMARK 465 ALA A 348
REMARK 465 TYR B 67
REMARK 465 GLY B 68
REMARK 465 GLN B 69
REMARK 465 GLU B 70
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 ND2 ASN A 15 O5 NAG C 1 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 PRO A 27 154.09 -48.33
REMARK 500 SER A 176 -168.49 67.62
REMARK 500 PHE A 212 -60.30 -135.69
REMARK 500 ILE A 307 -64.68 -129.25
REMARK 500 LYS A 325 171.59 69.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4PXF A 1 348 UNP P02699 OPSD_BOVIN 1 348
DBREF 4PXF B 67 77 UNP P08168 ARRS_BOVIN 67 77
SEQRES 1 A 348 MET ASN GLY THR GLU GLY PRO ASN PHE TYR VAL PRO PHE
SEQRES 2 A 348 SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU ALA
SEQRES 3 A 348 PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER MET
SEQRES 4 A 348 LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY PHE
SEQRES 5 A 348 PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN HIS
SEQRES 6 A 348 LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU ASN
SEQRES 7 A 348 LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY PHE
SEQRES 8 A 348 THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE VAL
SEQRES 9 A 348 PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE ALA
SEQRES 10 A 348 THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL VAL
SEQRES 11 A 348 LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO MET
SEQRES 12 A 348 SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET GLY
SEQRES 13 A 348 VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA ALA
SEQRES 14 A 348 PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU GLY
SEQRES 15 A 348 MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO HIS
SEQRES 16 A 348 GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET PHE
SEQRES 17 A 348 VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE PHE
SEQRES 18 A 348 CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA ALA
SEQRES 19 A 348 ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA GLU
SEQRES 20 A 348 LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE ALA
SEQRES 21 A 348 PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA PHE
SEQRES 22 A 348 TYR ILE PHE THR HIS GLN GLY SER ASP PHE GLY PRO ILE
SEQRES 23 A 348 PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER ALA
SEQRES 24 A 348 VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS GLN
SEQRES 25 A 348 PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY LYS
SEQRES 26 A 348 ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SER
SEQRES 27 A 348 LYS THR GLU THR SER GLN VAL ALA PRO ALA
SEQRES 1 B 11 TYR GLY GLN GLU ASP ILE ASP VAL MET GLY LEU
MODRES 4PXF ASN A 15 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET GLC D 1 11
HET GLC D 2 12
HET BOG A 405 20
HET BOG A 406 20
HET BOG A 407 20
HET PLM A 408 17
HET SO4 A 409 5
HET ACT A 410 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM PLM PALMITIC ACID
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 3 BMA C6 H12 O6
FORMUL 3 MAN C6 H12 O6
FORMUL 4 GLC 2(C6 H12 O6)
FORMUL 5 BOG 3(C14 H28 O6)
FORMUL 8 PLM C16 H32 O2
FORMUL 9 SO4 O4 S 2-
FORMUL 10 ACT C2 H3 O2 1-
FORMUL 11 HOH *11(H2 O)
HELIX 1 1 SER A 14 GLY A 18 5 5
HELIX 2 2 GLU A 33 HIS A 65 1 33
HELIX 3 3 LYS A 66 ARG A 69 5 4
HELIX 4 4 THR A 70 GLY A 90 1 21
HELIX 5 5 GLY A 90 LEU A 99 1 10
HELIX 6 6 PHE A 105 LYS A 141 1 37
HELIX 7 7 GLY A 149 VAL A 173 1 25
HELIX 8 8 HIS A 195 THR A 198 5 4
HELIX 9 9 ASN A 199 PHE A 212 1 14
HELIX 10 10 PHE A 212 GLN A 236 1 25
HELIX 11 11 SER A 240 HIS A 278 1 39
HELIX 12 12 GLY A 284 THR A 297 1 14
HELIX 13 13 THR A 297 ILE A 307 1 11
HELIX 14 14 ASN A 310 CYS A 322 1 13
HELIX 15 15 ILE B 72 GLY B 76 5 5
SHEET 1 A 2 THR A 4 GLY A 6 0
SHEET 2 A 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4
SHEET 1 B 2 TYR A 178 GLU A 181 0
SHEET 2 B 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181
SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.04
LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.33
LINK SG CYS A 323 C1 PLM A 408 1555 1555 1.87
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.45
LINK C1 GLC D 1 O1 GLC D 2 1555 1555 1.44
CRYST1 242.622 242.622 110.216 90.00 90.00 120.00 H 3 2 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 0.004122 0.002380 0.000000 0.00000
SCALE2 0.000000 0.004759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END