HEADER TRANSPORT PROTEIN 28-JAN-14 4COF
TITLE CRYSTAL STRUCTURE OF A HUMAN GAMMA-AMINOBUTYRIC ACID RECEPTOR, THE
TITLE 2 GABA(A)R-BETA3 HOMOPENTAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: RESIDUES 26-312,447-473;
COMPND 5 SYNONYM: GABA(A) RECEPTOR SUBUNIT BETA-3, GABA RECEPTOR, IONOTROPIC,
COMPND 6 BETA-3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS TRANSPORT PROTEIN, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.S.MILLER,A.R.ARICESCU
REVDAT 6 20-DEC-23 4COF 1 HETSYN SHEET
REVDAT 5 29-JUL-20 4COF 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 27-AUG-14 4COF 1 JRNL
REVDAT 3 18-JUN-14 4COF 1 JRNL
REVDAT 2 11-JUN-14 4COF 1 KEYWDS
REVDAT 1 04-JUN-14 4COF 0
JRNL AUTH P.S.MILLER,A.R.ARICESCU
JRNL TITL CRYSTAL STRUCTURE OF A HUMAN GABAA RECEPTOR
JRNL REF NATURE V. 512 270 2014
JRNL REFN ISSN 0028-0836
JRNL PMID 24909990
JRNL DOI 10.1038/NATURE13293
REMARK 2
REMARK 2 RESOLUTION. 2.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 76328
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 3835
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.97
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.76
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5599
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2364
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5333
REMARK 3 BIN R VALUE (WORKING SET) : 0.2343
REMARK 3 BIN FREE R VALUE : 0.2809
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.75
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 266
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13643
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 329
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 83.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 102.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.64520
REMARK 3 B22 (A**2) : -24.16500
REMARK 3 B33 (A**2) : 34.81020
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 17.90620
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.494
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.450
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.274
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.503
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.286
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.874
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 14364 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 19588 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 6453 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 260 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 2099 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 14364 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1934 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 16013 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.27
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.16
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|1 - A|217 }
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8047 -23.8317 120.8487
REMARK 3 T TENSOR
REMARK 3 T11: 0.1848 T22: -0.1029
REMARK 3 T33: -0.1731 T12: -0.1525
REMARK 3 T13: -0.1001 T23: -0.1456
REMARK 3 L TENSOR
REMARK 3 L11: 1.1868 L22: 0.7303
REMARK 3 L33: 2.9861 L12: -0.2868
REMARK 3 L13: -0.5209 L23: -0.0754
REMARK 3 S TENSOR
REMARK 3 S11: 0.1465 S12: 0.0056 S13: -0.2299
REMARK 3 S21: -0.0769 S22: -0.0855 S23: 0.0384
REMARK 3 S31: 0.5273 S32: -0.5487 S33: -0.0610
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|218 - A|447 }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7180 -19.0774 172.9785
REMARK 3 T TENSOR
REMARK 3 T11: 0.1507 T22: -0.0791
REMARK 3 T33: -0.1317 T12: -0.0728
REMARK 3 T13: -0.0380 T23: -0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 1.7411 L22: 1.3351
REMARK 3 L33: 2.5186 L12: 0.0668
REMARK 3 L13: 0.8123 L23: -0.4964
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: -0.0311 S13: -0.1917
REMARK 3 S21: 0.0056 S22: -0.0892 S23: -0.0020
REMARK 3 S31: 0.4027 S32: -0.1754 S33: 0.0986
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { B|10 - B|217 }
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4866 -9.7636 114.2808
REMARK 3 T TENSOR
REMARK 3 T11: -0.0030 T22: -0.0291
REMARK 3 T33: -0.1784 T12: 0.0410
REMARK 3 T13: 0.0616 T23: -0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 1.1743 L22: 2.3396
REMARK 3 L33: 4.0597 L12: -0.1999
REMARK 3 L13: 0.4516 L23: -0.1217
REMARK 3 S TENSOR
REMARK 3 S11: 0.0131 S12: 0.1937 S13: -0.0136
REMARK 3 S21: -0.2602 S22: -0.0694 S23: -0.0561
REMARK 3 S31: 0.2151 S32: 0.4816 S33: 0.0563
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { B|218 - B|447 }
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3199 -11.9511 165.7900
REMARK 3 T TENSOR
REMARK 3 T11: 0.0732 T22: 0.0500
REMARK 3 T33: -0.1482 T12: 0.0758
REMARK 3 T13: -0.0208 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.6501 L22: 1.3838
REMARK 3 L33: 2.0426 L12: 0.2431
REMARK 3 L13: 0.6137 L23: 0.7020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: 0.1889 S13: -0.0453
REMARK 3 S21: 0.0111 S22: -0.0336 S23: -0.1613
REMARK 3 S31: 0.2086 S32: 0.3289 S33: 0.1057
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { C|10 - C|217 }
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6072 16.4319 116.4461
REMARK 3 T TENSOR
REMARK 3 T11: 0.1598 T22: -0.1313
REMARK 3 T33: -0.1879 T12: -0.0748
REMARK 3 T13: -0.1059 T23: 0.0930
REMARK 3 L TENSOR
REMARK 3 L11: 2.3308 L22: 1.2189
REMARK 3 L33: 3.0139 L12: -0.5739
REMARK 3 L13: 0.3908 L23: -0.3393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0457 S12: 0.3349 S13: 0.0761
REMARK 3 S21: -0.1172 S22: -0.1334 S23: 0.0508
REMARK 3 S31: -0.3797 S32: -0.0069 S33: 0.1791
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { C|218 - C|447 }
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0078 10.1735 165.9037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: -0.0303
REMARK 3 T33: -0.1235 T12: -0.0761
REMARK 3 T13: -0.0815 T23: 0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 1.0281 L22: 1.1479
REMARK 3 L33: 3.6032 L12: 0.2795
REMARK 3 L13: 0.5274 L23: 1.0523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0628 S12: -0.0013 S13: 0.1924
REMARK 3 S21: -0.1309 S22: -0.0975 S23: -0.0274
REMARK 3 S31: -0.2736 S32: 0.2948 S33: 0.1603
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { D|10 - D|217 }
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5116 18.6308 125.8141
REMARK 3 T TENSOR
REMARK 3 T11: -0.0060 T22: 0.1084
REMARK 3 T33: -0.2371 T12: 0.2924
REMARK 3 T13: -0.1837 T23: -0.0924
REMARK 3 L TENSOR
REMARK 3 L11: 2.4839 L22: 1.9363
REMARK 3 L33: 1.5102 L12: 0.3984
REMARK 3 L13: 0.8175 L23: 0.3514
REMARK 3 S TENSOR
REMARK 3 S11: -0.1394 S12: 0.2350 S13: 0.1713
REMARK 3 S21: -0.0979 S22: -0.1114 S23: 0.0927
REMARK 3 S31: -0.3987 S32: -0.5118 S33: 0.2508
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { D|218 - D|448 }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1198 16.8524 173.1292
REMARK 3 T TENSOR
REMARK 3 T11: 0.1016 T22: -0.0178
REMARK 3 T33: -0.1232 T12: 0.1542
REMARK 3 T13: -0.1169 T23: -0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 0.7965 L22: 1.5794
REMARK 3 L33: 1.9241 L12: 0.1386
REMARK 3 L13: -0.4985 L23: 0.1749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: 0.0222 S13: 0.1813
REMARK 3 S21: 0.0670 S22: -0.0806 S23: 0.0692
REMARK 3 S31: -0.3403 S32: -0.2575 S33: 0.1160
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { E|10 - E|217 }
REMARK 3 ORIGIN FOR THE GROUP (A): -24.2739 -6.2554 129.2067
REMARK 3 T TENSOR
REMARK 3 T11: -0.2798 T22: 0.3977
REMARK 3 T33: -0.2936 T12: -0.1268
REMARK 3 T13: -0.0654 T23: -0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 1.6532 L22: 2.1589
REMARK 3 L33: 2.4893 L12: -0.2035
REMARK 3 L13: 0.9606 L23: 1.3708
REMARK 3 S TENSOR
REMARK 3 S11: -0.0054 S12: -0.1673 S13: -0.0675
REMARK 3 S21: -0.2546 S22: 0.0605 S23: 0.1274
REMARK 3 S31: -0.0372 S32: -0.5978 S33: -0.0552
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { E|218 - E|447 }
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7231 -1.3601 177.5875
REMARK 3 T TENSOR
REMARK 3 T11: -0.0724 T22: 0.1902
REMARK 3 T33: -0.1424 T12: -0.0148
REMARK 3 T13: -0.0474 T23: -0.0519
REMARK 3 L TENSOR
REMARK 3 L11: 1.4257 L22: 1.2410
REMARK 3 L33: 2.9432 L12: 0.0543
REMARK 3 L13: 0.6891 L23: -0.1694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0922 S12: -0.1258 S13: 0.0453
REMARK 3 S21: 0.0697 S22: -0.0224 S23: 0.1269
REMARK 3 S31: 0.1092 S32: -0.4160 S33: 0.1146
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 4COF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1290059620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76360
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.970
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.83000
REMARK 200 R SYM FOR SHELL (I) : NULL
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: PDB ENTRY 3RHW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11.5% PEG4000 100 MM SODIUM CHLORIDE,
REMARK 280 100 MM LITHIUM SULPHATE, 100 MM N-2-ACETAMIDO-IMINODIACETIC ACID,
REMARK 280 PH 6.5, 2% (W/V) BENZAMIDINE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 87.05000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 87.05000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.45000
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 GLU A -2
REMARK 465 THR A -1
REMARK 465 GLY A 0
REMARK 465 ASN A 448
REMARK 465 GLY A 449
REMARK 465 ALA A 450
REMARK 465 THR A 451
REMARK 465 GLU A 452
REMARK 465 THR A 453
REMARK 465 SER A 454
REMARK 465 GLN A 455
REMARK 465 VAL A 456
REMARK 465 ALA A 457
REMARK 465 PRO A 458
REMARK 465 ALA A 459
REMARK 465 GLU B -2
REMARK 465 THR B -1
REMARK 465 GLY B 0
REMARK 465 GLN B 1
REMARK 465 SER B 2
REMARK 465 VAL B 3
REMARK 465 ASN B 4
REMARK 465 ASP B 5
REMARK 465 PRO B 6
REMARK 465 GLY B 7
REMARK 465 ASN B 8
REMARK 465 MET B 9
REMARK 465 ASN B 448
REMARK 465 GLY B 449
REMARK 465 ALA B 450
REMARK 465 THR B 451
REMARK 465 GLU B 452
REMARK 465 THR B 453
REMARK 465 SER B 454
REMARK 465 GLN B 455
REMARK 465 VAL B 456
REMARK 465 ALA B 457
REMARK 465 PRO B 458
REMARK 465 ALA B 459
REMARK 465 GLU C -2
REMARK 465 THR C -1
REMARK 465 GLY C 0
REMARK 465 GLN C 1
REMARK 465 SER C 2
REMARK 465 VAL C 3
REMARK 465 ASN C 4
REMARK 465 ASP C 5
REMARK 465 PRO C 6
REMARK 465 GLY C 7
REMARK 465 ASN C 8
REMARK 465 MET C 9
REMARK 465 ASN C 448
REMARK 465 GLY C 449
REMARK 465 ALA C 450
REMARK 465 THR C 451
REMARK 465 GLU C 452
REMARK 465 THR C 453
REMARK 465 SER C 454
REMARK 465 GLN C 455
REMARK 465 VAL C 456
REMARK 465 ALA C 457
REMARK 465 PRO C 458
REMARK 465 ALA C 459
REMARK 465 GLU D -2
REMARK 465 THR D -1
REMARK 465 GLY D 0
REMARK 465 GLN D 1
REMARK 465 SER D 2
REMARK 465 VAL D 3
REMARK 465 ASN D 4
REMARK 465 ASP D 5
REMARK 465 PRO D 6
REMARK 465 GLY D 7
REMARK 465 ASN D 8
REMARK 465 MET D 9
REMARK 465 GLY D 449
REMARK 465 ALA D 450
REMARK 465 THR D 451
REMARK 465 GLU D 452
REMARK 465 THR D 453
REMARK 465 SER D 454
REMARK 465 GLN D 455
REMARK 465 VAL D 456
REMARK 465 ALA D 457
REMARK 465 PRO D 458
REMARK 465 ALA D 459
REMARK 465 GLU E -2
REMARK 465 THR E -1
REMARK 465 GLY E 0
REMARK 465 GLN E 1
REMARK 465 SER E 2
REMARK 465 VAL E 3
REMARK 465 ASN E 4
REMARK 465 ASP E 5
REMARK 465 PRO E 6
REMARK 465 GLY E 7
REMARK 465 ASN E 8
REMARK 465 MET E 9
REMARK 465 ASN E 448
REMARK 465 GLY E 449
REMARK 465 ALA E 450
REMARK 465 THR E 451
REMARK 465 GLU E 452
REMARK 465 THR E 453
REMARK 465 SER E 454
REMARK 465 GLN E 455
REMARK 465 VAL E 456
REMARK 465 ALA E 457
REMARK 465 PRO E 458
REMARK 465 ALA E 459
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 MET A 55 61.70 33.57
REMARK 500 PRO A 78 34.36 -94.45
REMARK 500 ASP A 95 47.34 -88.77
REMARK 500 LEU A 145 50.71 -103.46
REMARK 500 LYS A 274 70.02 -69.12
REMARK 500 MET B 55 61.91 33.83
REMARK 500 PRO B 78 34.09 -95.31
REMARK 500 ASP B 95 48.51 -88.20
REMARK 500 LEU B 145 54.96 -101.73
REMARK 500 GLU B 182 75.06 -109.80
REMARK 500 LYS B 274 70.48 -69.82
REMARK 500 MET C 55 61.12 33.68
REMARK 500 PRO C 78 34.71 -95.67
REMARK 500 ASP C 95 47.77 -87.17
REMARK 500 LEU C 145 43.69 -99.05
REMARK 500 GLU C 182 73.45 -109.90
REMARK 500 MET D 55 61.34 33.83
REMARK 500 PRO D 78 32.84 -95.66
REMARK 500 ASP D 95 46.43 -87.54
REMARK 500 LEU D 145 58.77 -103.52
REMARK 500 GLU D 182 76.48 -110.72
REMARK 500 LYS D 274 69.45 -69.89
REMARK 500 MET E 55 62.48 33.08
REMARK 500 PRO E 78 35.01 -96.24
REMARK 500 ASP E 95 47.50 -88.94
REMARK 500 LEU E 145 53.14 -99.38
REMARK 500 GLU E 182 78.98 -112.51
REMARK 500 LYS E 274 69.28 -68.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
DBREF 4COF A 1 307 UNP P28472 GBRB3_HUMAN 26 312
DBREF 4COF A 422 448 UNP P28472 GBRB3_HUMAN 447 473
DBREF 4COF B 1 307 UNP P28472 GBRB3_HUMAN 26 312
DBREF 4COF B 422 448 UNP P28472 GBRB3_HUMAN 447 473
DBREF 4COF C 1 307 UNP P28472 GBRB3_HUMAN 26 312
DBREF 4COF C 422 448 UNP P28472 GBRB3_HUMAN 447 473
DBREF 4COF D 1 307 UNP P28472 GBRB3_HUMAN 26 312
DBREF 4COF D 422 448 UNP P28472 GBRB3_HUMAN 447 473
DBREF 4COF E 1 307 UNP P28472 GBRB3_HUMAN 26 312
DBREF 4COF E 422 448 UNP P28472 GBRB3_HUMAN 447 473
SEQADV 4COF GLU A -2 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR A -1 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY A 0 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY A 449 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA A 450 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR A 451 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLU A 452 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR A 453 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER A 454 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLN A 455 UNP P28472 EXPRESSION TAG
SEQADV 4COF VAL A 456 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA A 457 UNP P28472 EXPRESSION TAG
SEQADV 4COF PRO A 458 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA A 459 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER A 308 UNP P28472 LINKER
SEQADV 4COF GLN A 309 UNP P28472 LINKER
SEQADV 4COF PRO A 310 UNP P28472 LINKER
SEQADV 4COF ALA A 311 UNP P28472 LINKER
SEQADV 4COF ARG A 312 UNP P28472 LINKER
SEQADV 4COF ALA A 313 UNP P28472 LINKER
SEQADV 4COF ALA A 314 UNP P28472 LINKER
SEQADV 4COF GLU B -2 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR B -1 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY B 0 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY B 449 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA B 450 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR B 451 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLU B 452 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR B 453 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER B 454 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLN B 455 UNP P28472 EXPRESSION TAG
SEQADV 4COF VAL B 456 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA B 457 UNP P28472 EXPRESSION TAG
SEQADV 4COF PRO B 458 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA B 459 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER B 308 UNP P28472 LINKER
SEQADV 4COF GLN B 309 UNP P28472 LINKER
SEQADV 4COF PRO B 310 UNP P28472 LINKER
SEQADV 4COF ALA B 311 UNP P28472 LINKER
SEQADV 4COF ARG B 312 UNP P28472 LINKER
SEQADV 4COF ALA B 313 UNP P28472 LINKER
SEQADV 4COF ALA B 314 UNP P28472 LINKER
SEQADV 4COF GLU C -2 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR C -1 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY C 0 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY C 449 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA C 450 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR C 451 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLU C 452 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR C 453 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER C 454 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLN C 455 UNP P28472 EXPRESSION TAG
SEQADV 4COF VAL C 456 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA C 457 UNP P28472 EXPRESSION TAG
SEQADV 4COF PRO C 458 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA C 459 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER C 308 UNP P28472 LINKER
SEQADV 4COF GLN C 309 UNP P28472 LINKER
SEQADV 4COF PRO C 310 UNP P28472 LINKER
SEQADV 4COF ALA C 311 UNP P28472 LINKER
SEQADV 4COF ARG C 312 UNP P28472 LINKER
SEQADV 4COF ALA C 313 UNP P28472 LINKER
SEQADV 4COF ALA C 314 UNP P28472 LINKER
SEQADV 4COF GLU D -2 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR D -1 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY D 0 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY D 449 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA D 450 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR D 451 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLU D 452 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR D 453 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER D 454 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLN D 455 UNP P28472 EXPRESSION TAG
SEQADV 4COF VAL D 456 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA D 457 UNP P28472 EXPRESSION TAG
SEQADV 4COF PRO D 458 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA D 459 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER D 308 UNP P28472 LINKER
SEQADV 4COF GLN D 309 UNP P28472 LINKER
SEQADV 4COF PRO D 310 UNP P28472 LINKER
SEQADV 4COF ALA D 311 UNP P28472 LINKER
SEQADV 4COF ARG D 312 UNP P28472 LINKER
SEQADV 4COF ALA D 313 UNP P28472 LINKER
SEQADV 4COF ALA D 314 UNP P28472 LINKER
SEQADV 4COF GLU E -2 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR E -1 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY E 0 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLY E 449 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA E 450 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR E 451 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLU E 452 UNP P28472 EXPRESSION TAG
SEQADV 4COF THR E 453 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER E 454 UNP P28472 EXPRESSION TAG
SEQADV 4COF GLN E 455 UNP P28472 EXPRESSION TAG
SEQADV 4COF VAL E 456 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA E 457 UNP P28472 EXPRESSION TAG
SEQADV 4COF PRO E 458 UNP P28472 EXPRESSION TAG
SEQADV 4COF ALA E 459 UNP P28472 EXPRESSION TAG
SEQADV 4COF SER E 308 UNP P28472 LINKER
SEQADV 4COF GLN E 309 UNP P28472 LINKER
SEQADV 4COF PRO E 310 UNP P28472 LINKER
SEQADV 4COF ALA E 311 UNP P28472 LINKER
SEQADV 4COF ARG E 312 UNP P28472 LINKER
SEQADV 4COF ALA E 313 UNP P28472 LINKER
SEQADV 4COF ALA E 314 UNP P28472 LINKER
SEQRES 1 A 355 GLU THR GLY GLN SER VAL ASN ASP PRO GLY ASN MET SER
SEQRES 2 A 355 PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS GLY TYR
SEQRES 3 A 355 ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL
SEQRES 4 A 355 CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE ASP MET
SEQRES 5 A 355 VAL SER GLU VAL ASN MET ASP TYR THR LEU THR MET TYR
SEQRES 6 A 355 PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA TYR SER
SEQRES 7 A 355 GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG VAL ALA
SEQRES 8 A 355 ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU ASN ASP
SEQRES 9 A 355 LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS ASN ARG
SEQRES 10 A 355 MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU TYR GLY
SEQRES 11 A 355 LEU ARG ILE THR THR THR ALA ALA CYS MET MET ASP LEU
SEQRES 12 A 355 ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR LEU GLU
SEQRES 13 A 355 ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE GLU PHE
SEQRES 14 A 355 TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY VAL GLU
SEQRES 15 A 355 ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU HIS ARG
SEQRES 16 A 355 LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY ALA TYR
SEQRES 17 A 355 PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG ASN ILE
SEQRES 18 A 355 GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER ILE LEU
SEQRES 19 A 355 ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE ASN TYR
SEQRES 20 A 355 ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE THR THR
SEQRES 21 A 355 VAL LEU THR MET THR THR ILE ASN THR HIS LEU ARG GLU
SEQRES 22 A 355 THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE ASP MET
SEQRES 23 A 355 TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU
SEQRES 24 A 355 LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SER GLN
SEQRES 25 A 355 PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE
SEQRES 26 A 355 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR
SEQRES 27 A 355 TRP LEU TYR TYR VAL ASN GLY ALA THR GLU THR SER GLN
SEQRES 28 A 355 VAL ALA PRO ALA
SEQRES 1 B 355 GLU THR GLY GLN SER VAL ASN ASP PRO GLY ASN MET SER
SEQRES 2 B 355 PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS GLY TYR
SEQRES 3 B 355 ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL
SEQRES 4 B 355 CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE ASP MET
SEQRES 5 B 355 VAL SER GLU VAL ASN MET ASP TYR THR LEU THR MET TYR
SEQRES 6 B 355 PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA TYR SER
SEQRES 7 B 355 GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG VAL ALA
SEQRES 8 B 355 ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU ASN ASP
SEQRES 9 B 355 LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS ASN ARG
SEQRES 10 B 355 MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU TYR GLY
SEQRES 11 B 355 LEU ARG ILE THR THR THR ALA ALA CYS MET MET ASP LEU
SEQRES 12 B 355 ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR LEU GLU
SEQRES 13 B 355 ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE GLU PHE
SEQRES 14 B 355 TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY VAL GLU
SEQRES 15 B 355 ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU HIS ARG
SEQRES 16 B 355 LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY ALA TYR
SEQRES 17 B 355 PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG ASN ILE
SEQRES 18 B 355 GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER ILE LEU
SEQRES 19 B 355 ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE ASN TYR
SEQRES 20 B 355 ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE THR THR
SEQRES 21 B 355 VAL LEU THR MET THR THR ILE ASN THR HIS LEU ARG GLU
SEQRES 22 B 355 THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE ASP MET
SEQRES 23 B 355 TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU
SEQRES 24 B 355 LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SER GLN
SEQRES 25 B 355 PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE
SEQRES 26 B 355 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR
SEQRES 27 B 355 TRP LEU TYR TYR VAL ASN GLY ALA THR GLU THR SER GLN
SEQRES 28 B 355 VAL ALA PRO ALA
SEQRES 1 C 355 GLU THR GLY GLN SER VAL ASN ASP PRO GLY ASN MET SER
SEQRES 2 C 355 PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS GLY TYR
SEQRES 3 C 355 ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL
SEQRES 4 C 355 CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE ASP MET
SEQRES 5 C 355 VAL SER GLU VAL ASN MET ASP TYR THR LEU THR MET TYR
SEQRES 6 C 355 PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA TYR SER
SEQRES 7 C 355 GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG VAL ALA
SEQRES 8 C 355 ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU ASN ASP
SEQRES 9 C 355 LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS ASN ARG
SEQRES 10 C 355 MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU TYR GLY
SEQRES 11 C 355 LEU ARG ILE THR THR THR ALA ALA CYS MET MET ASP LEU
SEQRES 12 C 355 ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR LEU GLU
SEQRES 13 C 355 ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE GLU PHE
SEQRES 14 C 355 TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY VAL GLU
SEQRES 15 C 355 ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU HIS ARG
SEQRES 16 C 355 LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY ALA TYR
SEQRES 17 C 355 PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG ASN ILE
SEQRES 18 C 355 GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER ILE LEU
SEQRES 19 C 355 ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE ASN TYR
SEQRES 20 C 355 ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE THR THR
SEQRES 21 C 355 VAL LEU THR MET THR THR ILE ASN THR HIS LEU ARG GLU
SEQRES 22 C 355 THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE ASP MET
SEQRES 23 C 355 TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU
SEQRES 24 C 355 LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SER GLN
SEQRES 25 C 355 PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE
SEQRES 26 C 355 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR
SEQRES 27 C 355 TRP LEU TYR TYR VAL ASN GLY ALA THR GLU THR SER GLN
SEQRES 28 C 355 VAL ALA PRO ALA
SEQRES 1 D 355 GLU THR GLY GLN SER VAL ASN ASP PRO GLY ASN MET SER
SEQRES 2 D 355 PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS GLY TYR
SEQRES 3 D 355 ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL
SEQRES 4 D 355 CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE ASP MET
SEQRES 5 D 355 VAL SER GLU VAL ASN MET ASP TYR THR LEU THR MET TYR
SEQRES 6 D 355 PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA TYR SER
SEQRES 7 D 355 GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG VAL ALA
SEQRES 8 D 355 ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU ASN ASP
SEQRES 9 D 355 LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS ASN ARG
SEQRES 10 D 355 MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU TYR GLY
SEQRES 11 D 355 LEU ARG ILE THR THR THR ALA ALA CYS MET MET ASP LEU
SEQRES 12 D 355 ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR LEU GLU
SEQRES 13 D 355 ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE GLU PHE
SEQRES 14 D 355 TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY VAL GLU
SEQRES 15 D 355 ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU HIS ARG
SEQRES 16 D 355 LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY ALA TYR
SEQRES 17 D 355 PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG ASN ILE
SEQRES 18 D 355 GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER ILE LEU
SEQRES 19 D 355 ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE ASN TYR
SEQRES 20 D 355 ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE THR THR
SEQRES 21 D 355 VAL LEU THR MET THR THR ILE ASN THR HIS LEU ARG GLU
SEQRES 22 D 355 THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE ASP MET
SEQRES 23 D 355 TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU
SEQRES 24 D 355 LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SER GLN
SEQRES 25 D 355 PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE
SEQRES 26 D 355 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR
SEQRES 27 D 355 TRP LEU TYR TYR VAL ASN GLY ALA THR GLU THR SER GLN
SEQRES 28 D 355 VAL ALA PRO ALA
SEQRES 1 E 355 GLU THR GLY GLN SER VAL ASN ASP PRO GLY ASN MET SER
SEQRES 2 E 355 PHE VAL LYS GLU THR VAL ASP LYS LEU LEU LYS GLY TYR
SEQRES 3 E 355 ASP ILE ARG LEU ARG PRO ASP PHE GLY GLY PRO PRO VAL
SEQRES 4 E 355 CYS VAL GLY MET ASN ILE ASP ILE ALA SER ILE ASP MET
SEQRES 5 E 355 VAL SER GLU VAL ASN MET ASP TYR THR LEU THR MET TYR
SEQRES 6 E 355 PHE GLN GLN TYR TRP ARG ASP LYS ARG LEU ALA TYR SER
SEQRES 7 E 355 GLY ILE PRO LEU ASN LEU THR LEU ASP ASN ARG VAL ALA
SEQRES 8 E 355 ASP GLN LEU TRP VAL PRO ASP THR TYR PHE LEU ASN ASP
SEQRES 9 E 355 LYS LYS SER PHE VAL HIS GLY VAL THR VAL LYS ASN ARG
SEQRES 10 E 355 MET ILE ARG LEU HIS PRO ASP GLY THR VAL LEU TYR GLY
SEQRES 11 E 355 LEU ARG ILE THR THR THR ALA ALA CYS MET MET ASP LEU
SEQRES 12 E 355 ARG ARG TYR PRO LEU ASP GLU GLN ASN CYS THR LEU GLU
SEQRES 13 E 355 ILE GLU SER TYR GLY TYR THR THR ASP ASP ILE GLU PHE
SEQRES 14 E 355 TYR TRP ARG GLY GLY ASP LYS ALA VAL THR GLY VAL GLU
SEQRES 15 E 355 ARG ILE GLU LEU PRO GLN PHE SER ILE VAL GLU HIS ARG
SEQRES 16 E 355 LEU VAL SER ARG ASN VAL VAL PHE ALA THR GLY ALA TYR
SEQRES 17 E 355 PRO ARG LEU SER LEU SER PHE ARG LEU LYS ARG ASN ILE
SEQRES 18 E 355 GLY TYR PHE ILE LEU GLN THR TYR MET PRO SER ILE LEU
SEQRES 19 E 355 ILE THR ILE LEU SER TRP VAL SER PHE TRP ILE ASN TYR
SEQRES 20 E 355 ASP ALA SER ALA ALA ARG VAL ALA LEU GLY ILE THR THR
SEQRES 21 E 355 VAL LEU THR MET THR THR ILE ASN THR HIS LEU ARG GLU
SEQRES 22 E 355 THR LEU PRO LYS ILE PRO TYR VAL LYS ALA ILE ASP MET
SEQRES 23 E 355 TYR LEU MET GLY CYS PHE VAL PHE VAL PHE LEU ALA LEU
SEQRES 24 E 355 LEU GLU TYR ALA PHE VAL ASN TYR ILE PHE PHE SER GLN
SEQRES 25 E 355 PRO ALA ARG ALA ALA ALA ILE ASP ARG TRP SER ARG ILE
SEQRES 26 E 355 VAL PHE PRO PHE THR PHE SER LEU PHE ASN LEU VAL TYR
SEQRES 27 E 355 TRP LEU TYR TYR VAL ASN GLY ALA THR GLU THR SER GLN
SEQRES 28 E 355 VAL ALA PRO ALA
MODRES 4COF ASN A 8 ASN GLYCOSYLATION SITE
MODRES 4COF ASN A 80 ASN GLYCOSYLATION SITE
MODRES 4COF ASN A 149 ASN GLYCOSYLATION SITE
MODRES 4COF ASN B 80 ASN GLYCOSYLATION SITE
MODRES 4COF ASN B 149 ASN GLYCOSYLATION SITE
MODRES 4COF ASN C 80 ASN GLYCOSYLATION SITE
MODRES 4COF ASN C 149 ASN GLYCOSYLATION SITE
MODRES 4COF ASN D 80 ASN GLYCOSYLATION SITE
MODRES 4COF ASN D 149 ASN GLYCOSYLATION SITE
MODRES 4COF ASN E 80 ASN GLYCOSYLATION SITE
MODRES 4COF ASN E 149 ASN GLYCOSYLATION SITE
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET NAG J 1 14
HET NAG J 2 14
HET BMA J 3 11
HET BEN A 500 9
HET NAG A1000 14
HET CL A1448 1
HET NAG A2000 14
HET BEN B 500 9
HET CL B1448 1
HET NAG B2000 14
HET BEN C 500 9
HET CL C1448 1
HET NAG C2000 14
HET BEN D 500 9
HET CL D1449 1
HET NAG D2000 14
HET BEN E 500 9
HET CL E1448 1
HET NAG E2000 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM BEN BENZAMIDINE
HETNAM CL CHLORIDE 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
FORMUL 6 NAG 16(C8 H15 N O6)
FORMUL 6 BMA 5(C6 H12 O6)
FORMUL 11 BEN 5(C7 H8 N2)
FORMUL 13 CL 5(CL 1-)
HELIX 1 1 MET A 9 LEU A 20 1 12
HELIX 2 2 ASN A 85 GLN A 90 1 6
HELIX 3 3 ILE A 218 TRP A 241 1 24
HELIX 4 4 SER A 247 THR A 271 1 25
HELIX 5 5 ALA A 280 ILE A 305 1 26
HELIX 6 6 PRO A 310 TYR A 446 1 30
HELIX 7 7 SER B 10 LEU B 20 1 11
HELIX 8 8 ASN B 85 GLN B 90 1 6
HELIX 9 9 ILE B 218 TRP B 241 1 24
HELIX 10 10 SER B 247 THR B 271 1 25
HELIX 11 11 ALA B 280 ILE B 305 1 26
HELIX 12 12 PRO B 310 TYR B 446 1 30
HELIX 13 13 SER C 10 LEU C 20 1 11
HELIX 14 14 ASN C 85 GLN C 90 1 6
HELIX 15 15 ILE C 218 TRP C 241 1 24
HELIX 16 16 SER C 247 THR C 271 1 25
HELIX 17 17 ALA C 280 ILE C 305 1 26
HELIX 18 18 PRO C 310 TYR C 446 1 30
HELIX 19 19 SER D 10 LEU D 20 1 11
HELIX 20 20 ASN D 85 GLN D 90 1 6
HELIX 21 21 ILE D 218 TRP D 241 1 24
HELIX 22 22 SER D 247 THR D 271 1 25
HELIX 23 23 ALA D 280 ILE D 305 1 26
HELIX 24 24 PRO D 310 TYR D 446 1 30
HELIX 25 25 SER E 10 LEU E 20 1 11
HELIX 26 26 ASN E 85 GLN E 90 1 6
HELIX 27 27 ILE E 218 TRP E 241 1 24
HELIX 28 28 SER E 247 THR E 271 1 25
HELIX 29 29 ALA E 280 ILE E 305 1 26
HELIX 30 30 PRO E 310 TYR E 446 1 30
SHEET 1 AA60 VAL A 36 SER A 51 0
SHEET 2 AA60 ASP A 56 ASP A 69 0
SHEET 3 AA60 LEU A 81 LEU A 83 0
SHEET 4 AA60 THR A 96 PHE A 98 0
SHEET 5 AA60 ASP A 101 VAL A 106 0
SHEET 6 AA60 ARG A 114 HIS A 119 0
SHEET 7 AA60 THR A 123 ALA A 135 0
SHEET 8 AA60 ASP A 146 SER A 156 0
SHEET 9 AA60 ILE A 164 TRP A 168 0
SHEET 10 AA60 VAL A 175 GLY A 177 0
SHEET 11 AA60 PHE A 186 VAL A 199 0
SHEET 12 AA60 ALA A 204 ARG A 216 0
SHEET 13 AA60 VAL B 36 SER B 51 0
SHEET 14 AA60 ASP B 56 ASP B 69 0
SHEET 15 AA60 LEU B 81 LEU B 83 0
SHEET 16 AA60 THR B 96 PHE B 98 0
SHEET 17 AA60 ASP B 101 VAL B 106 0
SHEET 18 AA60 ARG B 114 HIS B 119 0
SHEET 19 AA60 THR B 123 ALA B 135 0
SHEET 20 AA60 ASP B 146 SER B 156 0
SHEET 21 AA60 ILE B 164 TRP B 168 0
SHEET 22 AA60 VAL B 175 GLY B 177 0
SHEET 23 AA60 PHE B 186 VAL B 199 0
SHEET 24 AA60 ALA B 204 ARG B 216 0
SHEET 25 AA60 VAL C 36 SER C 51 0
SHEET 26 AA60 ASP C 56 ASP C 69 0
SHEET 27 AA60 LEU C 81 LEU C 83 0
SHEET 28 AA60 THR C 96 PHE C 98 0
SHEET 29 AA60 ASP C 101 VAL C 106 0
SHEET 30 AA60 ARG C 114 HIS C 119 0
SHEET 31 AA60 THR C 123 ALA C 135 0
SHEET 32 AA60 ASP C 146 SER C 156 0
SHEET 33 AA60 ILE C 164 TRP C 168 0
SHEET 34 AA60 VAL C 175 GLY C 177 0
SHEET 35 AA60 PHE C 186 VAL C 199 0
SHEET 36 AA60 ALA C 204 ARG C 216 0
SHEET 37 AA60 VAL D 36 SER D 51 0
SHEET 38 AA60 ASP D 56 ASP D 69 0
SHEET 39 AA60 LEU D 81 LEU D 83 0
SHEET 40 AA60 THR D 96 PHE D 98 0
SHEET 41 AA60 ASP D 101 VAL D 106 0
SHEET 42 AA60 ARG D 114 HIS D 119 0
SHEET 43 AA60 THR D 123 ALA D 135 0
SHEET 44 AA60 ASP D 146 SER D 156 0
SHEET 45 AA60 ILE D 164 TRP D 168 0
SHEET 46 AA60 VAL D 175 GLY D 177 0
SHEET 47 AA60 PHE D 186 VAL D 199 0
SHEET 48 AA60 ALA D 204 ARG D 216 0
SHEET 49 AA60 VAL E 36 SER E 51 0
SHEET 50 AA60 ASP E 56 ASP E 69 0
SHEET 51 AA60 LEU E 81 LEU E 83 0
SHEET 52 AA60 THR E 96 PHE E 98 0
SHEET 53 AA60 ASP E 101 VAL E 106 0
SHEET 54 AA60 ARG E 114 HIS E 119 0
SHEET 55 AA60 THR E 123 ALA E 135 0
SHEET 56 AA60 ASP E 146 SER E 156 0
SHEET 57 AA60 ILE E 164 TRP E 168 0
SHEET 58 AA60 VAL E 175 GLY E 177 0
SHEET 59 AA60 PHE E 186 VAL E 199 0
SHEET 60 AA60 ALA E 204 ARG E 216 0
SSBOND 1 CYS A 136 CYS A 150 1555 1555 2.06
SSBOND 2 CYS B 136 CYS B 150 1555 1555 2.07
SSBOND 3 CYS C 136 CYS C 150 1555 1555 2.07
SSBOND 4 CYS D 136 CYS D 150 1555 1555 2.07
SSBOND 5 CYS E 136 CYS E 150 1555 1555 2.06
LINK ND2 ASN A 8 C1 NAG A1000 1555 1555 1.43
LINK ND2 ASN A 80 C1 NAG A2000 1555 1555 1.43
LINK ND2 ASN A 149 C1 NAG F 1 1555 1555 1.43
LINK ND2 ASN B 80 C1 NAG B2000 1555 1555 1.43
LINK ND2 ASN B 149 C1 NAG G 1 1555 1555 1.43
LINK ND2 ASN C 80 C1 NAG C2000 1555 1555 1.43
LINK ND2 ASN C 149 C1 NAG H 1 1555 1555 1.43
LINK ND2 ASN D 80 C1 NAG D2000 1555 1555 1.43
LINK ND2 ASN D 149 C1 NAG I 1 1555 1555 1.43
LINK ND2 ASN E 80 C1 NAG E2000 1555 1555 1.43
LINK ND2 ASN E 149 C1 NAG J 1 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.42
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.43
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.42
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.43
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.42
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.43
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.42
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.43
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.43
LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44
CISPEP 1 VAL A 109 THR A 110 0 0.89
CISPEP 2 TYR A 143 PRO A 144 0 7.34
CISPEP 3 VAL B 109 THR B 110 0 -0.29
CISPEP 4 TYR B 143 PRO B 144 0 3.65
CISPEP 5 VAL C 109 THR C 110 0 1.15
CISPEP 6 TYR C 143 PRO C 144 0 4.76
CISPEP 7 VAL D 109 THR D 110 0 1.51
CISPEP 8 TYR D 143 PRO D 144 0 6.35
CISPEP 9 VAL E 109 THR E 110 0 3.50
CISPEP 10 TYR E 143 PRO E 144 0 4.40
CRYST1 174.100 108.900 207.440 90.00 107.43 90.00 C 1 2 1 20
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 0.005744 0.000000 0.001803 0.00000
SCALE2 0.000000 0.009183 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005053 0.00000
MTRIX1 1 0.396000 0.889700 0.227200 -28.91860 1
MTRIX2 1 -0.892200 0.314400 0.324300 -42.96190 1
MTRIX3 1 0.217100 -0.331100 0.918300 10.35590 1
MTRIX1 2 -0.584600 0.557700 0.589300 -76.73000 1
MTRIX2 2 -0.562400 -0.802000 0.201200 -27.97000 1
MTRIX3 2 0.584800 -0.213800 0.782500 28.29000 1
MTRIX1 3 -0.591500 -0.555200 0.584700 -76.88000 1
MTRIX2 3 0.549900 -0.808100 -0.211100 25.90000 1
MTRIX3 3 0.589700 0.196600 0.783300 28.46000 1
MTRIX1 4 0.385500 -0.894700 0.225700 -30.55000 1
MTRIX2 4 0.893600 0.301000 -0.332900 42.87000 1
MTRIX3 4 0.229900 0.330000 0.915500 11.43000 1
(ATOM LINES ARE NOT SHOWN.)
END
