HEADER APOPTOSIS 15-DEC-15 5FCG
TITLE CRYSTAL STRUCTURE OF BCL-2 IN COMPLEX WITH HBX-BH3 MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN X;
COMPND 8 CHAIN: C;
COMPND 9 FRAGMENT: UNP RESIDUES 110-135;
COMPND 10 SYNONYM: HBX,PEPTIDE X,PX;
COMPND 11 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: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HEPATITIS B VIRUS;
SOURCE 11 ORGANISM_COMMON: HBV;
SOURCE 12 ORGANISM_TAXID: 10407
KEYWDS COMPLEX, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR T.Y.JIANG,M.H.LIU,J.P.WU,Y.G.SHI
REVDAT 2 24-FEB-16 5FCG 1 JRNL ATOM HETATM
REVDAT 1 10-FEB-16 5FCG 0
JRNL AUTH T.Y.JIANG,M.H.LIU,J.P.WU,Y.G.SHI
JRNL TITL STRUCTURAL AND BIOCHEMICAL ANALYSIS OF BCL-2 INTERACTION
JRNL TITL 2 WITH THE HEPATITIS B VIRUS PROTEIN HBX
JRNL REF PROC.NATL.ACAD.SCI.USA 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26858413
JRNL DOI 10.1073/PNAS.1525616113
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 10804
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 518
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.7860 - 3.3306 1.00 2709 134 0.2214 0.2244
REMARK 3 2 3.3306 - 2.6438 1.00 2598 130 0.2571 0.2805
REMARK 3 3 2.6438 - 2.3097 1.00 2568 117 0.2658 0.3293
REMARK 3 4 2.3097 - 2.0986 0.96 2411 137 0.3520 0.3814
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.021 1503
REMARK 3 ANGLE : 2.037 2030
REMARK 3 CHIRALITY : 0.143 207
REMARK 3 PLANARITY : 0.009 264
REMARK 3 DIHEDRAL : 19.222 541
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 75.2023 181.2699 3.0680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1293 T22: 0.1420
REMARK 3 T33: 0.1016 T12: -0.0079
REMARK 3 T13: 0.0197 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.8013 L22: 2.2666
REMARK 3 L33: 1.2659 L12: 0.0988
REMARK 3 L13: 0.2004 L23: -0.2150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: -0.0634 S13: 0.0595
REMARK 3 S21: 0.0364 S22: -0.0187 S23: -0.0202
REMARK 3 S31: -0.0281 S32: 0.0275 S33: 0.0330
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6 - 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10943
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.16800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2XA0
REMARK 200
REMARK 200 REMARK: NEDDLE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM ACETATE, 500MM AMMONIUM
REMARK 280 SULFATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 31.88850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.49500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.88850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.49500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 ALA A 1
REMARK 465 HIS A 2
REMARK 465 MET A 3
REMARK 465 ALA A 4
REMARK 465 HIS A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 7
REMARK 465 ASN A 41
REMARK 465 ARG A 42
REMARK 465 THR A 43
REMARK 465 GLU A 44
REMARK 465 ALA A 45
REMARK 465 PRO A 46
REMARK 465 GLU A 47
REMARK 465 PRO A 165
REMARK 465 SER A 166
REMARK 465 MET A 167
REMARK 465 ARG A 168
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 NZ LYS C 118 O HOH C 201 1.82
REMARK 500 OD1 ASP A 12 O HOH A 301 1.82
REMARK 500 N ALA A 87 O HOH A 302 1.87
REMARK 500 OE1 GLU A 75 O HOH A 303 1.90
REMARK 500 O HOH A 361 O HOH C 207 1.90
REMARK 500 NH2 ARG A 67 O HOH A 304 1.99
REMARK 500 O HOH A 302 O HOH A 314 2.00
REMARK 500 CZ ARG A 70 O HOH A 305 2.05
REMARK 500 NH2 ARG A 70 O HOH A 305 2.05
REMARK 500 OD1 ASP A 64 O HOH A 306 2.07
REMARK 500 O SER A 77 O HOH A 307 2.10
REMARK 500 NH1 ARG A 67 O HOH A 308 2.14
REMARK 500 CD GLU A 75 O HOH A 303 2.16
REMARK 500 O HOH C 204 O HOH C 209 2.17
REMARK 500 CA ASP A 12 O HOH A 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 39 NH1 ARG A 107 4595 1.79
REMARK 500 NE2 GLN A 27 OE1 GLN A 151 1556 2.14
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 ASP A 33 CB ASP A 33 CG -0.170
REMARK 500 HIS A 81 C HIS A 81 O -0.123
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 ASP A 33 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 71 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 ARG A 71 CA - C - O ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG A 71 CA - C - N ANGL. DEV. = -16.4 DEGREES
REMARK 500 CYS C 115 CA - CB - SG ANGL. DEV. = 10.7 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 GLU A 39 -45.52 117.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A 81 LEU A 82 105.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE REFERENCE SEQUENCE DATABASE FOR CHAIN A DOES NOT CURRENTLY
REMARK 999 EXIST. RESIDUE ALA A 36 IS MUTATION.
DBREF 5FCG A 1 168 PDB 5FCG 5FCG 1 168
DBREF 5FCG C 110 135 UNP E9L5H4 E9L5H4_HBV 110 135
SEQRES 1 A 168 ALA HIS MET ALA HIS ALA GLY ARG SER GLY TYR ASP ASN
SEQRES 2 A 168 ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER
SEQRES 3 A 168 GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP ALA GLU
SEQRES 4 A 168 GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU
SEQRES 5 A 168 VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP PHE
SEQRES 6 A 168 SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER
SEQRES 7 A 168 GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY CYS PHE
SEQRES 8 A 168 ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN
SEQRES 9 A 168 TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL
SEQRES 10 A 168 MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU
SEQRES 11 A 168 VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN
SEQRES 12 A 168 ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP
SEQRES 13 A 168 ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 C 26 GLU TYR ILE LYS ASP CYS VAL PHE LYS ASP TRP GLU GLU
SEQRES 2 C 26 LEU GLY GLU GLU ILE ARG LEU LYS VAL PHE VAL LEU GLY
FORMUL 3 HOH *93(H2 O)
HELIX 1 AA1 ARG A 8 GLN A 27 1 20
HELIX 2 AA2 THR A 49 PHE A 73 1 25
HELIX 3 AA3 GLU A 75 LEU A 80 5 6
HELIX 4 AA4 THR A 86 ARG A 100 1 15
HELIX 5 AA5 ASN A 104 ARG A 125 1 22
HELIX 6 AA6 PRO A 129 LEU A 146 1 18
HELIX 7 AA7 LEU A 146 ASN A 153 1 8
HELIX 8 AA8 GLY A 154 GLU A 161 1 8
HELIX 9 AA9 LEU A 162 GLY A 164 5 3
HELIX 10 AB1 LYS C 113 LYS C 130 1 18
CISPEP 1 GLU C 110 TYR C 111 0 -10.59
CRYST1 63.777 82.990 33.487 90.00 90.00 90.00 P 21 21 2 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 0.015680 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012050 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029862 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
