HEADER TRANSPORT PROTEIN/TOXIN 02-JAN-16 5HBV
TITLE COMPLEX STRUCTURE OF FAB35 AND MOUSE NACHR ALPHA1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN ISOFORM V31;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 22-95;
COMPND 5 SYNONYM: BGTX V31,LONG NEUROTOXIN 1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA 1;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 22-231;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: FAB35, LIGHT CHAIN;
COMPND 14 CHAIN: C;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: FAB35, HEAVY CHAIN;
COMPND 17 CHAIN: D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;
SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT;
SOURCE 4 ORGANISM_TAXID: 8616;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 GENE: CHRNA1, ACRA;
SOURCE 10 EXPRESSION_SYSTEM: PICHIA;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 4919;
SOURCE 12 MOL_ID: 3;
SOURCE 13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 14 ORGANISM_COMMON: NORWAY RAT;
SOURCE 15 ORGANISM_TAXID: 10116;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 18 ORGANISM_COMMON: NORWAY RAT;
SOURCE 19 ORGANISM_TAXID: 10116
KEYWDS NICOTINIC ACETYLCHOLINE RECEPTOR ALPHA1, FAB35, COMPLEX, MYASTHENIA
KEYWDS 2 GRAVIS, TRANSPORT PROTEIN-TOXIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.NORIDOMI,G.WATANABE,M.N.HANSEN,G.W.HAN,L.CHEN
REVDAT 3 29-JUL-20 5HBV 1 COMPND REMARK HETNAM SSBOND
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 10-MAY-17 5HBV 1 JRNL
REVDAT 1 03-MAY-17 5HBV 0
JRNL AUTH K.NORIDOMI,G.WATANABE,M.N.HANSEN,G.W.HAN,L.CHEN
JRNL TITL STRUCTURAL INSIGHTS INTO THE MOLECULAR MECHANISMS OF
JRNL TITL 2 MYASTHENIA GRAVIS AND THEIR THERAPEUTIC IMPLICATIONS.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28440223
JRNL DOI 10.7554/ELIFE.23043
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 21877
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1117
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1563
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3700
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5554
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.76000
REMARK 3 B22 (A**2) : -1.07000
REMARK 3 B33 (A**2) : -3.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.85000
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): 0.376
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.357
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.720
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5817 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5147 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7954 ; 1.216 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12035 ; 0.876 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 712 ; 6.626 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 232 ;32.967 ;24.353
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 917 ;15.251 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;17.766 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 926 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6303 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1126 ; 0.001 ; 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): 2860 ; 2.589 ; 7.057
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2859 ; 2.588 ; 7.056
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3568 ; 4.508 ;10.576
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3569 ; 4.508 ;10.577
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2957 ; 2.120 ; 7.003
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2957 ; 2.120 ; 7.003
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4387 ; 3.687 ;10.478
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5940 ; 6.562 ;78.561
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5939 ; 6.563 ;78.580
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 5HBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-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 : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26304
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
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 (%) : 95.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 43.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.94400
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE TRIHYDRATE, CALCIUM
REMARK 280 ACETATE HYDRATE, PEG 8000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 79.95250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.01200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.95250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.01200
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 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 C 212
REMARK 465 CYS C 213
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 ARG A 72 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 77 CE NZ
REMARK 470 PHE B 137 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 210 CZ NH1 NH2
REMARK 470 LEU D 166 CG CD1 CD2
REMARK 470 TRP D 195 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 195 CZ3 CH2
REMARK 470 GLN D 209 CG CD OE1 NE2
REMARK 470 GLN D 210 CG CD OE1 NE2
REMARK 470 HIS D 211 CG ND1 CD2 CE1 NE2
REMARK 470 ARG D 216 CG CD NE CZ NH1 NH2
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 ASP A 30 -166.87 -112.32
REMARK 500 GLU A 56 79.08 -150.67
REMARK 500 ASN A 66 55.14 -118.89
REMARK 500 LEU B 56 79.86 -107.38
REMARK 500 ALA B 181 119.78 -166.76
REMARK 500 LEU C 47 -61.69 -96.73
REMARK 500 LYS C 50 57.74 39.20
REMARK 500 THR C 51 -53.08 67.75
REMARK 500 TYR C 91 31.10 -145.44
REMARK 500 ASN C 137 78.63 63.44
REMARK 500 SER D 68 113.41 -165.05
REMARK 500 ARG D 102 -117.02 52.48
REMARK 500 LEU D 137 -73.60 -76.19
REMARK 500 ASN D 162 73.89 31.19
REMARK 500 SER D 163 -97.75 61.93
REMARK 500 SER D 167 -106.91 58.12
REMARK 500 SER D 179 71.93 -153.53
REMARK 500 LEU D 218 58.19 -102.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HBT RELATED DB: PDB
REMARK 900 5HBT IS A COMPLEX WITH HUMAN NACHR, AND THIS IS WITH MOUSE NACHR.
DBREF 5HBV B 2 211 UNP P04756 ACHA_MOUSE 22 231
DBREF 5HBV C 1 213 PDB 5HBV 5HBV 1 213
DBREF 5HBV D 1 219 PDB 5HBV 5HBV 1 219
DBREF 5HBV A 1 74 UNP P60616 3L21V_BUNMU 22 95
SEQADV 5HBV LYS B 0 UNP P04756 EXPRESSION TAG
SEQADV 5HBV SER B 1 UNP P04756 EXPRESSION TAG
SEQADV 5HBV GLU B 8 UNP P04756 VAL 28 ENGINEERED MUTATION
SEQADV 5HBV ARG B 149 UNP P04756 TRP 169 ENGINEERED MUTATION
SEQADV 5HBV ALA B 155 UNP P04756 VAL 175 ENGINEERED MUTATION
SEQRES 1 A 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA
SEQRES 2 A 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS
SEQRES 3 A 74 MET TRP CYS ASP VAL PHE CYS SER SER ARG GLY LYS VAL
SEQRES 4 A 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS
SEQRES 5 A 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS
SEQRES 6 A 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY
SEQRES 1 B 212 LYS SER GLU HIS GLU THR ARG LEU GLU ALA LYS LEU PHE
SEQRES 2 B 212 GLU ASP TYR SER SER VAL VAL ARG PRO VAL GLU ASP HIS
SEQRES 3 B 212 ARG GLU ILE VAL GLN VAL THR VAL GLY LEU GLN LEU ILE
SEQRES 4 B 212 GLN LEU ILE ASN VAL ASP GLU VAL ASN GLN ILE VAL THR
SEQRES 5 B 212 THR ASN VAL ARG LEU LYS GLN GLN TRP VAL ASP TYR ASN
SEQRES 6 B 212 LEU LYS TRP ASN PRO ASP ASP TYR GLY GLY VAL LYS LYS
SEQRES 7 B 212 ILE HIS ILE PRO SER GLU LYS ILE TRP ARG PRO ASP VAL
SEQRES 8 B 212 VAL LEU TYR ASN ASN ALA ASP GLY ASP PHE ALA ILE VAL
SEQRES 9 B 212 LYS PHE THR LYS VAL LEU LEU ASP TYR THR GLY HIS ILE
SEQRES 10 B 212 THR TRP THR PRO PRO ALA ILE PHE LYS SER TYR CYS GLU
SEQRES 11 B 212 ILE ILE VAL THR HIS PHE PRO PHE ASP GLU GLN ASN CYS
SEQRES 12 B 212 SER MET LYS LEU GLY THR ARG THR TYR ASP GLY SER ALA
SEQRES 13 B 212 VAL ALA ILE ASN PRO GLU SER ASP GLN PRO ASP LEU SER
SEQRES 14 B 212 ASN PHE MET GLU SER GLY GLU TRP VAL ILE LYS GLU ALA
SEQRES 15 B 212 ARG GLY TRP LYS HIS TRP VAL PHE TYR SER CYS CYS PRO
SEQRES 16 B 212 THR THR PRO TYR LEU ASP ILE THR TYR HIS PHE VAL MET
SEQRES 17 B 212 GLN ARG LEU PRO
SEQRES 1 C 213 ASP ILE VAL ILE THR GLN SER PRO SER LEU LEU SER ALA
SEQRES 2 C 213 SER VAL GLY ASP ARG VAL THR LEU THR CYS LYS GLY SER
SEQRES 3 C 213 GLN ASN ILE ASP ASN TYR LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 C 213 LEU GLY GLU ALA PRO LYS LEU LEU ILE TYR LYS THR ASN
SEQRES 5 C 213 SER LEU GLN THR GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 C 213 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU
SEQRES 7 C 213 HIS SER GLU ASP LEU ALA THR TYR TYR CYS TYR GLN TYR
SEQRES 8 C 213 ILE ASN GLY TYR THR PHE GLY THR GLY THR LYS LEU GLU
SEQRES 9 C 213 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 C 213 PRO PRO SER THR GLU GLN LEU ALA THR GLY GLY ALA SER
SEQRES 11 C 213 VAL VAL CYS LEU MET ASN ASN PHE TYR PRO ARG ASP ILE
SEQRES 12 C 213 SER VAL LYS TRP LYS ILE ASP GLY THR GLU ARG ARG ASP
SEQRES 13 C 213 GLY VAL LEU ASP SER VAL THR ASP GLN ASP SER LYS ASP
SEQRES 14 C 213 SER THR TYR SER MET SER SER THR LEU SER LEU THR LYS
SEQRES 15 C 213 ALA ASP TYR GLU SER HIS ASN LEU TYR THR CYS GLU VAL
SEQRES 16 C 213 VAL HIS LYS THR SER SER SER PRO VAL VAL LYS SER PHE
SEQRES 17 C 213 ASN ARG ASN GLU CYS
SEQRES 1 D 219 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL GLN
SEQRES 2 D 219 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY
SEQRES 3 D 219 PHE SER LEU THR SER TYR SER VAL SER TRP LEU ARG GLN
SEQRES 4 D 219 PRO SER GLY LYS GLY PRO GLU TRP MET GLY ARG MET TRP
SEQRES 5 D 219 ASP ASP GLY GLY THR VAL TYR ASN SER GLY LEU LYS SER
SEQRES 6 D 219 ARG LEU SER ILE SER ARG ASP THR SER LYS ASN GLN VAL
SEQRES 7 D 219 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR GLY
SEQRES 8 D 219 THR TYR TYR CYS THR ARG ASP GLU ARG ILE ARG ALA ILE
SEQRES 9 D 219 ASN TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 D 219 VAL SER SER ALA GLU THR THR ALA PRO SER VAL TYR PRO
SEQRES 11 D 219 LEU ALA PRO GLY THR ALA LEU LYS SER ASN SER MET VAL
SEQRES 12 D 219 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 D 219 VAL THR VAL THR TRP ASN SER GLY ALA LEU SER SER GLY
SEQRES 14 D 219 VAL HIS THR PHE PRO ALA VAL LEU GLN SER GLY LEU TYR
SEQRES 15 D 219 THR LEU THR SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 D 219 PRO SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO GLY
SEQRES 17 D 219 GLN GLN HIS GLN ARG TRP THR ARG LYS LEU CYS
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET MAN E 6 11
HET MAN E 7 11
HET MAN E 8 11
HET MAN E 9 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 5 BMA C6 H12 O6
FORMUL 5 MAN 6(C6 H12 O6)
FORMUL 6 HOH *46(H2 O)
HELIX 1 AA1 PHE A 32 GLY A 37 1 6
HELIX 2 AA2 SER B 1 GLU B 13 1 13
HELIX 3 AA3 ASN B 68 GLY B 73 5 6
HELIX 4 AA4 GLU B 83 ILE B 85 5 3
HELIX 5 AA5 HIS C 79 LEU C 83 5 5
HELIX 6 AA6 SER C 120 THR C 126 1 7
HELIX 7 AA7 THR C 181 SER C 187 1 7
HELIX 8 AA8 SER D 61 LYS D 64 5 4
HELIX 9 AA9 GLN D 86 ASP D 89 5 4
HELIX 10 AB1 LEU D 166 SER D 168 5 3
HELIX 11 AB2 SER D 193 GLN D 198 1 6
SHEET 1 AA1 2 VAL A 2 THR A 5 0
SHEET 2 AA1 2 SER A 12 THR A 15 -1 O VAL A 14 N CYS A 3
SHEET 1 AA2 9 GLU A 56 CYS A 60 0
SHEET 2 AA2 9 LEU A 22 TRP A 28 -1 N CYS A 23 O CYS A 60
SHEET 3 AA2 9 VAL A 39 ALA A 45 -1 O VAL A 39 N TRP A 28
SHEET 4 AA2 9 TRP B 176 TYR B 190 -1 O PHE B 189 N VAL A 40
SHEET 5 AA2 9 CYS B 193 ARG B 209 -1 O ASP B 200 N HIS B 186
SHEET 6 AA2 9 GLU B 139 THR B 148 -1 N MET B 144 O TYR B 203
SHEET 7 AA2 9 PRO B 121 ILE B 130 -1 N GLU B 129 O ASN B 141
SHEET 8 AA2 9 ILE B 49 LYS B 66 -1 N THR B 52 O PHE B 124
SHEET 9 AA2 9 VAL B 90 TYR B 93 0
SHEET 1 AA3 8 LYS B 77 PRO B 81 0
SHEET 2 AA3 8 LYS B 107 ASP B 111 -1 O LEU B 110 N ILE B 78
SHEET 3 AA3 8 THR B 113 TRP B 118 -1 O THR B 117 N LEU B 109
SHEET 4 AA3 8 ILE B 49 LYS B 66 -1 N GLN B 58 O TRP B 118
SHEET 5 AA3 8 PRO B 121 ILE B 130 -1 O PHE B 124 N THR B 52
SHEET 6 AA3 8 GLU B 139 THR B 148 -1 O ASN B 141 N GLU B 129
SHEET 7 AA3 8 VAL B 29 ASP B 44 0
SHEET 8 AA3 8 VAL B 156 PRO B 160 1 O ASN B 159 N VAL B 31
SHEET 1 AA4 4 ILE C 4 SER C 7 0
SHEET 2 AA4 4 VAL C 19 GLY C 25 -1 O THR C 22 N SER C 7
SHEET 3 AA4 4 ASP C 70 ILE C 75 -1 O LEU C 73 N LEU C 21
SHEET 4 AA4 4 PHE C 62 SER C 67 -1 N SER C 65 O THR C 72
SHEET 1 AA5 6 LEU C 10 ALA C 13 0
SHEET 2 AA5 6 THR C 101 LEU C 105 1 O GLU C 104 N LEU C 11
SHEET 3 AA5 6 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 101
SHEET 4 AA5 6 LEU C 33 GLN C 38 -1 N ALA C 34 O TYR C 89
SHEET 5 AA5 6 LYS C 45 TYR C 49 -1 O LYS C 45 N GLN C 37
SHEET 6 AA5 6 SER C 53 LEU C 54 -1 O SER C 53 N TYR C 49
SHEET 1 AA6 4 LEU C 10 ALA C 13 0
SHEET 2 AA6 4 THR C 101 LEU C 105 1 O GLU C 104 N LEU C 11
SHEET 3 AA6 4 THR C 85 GLN C 90 -1 N TYR C 86 O THR C 101
SHEET 4 AA6 4 THR C 96 PHE C 97 -1 O THR C 96 N GLN C 90
SHEET 1 AA7 4 THR C 113 PHE C 117 0
SHEET 2 AA7 4 ALA C 129 PHE C 138 -1 O ASN C 136 N THR C 113
SHEET 3 AA7 4 TYR C 172 LEU C 180 -1 O LEU C 180 N ALA C 129
SHEET 4 AA7 4 VAL C 158 VAL C 162 -1 N SER C 161 O SER C 175
SHEET 1 AA8 4 THR C 152 GLU C 153 0
SHEET 2 AA8 4 ILE C 143 ILE C 149 -1 N ILE C 149 O THR C 152
SHEET 3 AA8 4 TYR C 191 HIS C 197 -1 O GLU C 194 N LYS C 146
SHEET 4 AA8 4 VAL C 204 PHE C 208 -1 O LYS C 206 N CYS C 193
SHEET 1 AA9 4 GLN D 3 SER D 7 0
SHEET 2 AA9 4 LEU D 18 SER D 25 -1 O THR D 23 N GLN D 5
SHEET 3 AA9 4 GLN D 77 MET D 82 -1 O VAL D 78 N CYS D 22
SHEET 4 AA9 4 LEU D 67 ASP D 72 -1 N ASP D 72 O GLN D 77
SHEET 1 AB1 6 LEU D 11 VAL D 12 0
SHEET 2 AB1 6 LEU D 115 VAL D 118 1 O THR D 117 N VAL D 12
SHEET 3 AB1 6 GLY D 91 ILE D 101 -1 N GLY D 91 O VAL D 116
SHEET 4 AB1 6 SER D 33 PRO D 40 -1 N LEU D 37 O TYR D 94
SHEET 5 AB1 6 GLU D 46 MET D 51 -1 O MET D 51 N VAL D 34
SHEET 6 AB1 6 THR D 57 TYR D 59 -1 O VAL D 58 N ARG D 50
SHEET 1 AB2 4 LEU D 11 VAL D 12 0
SHEET 2 AB2 4 LEU D 115 VAL D 118 1 O THR D 117 N VAL D 12
SHEET 3 AB2 4 GLY D 91 ILE D 101 -1 N GLY D 91 O VAL D 116
SHEET 4 AB2 4 ILE D 104 TRP D 110 -1 O ILE D 104 N ILE D 101
SHEET 1 AB3 4 SER D 127 LEU D 131 0
SHEET 2 AB3 4 VAL D 143 TYR D 152 -1 O LYS D 150 N SER D 127
SHEET 3 AB3 4 TYR D 182 VAL D 190 -1 O LEU D 184 N VAL D 149
SHEET 4 AB3 4 VAL D 170 THR D 172 -1 N HIS D 171 O SER D 187
SHEET 1 AB4 4 SER D 127 LEU D 131 0
SHEET 2 AB4 4 VAL D 143 TYR D 152 -1 O LYS D 150 N SER D 127
SHEET 3 AB4 4 TYR D 182 VAL D 190 -1 O LEU D 184 N VAL D 149
SHEET 4 AB4 4 VAL D 176 LEU D 177 -1 N VAL D 176 O THR D 183
SHEET 1 AB5 3 THR D 158 TRP D 161 0
SHEET 2 AB5 3 THR D 201 HIS D 206 -1 O ASN D 203 N THR D 160
SHEET 3 AB5 3 HIS D 211 ARG D 216 -1 O HIS D 211 N HIS D 206
SSBOND 1 CYS A 3 CYS A 16 1555 1555 2.09
SSBOND 2 CYS A 3 CYS A 23 1555 1555 2.05
SSBOND 3 CYS A 16 CYS A 44 1555 1555 2.03
SSBOND 4 CYS A 29 CYS A 33 1555 1555 2.07
SSBOND 5 CYS A 48 CYS A 59 1555 1555 2.04
SSBOND 6 CYS A 60 CYS A 65 1555 1555 2.03
SSBOND 7 CYS B 128 CYS B 142 1555 1555 2.04
SSBOND 8 CYS B 192 CYS B 193 1555 1555 2.06
SSBOND 9 CYS C 23 CYS C 88 1555 1555 2.05
SSBOND 10 CYS C 133 CYS C 193 1555 1555 2.03
SSBOND 11 CYS D 22 CYS D 95 1555 1555 2.04
SSBOND 12 CYS D 147 CYS D 202 1555 1555 2.04
LINK ND2 ASN B 141 C1 NAG E 1 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.43
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.44
LINK O6 BMA E 3 C1 MAN E 7 1555 1555 1.44
LINK O2 MAN E 4 C1 MAN E 5 1555 1555 1.44
LINK O2 MAN E 5 C1 MAN E 6 1555 1555 1.45
LINK O3 MAN E 7 C1 MAN E 8 1555 1555 1.45
LINK O6 MAN E 7 C1 MAN E 9 1555 1555 1.45
CISPEP 1 SER A 9 PRO A 10 0 -1.53
CISPEP 2 SER C 7 PRO C 8 0 -10.30
CISPEP 3 TYR C 139 PRO C 140 0 -1.64
CISPEP 4 PHE D 153 PRO D 154 0 -3.18
CISPEP 5 GLU D 155 PRO D 156 0 1.52
CRYST1 159.905 42.024 137.583 90.00 116.46 90.00 C 1 2 1 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 0.006254 0.000000 0.003112 0.00000
SCALE2 0.000000 0.023796 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008119 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
