HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 24-JUN-13 4LCW
TITLE THE STRUCTURE OF HUMAN MAIT TCR IN COMPLEX WITH MR1-K43A-RL-6-ME-7OH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I-RELATED GENE
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, C;
COMPND 5 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 23-292;
COMPND 6 SYNONYM: MHC CLASS I-RELATED GENE PROTEIN, CLASS I HISTOCOMPATIBILITY
COMPND 7 ANTIGEN-LIKE PROTEIN;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 12 CHAIN: B, F;
COMPND 13 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: MAIT T CELL RECEPTOR ALPHA CHAIN;
COMPND 17 CHAIN: D, G;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: MAIT T CELL RECEPTOR BETA CHAIN;
COMPND 21 CHAIN: E, H;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MR1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: B2M;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: TCR ALPHA;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PET30;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 30 ORGANISM_COMMON: HUMAN;
SOURCE 31 ORGANISM_TAXID: 9606;
SOURCE 32 GENE: TCR BETA;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 35 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 36 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS MHC CLASS I-RELATED PROTEIN, MAIT T CELL RECEPTOR, VITAMIN B2
KEYWDS 2 METABOLITES, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.PATEL,J.ROSSJOHN
REVDAT 3 20-SEP-23 4LCW 1 REMARK SEQADV
REVDAT 2 20-NOV-13 4LCW 1 JRNL
REVDAT 1 02-OCT-13 4LCW 0
JRNL AUTH R.REANTRAGOON,A.J.CORBETT,I.G.SAKALA,N.A.GHERARDIN,
JRNL AUTH 2 J.B.FURNESS,Z.CHEN,S.B.ECKLE,A.P.ULDRICH,R.W.BIRKINSHAW,
JRNL AUTH 3 O.PATEL,L.KOSTENKO,B.MEEHAN,K.KEDZIERSKA,L.LIU,D.P.FAIRLIE,
JRNL AUTH 4 T.H.HANSEN,D.I.GODFREY,J.ROSSJOHN,J.MCCLUSKEY,L.KJER-NIELSEN
JRNL TITL ANTIGEN-LOADED MR1 TETRAMERS DEFINE T CELL RECEPTOR
JRNL TITL 2 HETEROGENEITY IN MUCOSAL-ASSOCIATED INVARIANT T CELLS.
JRNL REF J.EXP.MED. V. 210 2305 2013
JRNL REFN ISSN 0022-1007
JRNL PMID 24101382
JRNL DOI 10.1084/JEM.20130958
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 80339
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : COPIED FROM 4L4T
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4021
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.46
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5912
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2142
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5613
REMARK 3 BIN R VALUE (WORKING SET) : 0.2121
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.06
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 299
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 : 12397
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.74
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.82590
REMARK 3 B22 (A**2) : -9.25240
REMARK 3 B33 (A**2) : 1.42650
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.48900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.271
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.284
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.924
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 12824 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 17487 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 5659 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 295 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1880 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 12824 ; 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 : 1654 ; 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 : 13953 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.50
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.94
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4LCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95453
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80366
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 75.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.68600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 4L4V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M BIS-TRIS
REMARK 280 -PROPANE PH 6.5 AND 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 107.95750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.68050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.95750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.68050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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, G, H
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
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 ASP A 247
REMARK 465 PRO A 248
REMARK 465 GLN A 249
REMARK 465 SER A 250
REMARK 465 SER A 251
REMARK 465 ASN A 252
REMARK 465 PRO A 270
REMARK 465 ARG B 97
REMARK 465 ASP B 98
REMARK 465 MET B 99
REMARK 465 GLU C 190
REMARK 465 THR C 191
REMARK 465 PHE C 192
REMARK 465 PRO C 193
REMARK 465 GLY C 194
REMARK 465 VAL C 195
REMARK 465 GLU C 220
REMARK 465 ILE C 221
REMARK 465 VAL C 222
REMARK 465 GLN C 223
REMARK 465 ASP C 247
REMARK 465 PRO C 248
REMARK 465 GLN C 249
REMARK 465 SER C 250
REMARK 465 PRO C 270
REMARK 465 GLU D 201
REMARK 465 SER D 202
REMARK 465 SER D 203
REMARK 465 ASN E 1
REMARK 465 ASP E 245
REMARK 465 ARG F 97
REMARK 465 ASP F 98
REMARK 465 MET F 99
REMARK 465 ASP G 123
REMARK 465 SER G 124
REMARK 465 LYS G 125
REMARK 465 SER G 126
REMARK 465 SER G 127
REMARK 465 ASP G 128
REMARK 465 LYS G 129
REMARK 465 LYS G 177
REMARK 465 SER G 178
REMARK 465 ASP G 179
REMARK 465 SER G 199
REMARK 465 PRO G 200
REMARK 465 GLU G 201
REMARK 465 SER G 202
REMARK 465 SER G 203
REMARK 465 ASN H 1
REMARK 465 ALA H 2
REMARK 465 ARG H 243
REMARK 465 ALA H 244
REMARK 465 ASP H 245
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 HIS A 17 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 190 CG CD OE1 OE2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 LEU A 253 CG CD1 CD2
REMARK 470 GLU B 16 CG CD OE1 OE2
REMARK 470 GLU B 36 CG CD OE1 OE2
REMARK 470 GLU B 44 CG CD OE1 OE2
REMARK 470 GLU B 47 CG CD OE1 OE2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 GLU B 74 CG CD OE1 OE2
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 HIS C 17 CG ND1 CD2 CE1 NE2
REMARK 470 GLU C 52 CG CD OE1 OE2
REMARK 470 GLU C 102 CG CD OE1 OE2
REMARK 470 GLN C 147 CG CD OE1 NE2
REMARK 470 LYS C 189 CG CD CE NZ
REMARK 470 TYR C 211 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 216 CG CD CE NZ
REMARK 470 GLU C 219 CG CD OE1 OE2
REMARK 470 GLU C 224 CG CD OE1 OE2
REMARK 470 GLU C 245 CG CD OE1 OE2
REMARK 470 ASN C 252 CG OD1 ND2
REMARK 470 LEU C 253 CG CD1 CD2
REMARK 470 GLN C 268 CG CD OE1 NE2
REMARK 470 GLN D 2 CG CD OE1 NE2
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 GLU D 56 CG CD OE1 OE2
REMARK 470 LYS D 57 CG CD CE NZ
REMARK 470 LYS D 76 CG CD CE NZ
REMARK 470 LYS D 125 CG CD CE NZ
REMARK 470 LYS D 147 CG CD CE NZ
REMARK 470 ASP D 148 CG OD1 OD2
REMARK 470 ASN D 184 CG OD1 ND2
REMARK 470 ASP D 194 CG OD1 OD2
REMARK 470 LYS E 9 CG CD CE NZ
REMARK 470 LYS E 57 CG CD CE NZ
REMARK 470 GLU E 116 CG CD OE1 OE2
REMARK 470 GLU E 133 CG CD OE1 OE2
REMARK 470 LYS E 165 CG CD CE NZ
REMARK 470 ASN E 185 CG OD1 ND2
REMARK 470 GLU E 220 CG CD OE1 OE2
REMARK 470 GLU E 223 CG CD OE1 OE2
REMARK 470 ARG E 243 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 16 CG CD OE1 OE2
REMARK 470 LYS F 19 CG CD CE NZ
REMARK 470 GLU F 44 CG CD OE1 OE2
REMARK 470 ARG F 45 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 47 CG CD OE1 OE2
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 LYS F 75 CG CD CE NZ
REMARK 470 GLU F 77 CG CD OE1 OE2
REMARK 470 GLN F 89 CG CD OE1 NE2
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 ASP G 110 CG OD1 OD2
REMARK 470 GLN G 112 CG CD OE1 NE2
REMARK 470 ARG G 122 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 138 CG OD1 OD2
REMARK 470 GLN G 140 CG CD OE1 NE2
REMARK 470 GLN G 145 CG CD OE1 NE2
REMARK 470 LYS G 147 CG CD CE NZ
REMARK 470 ASP G 148 CG OD1 OD2
REMARK 470 ASP G 150 CG OD1 OD2
REMARK 470 ARG G 162 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 165 CG OD1 OD2
REMARK 470 ASN G 176 CG OD1 ND2
REMARK 470 ASN G 184 CG OD1 ND2
REMARK 470 ASN G 187 CG OD1 ND2
REMARK 470 ASN G 188 CG OD1 ND2
REMARK 470 GLU G 193 CG CD OE1 OE2
REMARK 470 ASP G 194 CG OD1 OD2
REMARK 470 LYS H 9 CG CD CE NZ
REMARK 470 LYS H 14 CG CD CE NZ
REMARK 470 LYS H 57 CG CD CE NZ
REMARK 470 ARG H 77 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 79 CG CD OE1 OE2
REMARK 470 ARG H 111 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 116 CG CD OE1 OE2
REMARK 470 LYS H 119 CG CD CE NZ
REMARK 470 GLU H 125 CG CD OE1 OE2
REMARK 470 GLU H 133 CG CD OE1 OE2
REMARK 470 GLN H 140 CG CD OE1 NE2
REMARK 470 LYS H 165 CG CD CE NZ
REMARK 470 GLN H 176 CG CD OE1 NE2
REMARK 470 ARG H 206 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 220 CG CD OE1 OE2
REMARK 470 ASN H 221 CG OD1 ND2
REMARK 470 GLU H 223 CG CD OE1 OE2
REMARK 470 GLN H 226 CG CD OE1 NE2
REMARK 470 ASP H 227 CG OD1 OD2
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 29 -125.75 62.58
REMARK 500 PHE A 119 -58.43 -123.47
REMARK 500 THR A 191 -117.15 -89.76
REMARK 500 PRO A 193 120.75 -29.99
REMARK 500 ASP C 29 -123.11 56.24
REMARK 500 PHE C 119 -56.78 -127.60
REMARK 500 ASN C 217 48.65 39.87
REMARK 500 VAL D 50 -31.41 -133.13
REMARK 500 LYS D 57 82.87 -160.90
REMARK 500 ASN E 70 -169.36 -165.01
REMARK 500 TRP F 60 -2.70 75.84
REMARK 500 VAL G 50 -32.83 -131.89
REMARK 500 LYS G 57 66.18 -117.07
REMARK 500 ASP G 150 32.52 -95.88
REMARK 500 ASP H 26 51.11 -115.44
REMARK 500 ASN H 28 35.53 71.62
REMARK 500 ASN H 70 -168.72 -164.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VY A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VY C 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4L4V RELATED DB: PDB
DBREF 4LCW A 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 4LCW B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4LCW C 1 270 UNP Q95460 HMR1_HUMAN 23 292
DBREF 4LCW F 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 4LCW D 1 203 PDB 4LCW 4LCW 1 203
DBREF 4LCW G 1 203 PDB 4LCW 4LCW 1 203
DBREF 4LCW E 1 245 PDB 4LCW 4LCW 1 245
DBREF 4LCW H 1 245 PDB 4LCW 4LCW 1 245
SEQADV 4LCW MET A 0 UNP Q95460 EXPRESSION TAG
SEQADV 4LCW ALA A 43 UNP Q95460 LYS 65 ENGINEERED MUTATION
SEQADV 4LCW SER A 261 UNP Q95460 CYS 283 ENGINEERED MUTATION
SEQADV 4LCW MET C 0 UNP Q95460 EXPRESSION TAG
SEQADV 4LCW ALA C 43 UNP Q95460 LYS 65 ENGINEERED MUTATION
SEQADV 4LCW SER C 261 UNP Q95460 CYS 283 ENGINEERED MUTATION
SEQRES 1 A 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL
SEQRES 2 A 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL
SEQRES 3 A 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER
SEQRES 4 A 271 VAL THR ARG GLN ALA GLU PRO ARG ALA PRO TRP MET ALA
SEQRES 5 A 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN
SEQRES 6 A 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU
SEQRES 7 A 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS
SEQRES 8 A 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP
SEQRES 9 A 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY
SEQRES 10 A 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP
SEQRES 11 A 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA
SEQRES 12 A 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN
SEQRES 13 A 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE
SEQRES 14 A 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO
SEQRES 15 A 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY
SEQRES 16 A 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO
SEQRES 17 A 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU
SEQRES 18 A 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER
SEQRES 19 A 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU
SEQRES 20 A 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU
SEQRES 21 A 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO
SEQRES 1 B 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 B 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 B 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 B 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 B 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 B 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 B 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 271 MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL
SEQRES 2 C 271 SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL
SEQRES 3 C 271 GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER
SEQRES 4 C 271 VAL THR ARG GLN ALA GLU PRO ARG ALA PRO TRP MET ALA
SEQRES 5 C 271 GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN
SEQRES 6 C 271 LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU
SEQRES 7 C 271 LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS
SEQRES 8 C 271 THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP
SEQRES 9 C 271 GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY
SEQRES 10 C 271 GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP
SEQRES 11 C 271 LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA
SEQRES 12 C 271 TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN
SEQRES 13 C 271 TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE
SEQRES 14 C 271 LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO
SEQRES 15 C 271 PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY
SEQRES 16 C 271 VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO
SEQRES 17 C 271 PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU
SEQRES 18 C 271 ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER
SEQRES 19 C 271 GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU
SEQRES 20 C 271 ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU
SEQRES 21 C 271 HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO
SEQRES 1 D 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 D 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 D 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 D 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 D 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 D 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 D 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS
SEQRES 8 D 203 ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS
SEQRES 9 D 203 LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 D 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 D 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 D 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 D 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 D 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 D 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 D 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 E 245 ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU
SEQRES 2 E 245 LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP
SEQRES 3 E 245 MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO
SEQRES 4 E 245 GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU
SEQRES 5 E 245 GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES 6 E 245 VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU
SEQRES 7 E 245 GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 E 245 ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU
SEQRES 9 E 245 PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP
SEQRES 10 E 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 E 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 E 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 E 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 E 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 E 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 E 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 E 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 E 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 E 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
SEQRES 1 F 99 ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR
SEQRES 3 F 99 VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU
SEQRES 4 F 99 LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER
SEQRES 5 F 99 ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU
SEQRES 6 F 99 TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR
SEQRES 7 F 99 ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS
SEQRES 8 F 99 ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 G 203 GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR
SEQRES 2 G 203 GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR
SEQRES 3 G 203 SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA
SEQRES 4 G 203 GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP
SEQRES 5 G 203 GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER
SEQRES 6 G 203 ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU
SEQRES 7 G 203 GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS
SEQRES 8 G 203 ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS
SEQRES 9 G 203 LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA
SEQRES 10 G 203 VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER
SEQRES 11 G 203 VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL
SEQRES 12 G 203 SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS
SEQRES 13 G 203 CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN
SEQRES 14 G 203 SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS
SEQRES 15 G 203 ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR
SEQRES 16 G 203 PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 H 245 ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU
SEQRES 2 H 245 LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP
SEQRES 3 H 245 MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO
SEQRES 4 H 245 GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU
SEQRES 5 H 245 GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN
SEQRES 6 H 245 VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU
SEQRES 7 H 245 GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS
SEQRES 8 H 245 ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU
SEQRES 9 H 245 PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP
SEQRES 10 H 245 LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU
SEQRES 11 H 245 PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR
SEQRES 12 H 245 LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL
SEQRES 13 H 245 GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER
SEQRES 14 H 245 GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO
SEQRES 15 H 245 ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU
SEQRES 16 H 245 ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS
SEQRES 17 H 245 PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN
SEQRES 18 H 245 ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN
SEQRES 19 H 245 ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP
HET GOL A 301 6
HET 1VY A 302 23
HET 1VY C 301 23
HETNAM GOL GLYCEROL
HETNAM 1VY 1-DEOXY-1-(7-HYDROXY-6-METHYL-2,4-DIOXO-3,4-
HETNAM 2 1VY DIHYDROPTERIDIN-8(2H)-YL)-D-RIBITOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GOL C3 H8 O3
FORMUL 10 1VY 2(C12 H16 N4 O7)
FORMUL 12 HOH *334(H2 O)
HELIX 1 1 ALA A 47 LEU A 54 1 8
HELIX 2 2 ALA A 55 ASN A 85 1 31
HELIX 3 3 ASP A 133 GLU A 144 1 12
HELIX 4 4 ASN A 146 GLU A 159 1 14
HELIX 5 5 GLU A 159 GLY A 172 1 14
HELIX 6 6 GLY A 172 GLN A 177 1 6
HELIX 7 7 ALA C 47 LEU C 54 1 8
HELIX 8 8 ALA C 55 ASN C 85 1 31
HELIX 9 9 ASP C 133 ALA C 145 1 13
HELIX 10 10 ASN C 146 GLU C 159 1 14
HELIX 11 11 GLU C 159 GLY C 172 1 14
HELIX 12 12 GLY C 172 GLN C 177 1 6
HELIX 13 13 GLN D 79 SER D 83 5 5
HELIX 14 14 ALA D 181 PHE D 186 1 6
HELIX 15 15 ALA E 82 THR E 86 5 5
HELIX 16 16 ASP E 117 VAL E 121 5 5
HELIX 17 17 SER E 132 GLN E 140 1 9
HELIX 18 18 ALA E 199 GLN E 203 1 5
HELIX 19 19 GLN G 79 SER G 83 5 5
HELIX 20 20 ARG G 162 ASP G 165 5 4
HELIX 21 21 ALA H 82 THR H 86 5 5
HELIX 22 22 SER H 132 GLN H 140 1 9
HELIX 23 23 ALA H 199 ASN H 204 1 6
SHEET 1 A 8 GLU A 44 PRO A 45 0
SHEET 2 A 8 HIS A 31 ASP A 37 -1 N THR A 35 O GLU A 44
SHEET 3 A 8 PHE A 22 VAL A 28 -1 N GLY A 26 O ILE A 33
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N LEU A 10 O ILE A 23
SHEET 5 A 8 THR A 91 LEU A 100 -1 O ILE A 96 N TYR A 7
SHEET 6 A 8 THR A 106 TYR A 114 -1 O ALA A 113 N GLN A 93
SHEET 7 A 8 GLN A 117 ASN A 123 -1 O LEU A 120 N TYR A 112
SHEET 8 A 8 SER A 128 ALA A 131 -1 O SER A 128 N ASN A 123
SHEET 1 B 4 LEU A 183 GLU A 190 0
SHEET 2 B 4 THR A 196 PHE A 205 -1 O ALA A 197 N LYS A 189
SHEET 3 B 4 TYR A 238 GLU A 245 -1 O ALA A 240 N ALA A 202
SHEET 4 B 4 ASP A 226 TYR A 227 -1 N ASP A 226 O SER A 243
SHEET 1 C 4 LEU A 183 GLU A 190 0
SHEET 2 C 4 THR A 196 PHE A 205 -1 O ALA A 197 N LYS A 189
SHEET 3 C 4 TYR A 238 GLU A 245 -1 O ALA A 240 N ALA A 202
SHEET 4 C 4 LEU A 231 PRO A 232 -1 N LEU A 231 O GLN A 239
SHEET 1 D 4 GLU A 219 GLU A 220 0
SHEET 2 D 4 ILE A 210 LYS A 216 -1 N LYS A 216 O GLU A 219
SHEET 3 D 4 TYR A 254 HIS A 260 -1 O HIS A 257 N THR A 213
SHEET 4 D 4 VAL A 263 GLN A 268 -1 O MET A 265 N VAL A 258
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O PHE B 70 N ASN B 21
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 ILE B 35 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 HIS B 84 -1 O ARG B 81 N ASP B 38
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O VAL B 93 N CYS B 80
SHEET 1 H 8 GLU C 44 PRO C 45 0
SHEET 2 H 8 HIS C 31 ASP C 37 -1 N THR C 35 O GLU C 44
SHEET 3 H 8 PHE C 22 VAL C 28 -1 N SER C 24 O TYR C 36
SHEET 4 H 8 HIS C 3 VAL C 12 -1 N LEU C 10 O ILE C 23
SHEET 5 H 8 THR C 91 LEU C 100 -1 O TYR C 92 N GLY C 11
SHEET 6 H 8 THR C 106 TYR C 114 -1 O GLN C 111 N MET C 95
SHEET 7 H 8 GLN C 117 ASN C 123 -1 O LEU C 120 N TYR C 112
SHEET 8 H 8 SER C 128 ALA C 131 -1 O LEU C 130 N ILE C 121
SHEET 1 I 4 LEU C 183 ARG C 188 0
SHEET 2 I 4 ALA C 197 PHE C 205 -1 O HIS C 203 N LEU C 183
SHEET 3 I 4 TYR C 238 GLU C 245 -1 O ALA C 242 N CYS C 200
SHEET 4 I 4 ASP C 226 TYR C 227 -1 N ASP C 226 O SER C 243
SHEET 1 J 4 LEU C 183 ARG C 188 0
SHEET 2 J 4 ALA C 197 PHE C 205 -1 O HIS C 203 N LEU C 183
SHEET 3 J 4 TYR C 238 GLU C 245 -1 O ALA C 242 N CYS C 200
SHEET 4 J 4 LEU C 231 PRO C 232 -1 N LEU C 231 O GLN C 239
SHEET 1 K 3 TYR C 211 LYS C 216 0
SHEET 2 K 3 TYR C 254 HIS C 260 -1 O HIS C 257 N THR C 213
SHEET 3 K 3 VAL C 263 GLN C 268 -1 O MET C 265 N VAL C 258
SHEET 1 L 5 ASN D 3 ASP D 5 0
SHEET 2 L 5 VAL D 18 GLN D 25 -1 O GLN D 25 N ASN D 3
SHEET 3 L 5 TYR D 70 LEU D 75 -1 O LEU D 73 N ILE D 20
SHEET 4 L 5 PHE D 60 SER D 65 -1 N SER D 65 O TYR D 70
SHEET 5 L 5 GLY D 53 LYS D 57 -1 N GLU D 55 O SER D 62
SHEET 1 M 5 GLU D 9 THR D 13 0
SHEET 2 M 5 THR D 103 LYS D 108 1 O LYS D 108 N ALA D 12
SHEET 3 M 5 ALA D 84 LYS D 91 -1 N ALA D 84 O LEU D 105
SHEET 4 M 5 LEU D 32 GLN D 37 -1 N PHE D 33 O ALA D 89
SHEET 5 M 5 THR D 44 ASN D 49 -1 O LEU D 46 N TRP D 34
SHEET 1 N 4 GLU D 9 THR D 13 0
SHEET 2 N 4 THR D 103 LYS D 108 1 O LYS D 108 N ALA D 12
SHEET 3 N 4 ALA D 84 LYS D 91 -1 N ALA D 84 O LEU D 105
SHEET 4 N 4 LEU D 97 TRP D 99 -1 O ILE D 98 N VAL D 90
SHEET 1 O 4 ALA D 117 GLN D 120 0
SHEET 2 O 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 O 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 O 4 TYR D 152 ILE D 153 -1 N TYR D 152 O TRP D 174
SHEET 1 P 4 ALA D 117 GLN D 120 0
SHEET 2 P 4 SER D 130 THR D 135 -1 O LEU D 133 N TYR D 119
SHEET 3 P 4 PHE D 166 SER D 175 -1 O ALA D 173 N CYS D 132
SHEET 4 P 4 CYS D 157 MET D 161 -1 N MET D 161 O PHE D 166
SHEET 1 Q 4 VAL E 4 THR E 7 0
SHEET 2 Q 4 MET E 19 GLN E 25 -1 O ALA E 24 N THR E 5
SHEET 3 Q 4 SER E 75 LEU E 78 -1 O LEU E 76 N LEU E 21
SHEET 4 Q 4 TYR E 64 SER E 67 -1 N ASN E 65 O ARG E 77
SHEET 1 R 6 PHE E 10 LYS E 14 0
SHEET 2 R 6 SER E 110 LEU E 115 1 O LEU E 115 N LEU E 13
SHEET 3 R 6 SER E 87 SER E 94 -1 N SER E 87 O LEU E 112
SHEET 4 R 6 SER E 31 GLN E 37 -1 N TYR E 35 O PHE E 90
SHEET 5 R 6 ARG E 44 SER E 49 -1 O ILE E 46 N TRP E 34
SHEET 6 R 6 ASP E 56 LYS E 57 -1 O ASP E 56 N TYR E 48
SHEET 1 S 4 PHE E 10 LYS E 14 0
SHEET 2 S 4 SER E 110 LEU E 115 1 O LEU E 115 N LEU E 13
SHEET 3 S 4 SER E 87 SER E 94 -1 N SER E 87 O LEU E 112
SHEET 4 S 4 PHE E 105 PHE E 106 -1 O PHE E 105 N SER E 93
SHEET 1 T 4 GLU E 125 PHE E 129 0
SHEET 2 T 4 LYS E 141 PHE E 151 -1 O THR E 149 N GLU E 125
SHEET 3 T 4 TYR E 189 SER E 198 -1 O TYR E 189 N PHE E 151
SHEET 4 T 4 VAL E 171 THR E 173 -1 N CYS E 172 O ARG E 194
SHEET 1 U 4 GLU E 125 PHE E 129 0
SHEET 2 U 4 LYS E 141 PHE E 151 -1 O THR E 149 N GLU E 125
SHEET 3 U 4 TYR E 189 SER E 198 -1 O TYR E 189 N PHE E 151
SHEET 4 U 4 LEU E 178 LYS E 179 -1 N LEU E 178 O ALA E 190
SHEET 1 V 4 LYS E 165 VAL E 167 0
SHEET 2 V 4 VAL E 156 VAL E 162 -1 N VAL E 162 O LYS E 165
SHEET 3 V 4 HIS E 208 PHE E 215 -1 O GLN E 214 N GLU E 157
SHEET 4 V 4 GLN E 234 TRP E 241 -1 O ALA E 240 N PHE E 209
SHEET 1 W 4 LYS F 6 SER F 11 0
SHEET 2 W 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 W 4 PHE F 62 PHE F 70 -1 O TYR F 66 N CYS F 25
SHEET 4 W 4 GLU F 50 HIS F 51 -1 N GLU F 50 O TYR F 67
SHEET 1 X 4 LYS F 6 SER F 11 0
SHEET 2 X 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 X 4 PHE F 62 PHE F 70 -1 O TYR F 66 N CYS F 25
SHEET 4 X 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 Y 4 GLU F 44 ARG F 45 0
SHEET 2 Y 4 GLU F 36 LYS F 41 -1 N LYS F 41 O GLU F 44
SHEET 3 Y 4 TYR F 78 ASN F 83 -1 O ALA F 79 N LEU F 40
SHEET 4 Y 4 LYS F 91 LYS F 94 -1 O LYS F 91 N VAL F 82
SHEET 1 Z 5 ASN G 3 ASP G 5 0
SHEET 2 Z 5 VAL G 18 GLN G 25 -1 O GLN G 25 N ASN G 3
SHEET 3 Z 5 TYR G 70 LEU G 75 -1 O LEU G 73 N ILE G 20
SHEET 4 Z 5 PHE G 60 SER G 65 -1 N SER G 61 O LEU G 74
SHEET 5 Z 5 GLY G 53 LYS G 57 -1 N GLU G 55 O SER G 62
SHEET 1 AA 5 GLU G 9 THR G 13 0
SHEET 2 AA 5 THR G 103 LYS G 108 1 O ILE G 106 N MET G 10
SHEET 3 AA 5 ALA G 84 LYS G 91 -1 N ALA G 84 O LEU G 105
SHEET 4 AA 5 LEU G 32 GLN G 37 -1 N PHE G 33 O ALA G 89
SHEET 5 AA 5 THR G 44 ASN G 49 -1 O ASN G 49 N LEU G 32
SHEET 1 AB 4 GLU G 9 THR G 13 0
SHEET 2 AB 4 THR G 103 LYS G 108 1 O ILE G 106 N MET G 10
SHEET 3 AB 4 ALA G 84 LYS G 91 -1 N ALA G 84 O LEU G 105
SHEET 4 AB 4 LEU G 97 TRP G 99 -1 O ILE G 98 N VAL G 90
SHEET 1 AC 4 ALA G 117 LEU G 121 0
SHEET 2 AC 4 VAL G 131 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AC 4 PHE G 166 SER G 175 -1 O ALA G 171 N PHE G 134
SHEET 4 AC 4 VAL G 151 ILE G 153 -1 N TYR G 152 O TRP G 174
SHEET 1 AD 4 ALA G 117 LEU G 121 0
SHEET 2 AD 4 VAL G 131 THR G 135 -1 O LEU G 133 N TYR G 119
SHEET 3 AD 4 PHE G 166 SER G 175 -1 O ALA G 171 N PHE G 134
SHEET 4 AD 4 CYS G 157 MET G 161 -1 N MET G 161 O PHE G 166
SHEET 1 AE 4 VAL H 4 THR H 7 0
SHEET 2 AE 4 MET H 19 GLN H 25 -1 O ALA H 24 N THR H 5
SHEET 3 AE 4 PHE H 74 LEU H 78 -1 O LEU H 76 N LEU H 21
SHEET 4 AE 4 TYR H 64 ARG H 68 -1 N ASN H 65 O ARG H 77
SHEET 1 AF 6 PHE H 10 LYS H 14 0
SHEET 2 AF 6 SER H 110 LEU H 115 1 O THR H 113 N LEU H 13
SHEET 3 AF 6 SER H 87 SER H 94 -1 N SER H 87 O LEU H 112
SHEET 4 AF 6 SER H 31 GLN H 37 -1 N TYR H 35 O PHE H 90
SHEET 5 AF 6 ARG H 44 SER H 49 -1 O SER H 49 N MET H 32
SHEET 6 AF 6 ASP H 56 LYS H 57 -1 O ASP H 56 N TYR H 48
SHEET 1 AG 4 PHE H 10 LYS H 14 0
SHEET 2 AG 4 SER H 110 LEU H 115 1 O THR H 113 N LEU H 13
SHEET 3 AG 4 SER H 87 SER H 94 -1 N SER H 87 O LEU H 112
SHEET 4 AG 4 PHE H 105 PHE H 106 -1 O PHE H 105 N SER H 93
SHEET 1 AH 4 GLU H 125 PHE H 129 0
SHEET 2 AH 4 LYS H 141 PHE H 151 -1 O LEU H 147 N ALA H 127
SHEET 3 AH 4 TYR H 189 SER H 198 -1 O LEU H 191 N ALA H 148
SHEET 4 AH 4 VAL H 171 THR H 173 -1 N CYS H 172 O ARG H 194
SHEET 1 AI 4 GLU H 125 PHE H 129 0
SHEET 2 AI 4 LYS H 141 PHE H 151 -1 O LEU H 147 N ALA H 127
SHEET 3 AI 4 TYR H 189 SER H 198 -1 O LEU H 191 N ALA H 148
SHEET 4 AI 4 LEU H 178 LYS H 179 -1 N LEU H 178 O ALA H 190
SHEET 1 AJ 4 LYS H 165 VAL H 167 0
SHEET 2 AJ 4 VAL H 156 VAL H 162 -1 N VAL H 162 O LYS H 165
SHEET 3 AJ 4 HIS H 208 PHE H 215 -1 O GLN H 212 N SER H 159
SHEET 4 AJ 4 GLN H 234 TRP H 241 -1 O ALA H 238 N CYS H 211
SSBOND 1 CYS A 98 CYS A 161 1555 1555 2.06
SSBOND 2 CYS A 200 CYS A 256 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.03
SSBOND 4 CYS C 98 CYS C 161 1555 1555 2.07
SSBOND 5 CYS C 200 CYS C 256 1555 1555 2.02
SSBOND 6 CYS D 22 CYS D 88 1555 1555 2.04
SSBOND 7 CYS D 132 CYS D 182 1555 1555 2.05
SSBOND 8 CYS D 157 CYS E 172 1555 1555 2.06
SSBOND 9 CYS E 23 CYS E 91 1555 1555 2.03
SSBOND 10 CYS E 146 CYS E 211 1555 1555 2.03
SSBOND 11 CYS F 25 CYS F 80 1555 1555 2.04
SSBOND 12 CYS G 22 CYS G 88 1555 1555 2.03
SSBOND 13 CYS G 132 CYS G 182 1555 1555 2.06
SSBOND 14 CYS G 157 CYS H 172 1555 1555 2.05
SSBOND 15 CYS H 23 CYS H 91 1555 1555 2.04
SSBOND 16 CYS H 146 CYS H 211 1555 1555 2.03
CISPEP 1 TYR A 206 PRO A 207 0 5.66
CISPEP 2 HIS B 31 PRO B 32 0 5.17
CISPEP 3 TYR C 206 PRO C 207 0 3.64
CISPEP 4 THR E 7 PRO E 8 0 -7.04
CISPEP 5 TYR E 152 PRO E 153 0 -1.76
CISPEP 6 HIS F 31 PRO F 32 0 4.68
CISPEP 7 THR H 7 PRO H 8 0 -3.58
CISPEP 8 TYR H 152 PRO H 153 0 -0.07
SITE 1 AC1 4 GLU A 180 PRO A 181 GLY A 204 GLN D 19
SITE 1 AC2 14 TYR A 7 ARG A 9 SER A 24 THR A 34
SITE 2 AC2 14 TYR A 62 TRP A 69 ARG A 94 ILE A 96
SITE 3 AC2 14 TYR A 152 TRP A 156 HOH A 402 HOH A 407
SITE 4 AC2 14 HOH A 408 TYR G 95
SITE 1 AC3 16 TYR C 7 ARG C 9 SER C 24 TYR C 62
SITE 2 AC3 16 LEU C 66 TRP C 69 ARG C 94 ILE C 96
SITE 3 AC3 16 TYR C 152 GLN C 153 TRP C 156 HOH C 401
SITE 4 AC3 16 HOH C 407 HOH C 408 TYR D 95 HOH D 401
CRYST1 215.915 69.361 142.829 90.00 104.30 90.00 C 1 2 1 8
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 0.004631 0.000000 0.001181 0.00000
SCALE2 0.000000 0.014417 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007225 0.00000
(ATOM LINES ARE NOT SHOWN.)
END