HEADER IMMUNE SYSTEM 10-FEB-15 4Y4H
TITLE CRYSTAL STRUCTURE OF THE MCD1D/GCK152/INKTCR TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIGEN-PRESENTING GLYCOPROTEIN CD1D1;
COMPND 3 CHAIN: A, E;
COMPND 4 FRAGMENT: ECTODOMAIN, UNP RESIDUES 19-297;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 8 CHAIN: B, F;
COMPND 9 FRAGMENT: UNP RESIDUES 21-119;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: CHIMERIC TCR VALPHA14/JALPHA18 CHAIN (MOUSE VARIABLE
COMPND 13 DOMAIN/ HUMAN CONSTANT DOMAIN);
COMPND 14 CHAIN: C, G;
COMPND 15 SYNONYM: PROTEIN TRAV11D,HUMAN NKT TCR BETA CHAIN;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: CHIMERIC TCR VBETA8.2 CHAIN (MOUSE VARIABLE DOMAIN/ HUMAN
COMPND 19 CONSTANT DOMAIN);
COMPND 20 CHAIN: D, H;
COMPND 21 SYNONYM: BETA-CHAIN,T-CELL RECEPTOR BETA-2 CHAIN C REGION;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CD1D1, CD1.1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBACPHP10;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: B2M;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PBACP10PH;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 24 ORGANISM_TAXID: 10090, 9606;
SOURCE 25 GENE: TRAV11, TRAV11D, HDCMA22P;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET22B+;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 34 ORGANISM_TAXID: 10090,9606;
SOURCE 35 GENE: TRBC2, TCRBC2;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PET22B+
KEYWDS MHC-FOLD, IG-FOLD, GLYCOLIPID ANTIGEN PRESENTATION, T CELL RECEPTOR,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.ZAJONC,E.D.YU
REVDAT 4 29-JUL-20 4Y4H 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 11-DEC-19 4Y4H 1 REMARK
REVDAT 2 13-SEP-17 4Y4H 1 SOURCE REMARK
REVDAT 1 27-MAY-15 4Y4H 0
JRNL AUTH A.BIRKHOLZ,M.NEMCOVIC,E.D.YU,E.GIRARDI,J.WANG,A.KHURANA,
JRNL AUTH 2 N.PAUWELS,R.W.FRANCK,M.TSUJI,A.HOWELL,S.CALENBERGH,
JRNL AUTH 3 M.KRONENBERG,D.M.ZAJONC
JRNL TITL STRUCTURAL MODIFICATIONS OF ALPHAGALCER IN BOTH LIPID AND
JRNL TITL 2 CARBOHYDRATE MOIETY INFLUENCE ACTIVATION OF MURINE AND HUMAN
JRNL TITL 3 INKT CELLS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0104
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 41334
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) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1334
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 222
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
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): 0.496
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.361
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.310
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12824 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17546 ; 1.249 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1596 ; 5.673 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 573 ;35.664 ;24.311
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1765 ;15.498 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;13.074 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1952 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9965 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 279 1
REMARK 3 1 E 1 E 279 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1992 ; 0.040 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 1992 ;11.150 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 99 1
REMARK 3 1 F 1 F 99 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 719 ; 0.030 ; 0.050
REMARK 3 TIGHT THERMAL 2 B (A**2): 719 ;10.410 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 205 1
REMARK 3 1 G 1 G 205 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 1514 ; 0.040 ; 0.050
REMARK 3 TIGHT THERMAL 3 C (A**2): 1514 ; 4.240 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 1 D 240 1
REMARK 3 1 H 1 H 240 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 D (A): 1828 ; 0.040 ; 0.050
REMARK 3 TIGHT THERMAL 4 D (A**2): 1828 ; 4.360 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4Y4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000206848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-11
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 : SSRL
REMARK 200 BEAMLINE : BL7-1
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 : SINGLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42694
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.59900
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000, 0.2M DI-AMMONIUM
REMARK 280 HYDROGEN CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 75.18950
REMARK 290 SMTRY3 2 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, C, D, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H, K
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 SER A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 3
REMARK 465 GLN A 4
REMARK 465 GLN A 5
REMARK 465 LYS A 6
REMARK 465 SER A 198
REMARK 465 SER A 199
REMARK 465 ALA A 200
REMARK 465 HIS A 201
REMARK 465 GLY A 202
REMARK 465 HIS A 203
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 HIS A 285
REMARK 465 ILE B 1
REMARK 465 ASP B 98
REMARK 465 MET B 99
REMARK 465 MET C 0
REMARK 465 LYS C 1
REMARK 465 SER C 183
REMARK 465 PRO C 205
REMARK 465 GLU C 206
REMARK 465 SER C 207
REMARK 465 SER C 208
REMARK 465 MET D 0
REMARK 465 GLU D 1
REMARK 465 SER E 1
REMARK 465 GLU E 2
REMARK 465 ALA E 3
REMARK 465 GLN E 4
REMARK 465 GLN E 5
REMARK 465 LYS E 6
REMARK 465 SER E 198
REMARK 465 SER E 199
REMARK 465 ALA E 200
REMARK 465 HIS E 201
REMARK 465 GLY E 202
REMARK 465 HIS E 203
REMARK 465 HIS E 280
REMARK 465 HIS E 281
REMARK 465 HIS E 282
REMARK 465 HIS E 283
REMARK 465 HIS E 284
REMARK 465 HIS E 285
REMARK 465 ILE F 1
REMARK 465 ASP F 98
REMARK 465 MET F 99
REMARK 465 MET G 0
REMARK 465 LYS G 1
REMARK 465 SER G 183
REMARK 465 PRO G 205
REMARK 465 GLU G 206
REMARK 465 SER G 207
REMARK 465 SER G 208
REMARK 465 MET H 0
REMARK 465 GLU H 1
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 21 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 35 CG CD1 CD2
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 ASN A 110 CB CG OD1 ND2
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 175 CG CD1 CD2
REMARK 470 LYS A 180 CG CD CE NZ
REMARK 470 LYS A 185 CG CD CE NZ
REMARK 470 LYS A 188 CG CD CE NZ
REMARK 470 SER A 195 OG
REMARK 470 GLN A 205 CG CD OE1 NE2
REMARK 470 LEU A 206 CG CD1 CD2
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 TRP A 222 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 222 CZ3 CH2
REMARK 470 ARG A 224 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 227 CG CD OE1 NE2
REMARK 470 ARG A 234 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 251 CG CD1 CD2
REMARK 470 GLU A 254 CG CD OE1 OE2
REMARK 470 ALA A 259 CB
REMARK 470 ARG A 264 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 266 CG CD CE NZ
REMARK 470 GLN A 273 CG CD OE1 NE2
REMARK 470 ILE A 275 CG1 CG2 CD1
REMARK 470 ILE A 276 CG1 CG2 CD1
REMARK 470 LEU A 277 CG CD1 CD2
REMARK 470 LYS B 3 CB CG CD CE NZ
REMARK 470 GLN B 6 CG CD OE1 NE2
REMARK 470 VAL B 9 CG1 CG2
REMARK 470 GLU B 16 CG CD OE1 OE2
REMARK 470 LYS B 19 CG CD CE NZ
REMARK 470 ILE B 22 CG1 CG2 CD1
REMARK 470 LEU B 23 CG CD1 CD2
REMARK 470 GLN B 29 CG CD OE1 NE2
REMARK 470 ILE B 35 CG1 CG2 CD1
REMARK 470 GLU B 36 CG CD OE1 OE2
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 LYS B 45 CG CD CE NZ
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 ARG B 81 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 LYS C 42 CG CD CE NZ
REMARK 470 LYS C 130 CG CD CE NZ
REMARK 470 LYS C 134 CG CD CE NZ
REMARK 470 GLN C 145 CG CD OE1 NE2
REMARK 470 GLN C 150 CG CD OE1 NE2
REMARK 470 LYS C 152 CG CD CE NZ
REMARK 470 LYS C 161 CG CD CE NZ
REMARK 470 LYS C 182 CG CD CE NZ
REMARK 470 ILE C 195 CG1 CG2 CD1
REMARK 470 GLU C 198 CG CD OE1 OE2
REMARK 470 LYS D 11 CG CD CE NZ
REMARK 470 LYS D 65 CG CD CE NZ
REMARK 470 GLU D 72 CG CD OE1 OE2
REMARK 470 LYS D 121 CG CD CE NZ
REMARK 470 LYS D 129 CG CD CE NZ
REMARK 470 LYS D 161 CG CD CE NZ
REMARK 470 LYS D 175 CG CD CE NZ
REMARK 470 ASN D 181 CG OD1 ND2
REMARK 470 GLU D 216 CG CD OE1 OE2
REMARK 470 GLU D 219 CG CD OE1 OE2
REMARK 470 ASP D 223 CG OD1 OD2
REMARK 470 ARG E 21 CG CD NE CZ NH1 NH2
REMARK 470 LEU E 32 CG CD1 CD2
REMARK 470 LEU E 35 CG CD1 CD2
REMARK 470 ARG E 39 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 51 CG CD CE NZ
REMARK 470 GLU E 64 CG CD OE1 OE2
REMARK 470 LYS E 65 CG CD CE NZ
REMARK 470 LYS E 91 CG CD CE NZ
REMARK 470 ASN E 110 CB CG OD1 ND2
REMARK 470 LYS E 123 CG CD CE NZ
REMARK 470 ARG E 173 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 180 CG CD CE NZ
REMARK 470 LYS E 185 CG CD CE NZ
REMARK 470 LYS E 188 CG CD CE NZ
REMARK 470 LEU E 193 CG CD1 CD2
REMARK 470 VAL E 196 CG1 CG2
REMARK 470 GLN E 205 CG CD OE1 NE2
REMARK 470 LYS E 216 CG CD CE NZ
REMARK 470 GLN E 227 CG CD OE1 NE2
REMARK 470 ARG E 234 CG CD NE CZ NH1 NH2
REMARK 470 VAL E 253 CG1 CG2
REMARK 470 GLU E 254 CG CD OE1 OE2
REMARK 470 GLU E 257 CG CD OE1 OE2
REMARK 470 ALA E 259 CB
REMARK 470 ARG E 264 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 273 CG CD OE1 NE2
REMARK 470 ILE E 275 CG1 CG2 CD1
REMARK 470 LEU E 277 CG CD1 CD2
REMARK 470 TRP E 279 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP E 279 CZ3 CH2
REMARK 470 LYS F 3 CB CG CD CE NZ
REMARK 470 GLU F 16 CG CD OE1 OE2
REMARK 470 LYS F 19 CG CD CE NZ
REMARK 470 GLN F 29 CG CD OE1 NE2
REMARK 470 GLU F 36 CG CD OE1 OE2
REMARK 470 LYS F 44 CG CD CE NZ
REMARK 470 LYS F 45 CG CD CE NZ
REMARK 470 LYS F 48 CG CD CE NZ
REMARK 470 LYS F 58 CG CD CE NZ
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 LYS F 83 CG CD CE NZ
REMARK 470 LYS F 91 CG CD CE NZ
REMARK 470 LYS G 42 CG CD CE NZ
REMARK 470 LYS G 56 CG CD CE NZ
REMARK 470 LYS G 130 CG CD CE NZ
REMARK 470 LYS G 134 CG CD CE NZ
REMARK 470 GLN G 145 CG CD OE1 NE2
REMARK 470 GLN G 150 CG CD OE1 NE2
REMARK 470 LYS G 152 CG CD CE NZ
REMARK 470 LYS G 161 CG CD CE NZ
REMARK 470 LYS G 182 CG CD CE NZ
REMARK 470 ASP G 184 CG OD1 OD2
REMARK 470 ASN G 189 CG OD1 ND2
REMARK 470 ILE G 195 CG1 CG2 CD1
REMARK 470 GLU G 198 CG CD OE1 OE2
REMARK 470 LYS H 57 CG CD CE NZ
REMARK 470 LYS H 65 CG CD CE NZ
REMARK 470 GLU H 72 CG CD OE1 OE2
REMARK 470 ARG H 115 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 121 CG CD CE NZ
REMARK 470 LYS H 129 CG CD CE NZ
REMARK 470 LYS H 161 CG CD CE NZ
REMARK 470 GLN H 172 CG CD OE1 NE2
REMARK 470 LEU H 180 CG CD1 CD2
REMARK 470 ASN H 181 CG OD1 ND2
REMARK 470 GLU H 216 CG CD OE1 OE2
REMARK 470 GLU H 219 CG CD OE1 OE2
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 HIS G 76 CG HIS G 76 CD2 0.054
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 VAL A 125 -33.83 -131.78
REMARK 500 ASP A 166 -66.38 -105.06
REMARK 500 PRO A 215 -177.16 -65.65
REMARK 500 PRO B 33 5.29 -65.90
REMARK 500 TRP B 60 1.94 81.65
REMARK 500 VAL C 27 127.09 -33.92
REMARK 500 LYS C 42 -166.33 -64.33
REMARK 500 VAL C 51 -32.52 -131.01
REMARK 500 ASN C 118 79.51 -117.20
REMARK 500 ASP C 120 52.71 -163.65
REMARK 500 SER C 132 -12.63 -49.23
REMARK 500 GLN C 145 0.77 -64.60
REMARK 500 GLN C 150 -177.01 -57.36
REMARK 500 PHE C 191 47.11 -105.80
REMARK 500 ASN C 193 4.68 -65.90
REMARK 500 ASP D 95 -140.72 -96.60
REMARK 500 GLN D 222 165.88 -49.87
REMARK 500 VAL E 125 -34.78 -133.47
REMARK 500 ASP E 166 -63.83 -103.73
REMARK 500 PRO E 215 -179.27 -65.91
REMARK 500 GLU E 257 23.31 -79.85
REMARK 500 PRO F 33 6.45 -69.07
REMARK 500 TRP F 60 0.83 80.80
REMARK 500 VAL G 27 131.04 -39.48
REMARK 500 LYS G 42 -166.25 -69.82
REMARK 500 ALA G 79 73.95 49.13
REMARK 500 THR G 85 102.85 -59.23
REMARK 500 ASN G 118 78.06 -117.38
REMARK 500 ASP G 120 55.81 -165.29
REMARK 500 SER G 132 -12.61 -48.36
REMARK 500 GLN G 150 -175.51 -56.45
REMARK 500 PHE G 191 46.27 -105.40
REMARK 500 ASN G 193 5.20 -67.08
REMARK 500 ARG H 68 77.84 -113.94
REMARK 500 ASP H 95 -141.43 -95.44
REMARK 500 PRO H 149 -162.84 -78.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Y4F RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXES BUT CONTAINING DIFFERENT GLYCOLIPID ANTIGENS
REMARK 900 RELATED ID: 4Y16 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXES BUT CONTAINING DIFFERENT GLYCOLIPID ANTIGENS
REMARK 900 RELATED ID: 4Y2D RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXES BUT CONTAINING DIFFERENT GLYCOLIPID ANTIGENS
REMARK 900 RELATED ID: 4Y4K RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXES BUT CONTAINING DIFFERENT GLYCOLIPID ANTIGENS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 TCR ALPHA CHAIN (CHAIN C):
REMARK 999 MKTQVEQSPQSLVVRQGENCVLQCNYSVTPDNHLRWFKQDTGKGLVSLTVLVDQKDKTSNGRYSATLD
REMARK 999 KDAKHSTLHITATLLDDTATYICVVGDRGSALGRLHFGAGTQLIVI (MURINE VARIABLE
REMARK 999 DOMAIN)
REMARK 999 PDIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSN
REMARK 999 KSDFACANAFNNSIIPEDTFFPSPESS (HUMAN CONSTANT DOMAIN) TCR BETA CHAIN
REMARK 999 (CHAIN D):
REMARK 999 MEAAVTQSPRNKVAVTGGKVTLSCNQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKAS
REMARK 999 RPSQENFSLILELATPSQTSVYFCASGDEGYTQYFGPGTRLLVLEDLRNVTPPKVSLFEPSK (MURI
REMARK 999 NE VARIABLE DOMAIN)
REMARK 999 AEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPALNDSRYSLSSRLRVSATF
REMARK 999 WQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA (HUMAN CONSTANT DOMAIN)
DBREF 4Y4H A 1 279 UNP P11609 CD1D1_MOUSE 19 297
DBREF 4Y4H B 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4Y4H C 0 208 PDB 4Y4H 4Y4H 0 208
DBREF 4Y4H D 0 240 PDB 4Y4H 4Y4H 0 240
DBREF 4Y4H E 1 279 UNP P11609 CD1D1_MOUSE 19 297
DBREF 4Y4H F 1 99 UNP P01887 B2MG_MOUSE 21 119
DBREF 4Y4H G 0 208 PDB 4Y4H 4Y4H 0 208
DBREF 4Y4H H 0 240 PDB 4Y4H 4Y4H 0 240
SEQADV 4Y4H HIS A 201 UNP P11609 ASP 219 VARIANT
SEQADV 4Y4H HIS A 280 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS A 281 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS A 282 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS A 283 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS A 284 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS A 285 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS E 201 UNP P11609 ASP 219 VARIANT
SEQADV 4Y4H HIS E 280 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS E 281 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS E 282 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS E 283 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS E 284 UNP P11609 EXPRESSION TAG
SEQADV 4Y4H HIS E 285 UNP P11609 EXPRESSION TAG
SEQRES 1 A 285 SER GLU ALA GLN GLN LYS ASN TYR THR PHE ARG CYS LEU
SEQRES 2 A 285 GLN MET SER SER PHE ALA ASN ARG SER TRP SER ARG THR
SEQRES 3 A 285 ASP SER VAL VAL TRP LEU GLY ASP LEU GLN THR HIS ARG
SEQRES 4 A 285 TRP SER ASN ASP SER ALA THR ILE SER PHE THR LYS PRO
SEQRES 5 A 285 TRP SER GLN GLY LYS LEU SER ASN GLN GLN TRP GLU LYS
SEQRES 6 A 285 LEU GLN HIS MET PHE GLN VAL TYR ARG VAL SER PHE THR
SEQRES 7 A 285 ARG ASP ILE GLN GLU LEU VAL LYS MET MET SER PRO LYS
SEQRES 8 A 285 GLU ASP TYR PRO ILE GLU ILE GLN LEU SER ALA GLY CYS
SEQRES 9 A 285 GLU MET TYR PRO GLY ASN ALA SER GLU SER PHE LEU HIS
SEQRES 10 A 285 VAL ALA PHE GLN GLY LYS TYR VAL VAL ARG PHE TRP GLY
SEQRES 11 A 285 THR SER TRP GLN THR VAL PRO GLY ALA PRO SER TRP LEU
SEQRES 12 A 285 ASP LEU PRO ILE LYS VAL LEU ASN ALA ASP GLN GLY THR
SEQRES 13 A 285 SER ALA THR VAL GLN MET LEU LEU ASN ASP THR CYS PRO
SEQRES 14 A 285 LEU PHE VAL ARG GLY LEU LEU GLU ALA GLY LYS SER ASP
SEQRES 15 A 285 LEU GLU LYS GLN GLU LYS PRO VAL ALA TRP LEU SER SER
SEQRES 16 A 285 VAL PRO SER SER ALA HIS GLY HIS ARG GLN LEU VAL CYS
SEQRES 17 A 285 HIS VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL MET
SEQRES 18 A 285 TRP MET ARG GLY ASP GLN GLU GLN GLN GLY THR HIS ARG
SEQRES 19 A 285 GLY ASP PHE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU
SEQRES 20 A 285 GLN ALA THR LEU ASP VAL GLU ALA GLY GLU GLU ALA GLY
SEQRES 21 A 285 LEU ALA CYS ARG VAL LYS HIS SER SER LEU GLY GLY GLN
SEQRES 22 A 285 ASP ILE ILE LEU TYR TRP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 B 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 B 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 B 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 B 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 B 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 B 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 B 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 C 209 MET LYS THR GLN VAL GLU GLN SER PRO GLN SER LEU VAL
SEQRES 2 C 209 VAL ARG GLN GLY GLU ASN CYS VAL LEU GLN CYS ASN TYR
SEQRES 3 C 209 SER VAL THR PRO ASP ASN HIS LEU ARG TRP PHE LYS GLN
SEQRES 4 C 209 ASP THR GLY LYS GLY LEU VAL SER LEU THR VAL LEU VAL
SEQRES 5 C 209 ASP GLN LYS ASP LYS THR SER ASN GLY ARG TYR SER ALA
SEQRES 6 C 209 THR LEU ASP LYS ASP ALA LYS HIS SER THR LEU HIS ILE
SEQRES 7 C 209 THR ALA THR LEU LEU ASP ASP THR ALA THR TYR ILE CYS
SEQRES 8 C 209 VAL VAL GLY ASP ARG GLY SER ALA LEU GLY ARG LEU HIS
SEQRES 9 C 209 PHE GLY ALA GLY THR GLN LEU ILE VAL ILE PRO ASP ILE
SEQRES 10 C 209 GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER
SEQRES 11 C 209 LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE
SEQRES 12 C 209 ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP
SEQRES 13 C 209 VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER
SEQRES 14 C 209 MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN
SEQRES 15 C 209 LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER
SEQRES 16 C 209 ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER
SEQRES 17 C 209 SER
SEQRES 1 D 241 MET GLU ALA ALA VAL THR GLN SER PRO ARG ASN LYS VAL
SEQRES 2 D 241 ALA VAL THR GLY GLY LYS VAL THR LEU SER CYS ASN GLN
SEQRES 3 D 241 THR ASN ASN HIS ASN ASN MET TYR TRP TYR ARG GLN ASP
SEQRES 4 D 241 THR GLY HIS GLY LEU ARG LEU ILE HIS TYR SER TYR GLY
SEQRES 5 D 241 ALA GLY SER THR GLU LYS GLY ASP ILE PRO ASP GLY TYR
SEQRES 6 D 241 LYS ALA SER ARG PRO SER GLN GLU ASN PHE SER LEU ILE
SEQRES 7 D 241 LEU GLU LEU ALA THR PRO SER GLN THR SER VAL TYR PHE
SEQRES 8 D 241 CYS ALA SER GLY ASP GLU GLY TYR THR GLN TYR PHE GLY
SEQRES 9 D 241 PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU ARG ASN
SEQRES 10 D 241 VAL THR PRO PRO LYS VAL SER LEU PHE GLU PRO SER LYS
SEQRES 11 D 241 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS
SEQRES 12 D 241 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER
SEQRES 13 D 241 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS
SEQRES 14 D 241 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN
SEQRES 15 D 241 ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER
SEQRES 16 D 241 ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS
SEQRES 17 D 241 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP
SEQRES 18 D 241 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER
SEQRES 19 D 241 ALA GLU ALA TRP GLY ARG ALA
SEQRES 1 E 285 SER GLU ALA GLN GLN LYS ASN TYR THR PHE ARG CYS LEU
SEQRES 2 E 285 GLN MET SER SER PHE ALA ASN ARG SER TRP SER ARG THR
SEQRES 3 E 285 ASP SER VAL VAL TRP LEU GLY ASP LEU GLN THR HIS ARG
SEQRES 4 E 285 TRP SER ASN ASP SER ALA THR ILE SER PHE THR LYS PRO
SEQRES 5 E 285 TRP SER GLN GLY LYS LEU SER ASN GLN GLN TRP GLU LYS
SEQRES 6 E 285 LEU GLN HIS MET PHE GLN VAL TYR ARG VAL SER PHE THR
SEQRES 7 E 285 ARG ASP ILE GLN GLU LEU VAL LYS MET MET SER PRO LYS
SEQRES 8 E 285 GLU ASP TYR PRO ILE GLU ILE GLN LEU SER ALA GLY CYS
SEQRES 9 E 285 GLU MET TYR PRO GLY ASN ALA SER GLU SER PHE LEU HIS
SEQRES 10 E 285 VAL ALA PHE GLN GLY LYS TYR VAL VAL ARG PHE TRP GLY
SEQRES 11 E 285 THR SER TRP GLN THR VAL PRO GLY ALA PRO SER TRP LEU
SEQRES 12 E 285 ASP LEU PRO ILE LYS VAL LEU ASN ALA ASP GLN GLY THR
SEQRES 13 E 285 SER ALA THR VAL GLN MET LEU LEU ASN ASP THR CYS PRO
SEQRES 14 E 285 LEU PHE VAL ARG GLY LEU LEU GLU ALA GLY LYS SER ASP
SEQRES 15 E 285 LEU GLU LYS GLN GLU LYS PRO VAL ALA TRP LEU SER SER
SEQRES 16 E 285 VAL PRO SER SER ALA HIS GLY HIS ARG GLN LEU VAL CYS
SEQRES 17 E 285 HIS VAL SER GLY PHE TYR PRO LYS PRO VAL TRP VAL MET
SEQRES 18 E 285 TRP MET ARG GLY ASP GLN GLU GLN GLN GLY THR HIS ARG
SEQRES 19 E 285 GLY ASP PHE LEU PRO ASN ALA ASP GLU THR TRP TYR LEU
SEQRES 20 E 285 GLN ALA THR LEU ASP VAL GLU ALA GLY GLU GLU ALA GLY
SEQRES 21 E 285 LEU ALA CYS ARG VAL LYS HIS SER SER LEU GLY GLY GLN
SEQRES 22 E 285 ASP ILE ILE LEU TYR TRP HIS HIS HIS HIS HIS HIS
SEQRES 1 F 99 ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS
SEQRES 2 F 99 PRO PRO GLU ASN GLY LYS PRO ASN ILE LEU ASN CYS TYR
SEQRES 3 F 99 VAL THR GLN PHE HIS PRO PRO HIS ILE GLU ILE GLN MET
SEQRES 4 F 99 LEU LYS ASN GLY LYS LYS ILE PRO LYS VAL GLU MET SER
SEQRES 5 F 99 ASP MET SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU
SEQRES 6 F 99 ALA HIS THR GLU PHE THR PRO THR GLU THR ASP THR TYR
SEQRES 7 F 99 ALA CYS ARG VAL LYS HIS ALA SER MET ALA GLU PRO LYS
SEQRES 8 F 99 THR VAL TYR TRP ASP ARG ASP MET
SEQRES 1 G 209 MET LYS THR GLN VAL GLU GLN SER PRO GLN SER LEU VAL
SEQRES 2 G 209 VAL ARG GLN GLY GLU ASN CYS VAL LEU GLN CYS ASN TYR
SEQRES 3 G 209 SER VAL THR PRO ASP ASN HIS LEU ARG TRP PHE LYS GLN
SEQRES 4 G 209 ASP THR GLY LYS GLY LEU VAL SER LEU THR VAL LEU VAL
SEQRES 5 G 209 ASP GLN LYS ASP LYS THR SER ASN GLY ARG TYR SER ALA
SEQRES 6 G 209 THR LEU ASP LYS ASP ALA LYS HIS SER THR LEU HIS ILE
SEQRES 7 G 209 THR ALA THR LEU LEU ASP ASP THR ALA THR TYR ILE CYS
SEQRES 8 G 209 VAL VAL GLY ASP ARG GLY SER ALA LEU GLY ARG LEU HIS
SEQRES 9 G 209 PHE GLY ALA GLY THR GLN LEU ILE VAL ILE PRO ASP ILE
SEQRES 10 G 209 GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER
SEQRES 11 G 209 LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE
SEQRES 12 G 209 ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP
SEQRES 13 G 209 VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER
SEQRES 14 G 209 MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN
SEQRES 15 G 209 LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER
SEQRES 16 G 209 ILE ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER
SEQRES 17 G 209 SER
SEQRES 1 H 241 MET GLU ALA ALA VAL THR GLN SER PRO ARG ASN LYS VAL
SEQRES 2 H 241 ALA VAL THR GLY GLY LYS VAL THR LEU SER CYS ASN GLN
SEQRES 3 H 241 THR ASN ASN HIS ASN ASN MET TYR TRP TYR ARG GLN ASP
SEQRES 4 H 241 THR GLY HIS GLY LEU ARG LEU ILE HIS TYR SER TYR GLY
SEQRES 5 H 241 ALA GLY SER THR GLU LYS GLY ASP ILE PRO ASP GLY TYR
SEQRES 6 H 241 LYS ALA SER ARG PRO SER GLN GLU ASN PHE SER LEU ILE
SEQRES 7 H 241 LEU GLU LEU ALA THR PRO SER GLN THR SER VAL TYR PHE
SEQRES 8 H 241 CYS ALA SER GLY ASP GLU GLY TYR THR GLN TYR PHE GLY
SEQRES 9 H 241 PRO GLY THR ARG LEU LEU VAL LEU GLU ASP LEU ARG ASN
SEQRES 10 H 241 VAL THR PRO PRO LYS VAL SER LEU PHE GLU PRO SER LYS
SEQRES 11 H 241 ALA GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS
SEQRES 12 H 241 LEU ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER
SEQRES 13 H 241 TRP TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS
SEQRES 14 H 241 THR ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN
SEQRES 15 H 241 ASP SER ARG TYR SER LEU SER SER ARG LEU ARG VAL SER
SEQRES 16 H 241 ALA THR PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS
SEQRES 17 H 241 GLN VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP
SEQRES 18 H 241 THR GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER
SEQRES 19 H 241 ALA GLU ALA TRP GLY ARG ALA
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG A 301 14
HET 49X A 306 48
HET NAG E 301 14
HET NAG E 302 14
HET 49X E 305 48
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 49X (1R)-1,5-ANHYDRO-1-{(1E,3S,4S,5R)-4,5-DIHYDROXY-3-[(8-
HETNAM 2 49X PHENYLOCTANOYL)AMINO]NONADEC-1-EN-1-YL}-D-GALACTITOL
HETSYN 49X GCK152
FORMUL 9 NAG 9(C8 H15 N O6)
FORMUL 13 49X 2(C39 H67 N O8)
HELIX 1 AA1 SER A 59 MET A 87 1 29
HELIX 2 AA2 PRO A 140 TRP A 142 5 3
HELIX 3 AA3 LEU A 143 ASP A 153 1 11
HELIX 4 AA4 ASP A 153 ASP A 166 1 14
HELIX 5 AA5 ASP A 166 GLY A 179 1 14
HELIX 6 AA6 GLY A 179 GLU A 184 1 6
HELIX 7 AA7 LEU C 81 THR C 85 5 5
HELIX 8 AA8 ARG C 167 ASP C 170 5 4
HELIX 9 AA9 ALA C 186 ALA C 190 5 5
HELIX 10 AB1 THR D 82 THR D 86 5 5
HELIX 11 AB2 SER D 128 GLN D 136 1 9
HELIX 12 AB3 ALA D 195 ASN D 200 1 6
HELIX 13 AB4 SER E 59 MET E 87 1 29
HELIX 14 AB5 PRO E 140 TRP E 142 5 3
HELIX 15 AB6 LEU E 143 ASP E 153 1 11
HELIX 16 AB7 ASP E 153 ASP E 166 1 14
HELIX 17 AB8 ASP E 166 GLY E 179 1 14
HELIX 18 AB9 GLY E 179 GLU E 184 1 6
HELIX 19 AC1 LEU G 81 THR G 85 5 5
HELIX 20 AC2 ARG G 167 ASP G 170 5 4
HELIX 21 AC3 ALA G 186 ALA G 190 5 5
HELIX 22 AC4 THR H 82 THR H 86 5 5
HELIX 23 AC5 SER H 128 GLN H 136 1 9
HELIX 24 AC6 ALA H 195 ASN H 200 1 6
SHEET 1 AA1 8 SER A 48 PHE A 49 0
SHEET 2 AA1 8 LEU A 35 TRP A 40 -1 N ARG A 39 O SER A 48
SHEET 3 AA1 8 SER A 24 LEU A 32 -1 N VAL A 30 O THR A 37
SHEET 4 AA1 8 PHE A 10 PHE A 18 -1 N LEU A 13 O VAL A 29
SHEET 5 AA1 8 ILE A 96 MET A 106 -1 O ALA A 102 N CYS A 12
SHEET 6 AA1 8 SER A 112 PHE A 120 -1 O ALA A 119 N GLN A 99
SHEET 7 AA1 8 LYS A 123 TRP A 129 -1 O VAL A 126 N VAL A 118
SHEET 8 AA1 8 SER A 132 THR A 135 -1 O GLN A 134 N ARG A 127
SHEET 1 AA2 4 VAL A 190 VAL A 196 0
SHEET 2 AA2 4 GLN A 205 PHE A 213 -1 O VAL A 207 N SER A 194
SHEET 3 AA2 4 THR A 244 ASP A 252 -1 O LEU A 247 N VAL A 210
SHEET 4 AA2 4 THR A 232 ARG A 234 -1 N HIS A 233 O THR A 250
SHEET 1 AA3 4 VAL A 190 VAL A 196 0
SHEET 2 AA3 4 GLN A 205 PHE A 213 -1 O VAL A 207 N SER A 194
SHEET 3 AA3 4 THR A 244 ASP A 252 -1 O LEU A 247 N VAL A 210
SHEET 4 AA3 4 LEU A 238 ASN A 240 -1 N LEU A 238 O TYR A 246
SHEET 1 AA4 4 GLN A 227 GLU A 228 0
SHEET 2 AA4 4 TRP A 219 ARG A 224 -1 N ARG A 224 O GLN A 227
SHEET 3 AA4 4 ALA A 262 LYS A 266 -1 O LYS A 266 N TRP A 219
SHEET 4 AA4 4 ILE A 275 TYR A 278 -1 O LEU A 277 N CYS A 263
SHEET 1 AA5 4 GLN B 6 SER B 11 0
SHEET 2 AA5 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA5 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 AA5 4 GLU B 50 MET B 51 -1 N GLU B 50 O HIS B 67
SHEET 1 AA6 4 GLN B 6 SER B 11 0
SHEET 2 AA6 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 AA6 4 PHE B 62 PHE B 70 -1 O ALA B 66 N CYS B 25
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 LYS B 44 LYS B 45 0
SHEET 2 AA7 4 ILE B 35 LYS B 41 -1 N LYS B 41 O LYS B 44
SHEET 3 AA7 4 TYR B 78 HIS B 84 -1 O ARG B 81 N GLN B 38
SHEET 4 AA7 4 LYS B 91 TYR B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 AA8 5 VAL C 4 SER C 7 0
SHEET 2 AA8 5 CYS C 19 TYR C 25 -1 O ASN C 24 N GLU C 5
SHEET 3 AA8 5 HIS C 72 ILE C 77 -1 O SER C 73 N CYS C 23
SHEET 4 AA8 5 TYR C 62 ASP C 67 -1 N SER C 63 O HIS C 76
SHEET 5 AA8 5 LYS C 54 ASN C 59 -1 N ASN C 59 O TYR C 62
SHEET 1 AA9 5 SER C 10 ARG C 14 0
SHEET 2 AA9 5 THR C 108 ILE C 113 1 O ILE C 113 N VAL C 13
SHEET 3 AA9 5 ALA C 86 GLY C 93 -1 N TYR C 88 O THR C 108
SHEET 4 AA9 5 HIS C 32 GLN C 38 -1 N ARG C 34 O VAL C 91
SHEET 5 AA9 5 LEU C 44 LEU C 50 -1 O LEU C 50 N LEU C 33
SHEET 1 AB1 4 SER C 10 ARG C 14 0
SHEET 2 AB1 4 THR C 108 ILE C 113 1 O ILE C 113 N VAL C 13
SHEET 3 AB1 4 ALA C 86 GLY C 93 -1 N TYR C 88 O THR C 108
SHEET 4 AB1 4 LEU C 102 PHE C 104 -1 O HIS C 103 N VAL C 92
SHEET 1 AB2 8 VAL C 156 ILE C 158 0
SHEET 2 AB2 8 PHE C 171 SER C 180 -1 O TRP C 179 N TYR C 157
SHEET 3 AB2 8 SER C 135 THR C 140 -1 N CYS C 137 O ALA C 178
SHEET 4 AB2 8 ALA C 122 ASP C 128 -1 N TYR C 124 O LEU C 138
SHEET 5 AB2 8 LYS D 121 GLU D 126 -1 O GLU D 126 N ARG C 127
SHEET 6 AB2 8 LYS D 137 PHE D 147 -1 O VAL D 141 N PHE D 125
SHEET 7 AB2 8 TYR D 185 SER D 194 -1 O TYR D 185 N PHE D 147
SHEET 8 AB2 8 VAL D 167 THR D 169 -1 N CYS D 168 O ARG D 190
SHEET 1 AB3 8 CYS C 162 MET C 166 0
SHEET 2 AB3 8 PHE C 171 SER C 180 -1 O PHE C 171 N MET C 166
SHEET 3 AB3 8 SER C 135 THR C 140 -1 N CYS C 137 O ALA C 178
SHEET 4 AB3 8 ALA C 122 ASP C 128 -1 N TYR C 124 O LEU C 138
SHEET 5 AB3 8 LYS D 121 GLU D 126 -1 O GLU D 126 N ARG C 127
SHEET 6 AB3 8 LYS D 137 PHE D 147 -1 O VAL D 141 N PHE D 125
SHEET 7 AB3 8 TYR D 185 SER D 194 -1 O TYR D 185 N PHE D 147
SHEET 8 AB3 8 LEU D 174 LYS D 175 -1 N LEU D 174 O SER D 186
SHEET 1 AB4 4 VAL D 4 SER D 7 0
SHEET 2 AB4 4 VAL D 19 GLN D 25 -1 O ASN D 24 N THR D 5
SHEET 3 AB4 4 ASN D 73 LEU D 78 -1 O LEU D 76 N LEU D 21
SHEET 4 AB4 4 LYS D 65 SER D 67 -1 N LYS D 65 O ILE D 77
SHEET 1 AB5 6 ASN D 10 VAL D 14 0
SHEET 2 AB5 6 THR D 106 LEU D 111 1 O LEU D 111 N ALA D 13
SHEET 3 AB5 6 SER D 87 GLY D 94 -1 N TYR D 89 O THR D 106
SHEET 4 AB5 6 ASN D 31 GLN D 37 -1 N TYR D 35 O PHE D 90
SHEET 5 AB5 6 ARG D 44 SER D 49 -1 O ILE D 46 N TRP D 34
SHEET 6 AB5 6 GLU D 56 LYS D 57 -1 O GLU D 56 N TYR D 48
SHEET 1 AB6 4 ASN D 10 VAL D 14 0
SHEET 2 AB6 4 THR D 106 LEU D 111 1 O LEU D 111 N ALA D 13
SHEET 3 AB6 4 SER D 87 GLY D 94 -1 N TYR D 89 O THR D 106
SHEET 4 AB6 4 TYR D 101 PHE D 102 -1 O TYR D 101 N SER D 93
SHEET 1 AB7 4 LYS D 161 VAL D 163 0
SHEET 2 AB7 4 VAL D 152 VAL D 158 -1 N TRP D 156 O VAL D 163
SHEET 3 AB7 4 HIS D 204 PHE D 211 -1 O ARG D 206 N TRP D 157
SHEET 4 AB7 4 GLN D 230 TRP D 237 -1 O GLN D 230 N PHE D 211
SHEET 1 AB8 8 SER E 48 PHE E 49 0
SHEET 2 AB8 8 LEU E 35 TRP E 40 -1 N ARG E 39 O SER E 48
SHEET 3 AB8 8 TRP E 23 LEU E 32 -1 N VAL E 30 O THR E 37
SHEET 4 AB8 8 PHE E 10 ASN E 20 -1 N LEU E 13 O VAL E 29
SHEET 5 AB8 8 ILE E 96 MET E 106 -1 O ILE E 96 N PHE E 18
SHEET 6 AB8 8 SER E 112 PHE E 120 -1 O ALA E 119 N GLN E 99
SHEET 7 AB8 8 LYS E 123 TRP E 129 -1 O VAL E 126 N VAL E 118
SHEET 8 AB8 8 SER E 132 THR E 135 -1 O SER E 132 N TRP E 129
SHEET 1 AB9 4 VAL E 190 VAL E 196 0
SHEET 2 AB9 4 GLN E 205 PHE E 213 -1 O VAL E 207 N SER E 194
SHEET 3 AB9 4 THR E 244 ASP E 252 -1 O LEU E 247 N VAL E 210
SHEET 4 AB9 4 THR E 232 ARG E 234 -1 N HIS E 233 O THR E 250
SHEET 1 AC1 4 VAL E 190 VAL E 196 0
SHEET 2 AC1 4 GLN E 205 PHE E 213 -1 O VAL E 207 N SER E 194
SHEET 3 AC1 4 THR E 244 ASP E 252 -1 O LEU E 247 N VAL E 210
SHEET 4 AC1 4 LEU E 238 ASN E 240 -1 N LEU E 238 O TYR E 246
SHEET 1 AC2 4 GLN E 227 GLU E 228 0
SHEET 2 AC2 4 TRP E 219 ARG E 224 -1 N ARG E 224 O GLN E 227
SHEET 3 AC2 4 ALA E 262 LYS E 266 -1 O ALA E 262 N MET E 223
SHEET 4 AC2 4 ILE E 275 TYR E 278 -1 O ILE E 275 N VAL E 265
SHEET 1 AC3 4 GLN F 6 SER F 11 0
SHEET 2 AC3 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 AC3 4 PHE F 62 PHE F 70 -1 O ALA F 66 N CYS F 25
SHEET 4 AC3 4 GLU F 50 MET F 51 -1 N GLU F 50 O HIS F 67
SHEET 1 AC4 4 GLN F 6 SER F 11 0
SHEET 2 AC4 4 ASN F 21 PHE F 30 -1 O ASN F 24 N TYR F 10
SHEET 3 AC4 4 PHE F 62 PHE F 70 -1 O ALA F 66 N CYS F 25
SHEET 4 AC4 4 SER F 55 PHE F 56 -1 N SER F 55 O TYR F 63
SHEET 1 AC5 4 LYS F 44 LYS F 45 0
SHEET 2 AC5 4 ILE F 35 LYS F 41 -1 N LYS F 41 O LYS F 44
SHEET 3 AC5 4 TYR F 78 HIS F 84 -1 O ARG F 81 N GLN F 38
SHEET 4 AC5 4 LYS F 91 TYR F 94 -1 O LYS F 91 N VAL F 82
SHEET 1 AC6 5 VAL G 4 SER G 7 0
SHEET 2 AC6 5 CYS G 19 TYR G 25 -1 O ASN G 24 N GLU G 5
SHEET 3 AC6 5 HIS G 72 ILE G 77 -1 O SER G 73 N CYS G 23
SHEET 4 AC6 5 TYR G 62 ASP G 67 -1 N SER G 63 O HIS G 76
SHEET 5 AC6 5 LYS G 54 ASN G 59 -1 N ASP G 55 O LEU G 66
SHEET 1 AC7 5 SER G 10 ARG G 14 0
SHEET 2 AC7 5 THR G 108 ILE G 113 1 O ILE G 113 N VAL G 13
SHEET 3 AC7 5 ALA G 86 GLY G 93 -1 N ALA G 86 O LEU G 110
SHEET 4 AC7 5 HIS G 32 GLN G 38 -1 N ARG G 34 O VAL G 91
SHEET 5 AC7 5 LEU G 44 LEU G 50 -1 O LEU G 50 N LEU G 33
SHEET 1 AC8 4 SER G 10 ARG G 14 0
SHEET 2 AC8 4 THR G 108 ILE G 113 1 O ILE G 113 N VAL G 13
SHEET 3 AC8 4 ALA G 86 GLY G 93 -1 N ALA G 86 O LEU G 110
SHEET 4 AC8 4 LEU G 102 PHE G 104 -1 O HIS G 103 N VAL G 92
SHEET 1 AC9 4 ALA G 122 ARG G 127 0
SHEET 2 AC9 4 SER G 135 THR G 140 -1 O LEU G 138 N TYR G 124
SHEET 3 AC9 4 PHE G 171 SER G 180 -1 O ALA G 178 N CYS G 137
SHEET 4 AC9 4 VAL G 156 ILE G 158 -1 N TYR G 157 O TRP G 179
SHEET 1 AD1 4 ALA G 122 ARG G 127 0
SHEET 2 AD1 4 SER G 135 THR G 140 -1 O LEU G 138 N TYR G 124
SHEET 3 AD1 4 PHE G 171 SER G 180 -1 O ALA G 178 N CYS G 137
SHEET 4 AD1 4 CYS G 162 MET G 166 -1 N MET G 166 O PHE G 171
SHEET 1 AD2 4 VAL H 4 SER H 7 0
SHEET 2 AD2 4 VAL H 19 GLN H 25 -1 O ASN H 24 N THR H 5
SHEET 3 AD2 4 ASN H 73 LEU H 78 -1 O LEU H 76 N LEU H 21
SHEET 4 AD2 4 LYS H 65 SER H 67 -1 N LYS H 65 O ILE H 77
SHEET 1 AD3 6 ASN H 10 VAL H 14 0
SHEET 2 AD3 6 THR H 106 LEU H 111 1 O LEU H 111 N ALA H 13
SHEET 3 AD3 6 SER H 87 GLY H 94 -1 N TYR H 89 O THR H 106
SHEET 4 AD3 6 ASN H 31 GLN H 37 -1 N TYR H 35 O PHE H 90
SHEET 5 AD3 6 ARG H 44 SER H 49 -1 O ILE H 46 N TRP H 34
SHEET 6 AD3 6 GLU H 56 LYS H 57 -1 O GLU H 56 N TYR H 48
SHEET 1 AD4 4 ASN H 10 VAL H 14 0
SHEET 2 AD4 4 THR H 106 LEU H 111 1 O LEU H 111 N ALA H 13
SHEET 3 AD4 4 SER H 87 GLY H 94 -1 N TYR H 89 O THR H 106
SHEET 4 AD4 4 TYR H 101 PHE H 102 -1 O TYR H 101 N SER H 93
SHEET 1 AD5 4 LYS H 121 PHE H 125 0
SHEET 2 AD5 4 LYS H 137 PHE H 147 -1 O VAL H 141 N PHE H 125
SHEET 3 AD5 4 TYR H 185 SER H 194 -1 O TYR H 185 N PHE H 147
SHEET 4 AD5 4 VAL H 167 THR H 169 -1 N CYS H 168 O ARG H 190
SHEET 1 AD6 4 LYS H 121 PHE H 125 0
SHEET 2 AD6 4 LYS H 137 PHE H 147 -1 O VAL H 141 N PHE H 125
SHEET 3 AD6 4 TYR H 185 SER H 194 -1 O TYR H 185 N PHE H 147
SHEET 4 AD6 4 LEU H 174 LYS H 175 -1 N LEU H 174 O SER H 186
SHEET 1 AD7 4 LYS H 161 VAL H 163 0
SHEET 2 AD7 4 VAL H 152 VAL H 158 -1 N TRP H 156 O VAL H 163
SHEET 3 AD7 4 HIS H 204 PHE H 211 -1 O GLN H 210 N GLU H 153
SHEET 4 AD7 4 GLN H 230 TRP H 237 -1 O GLN H 230 N PHE H 211
SSBOND 1 CYS A 104 CYS A 168 1555 1555 2.07
SSBOND 2 CYS A 208 CYS A 263 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.05
SSBOND 4 CYS C 23 CYS C 90 1555 1555 2.05
SSBOND 5 CYS C 137 CYS C 187 1555 1555 2.06
SSBOND 6 CYS C 162 CYS D 168 1555 1555 2.05
SSBOND 7 CYS D 23 CYS D 91 1555 1555 2.03
SSBOND 8 CYS D 142 CYS D 207 1555 1555 2.01
SSBOND 9 CYS E 104 CYS E 168 1555 1555 2.09
SSBOND 10 CYS E 208 CYS E 263 1555 1555 2.05
SSBOND 11 CYS F 25 CYS F 80 1555 1555 2.03
SSBOND 12 CYS G 23 CYS G 90 1555 1555 2.07
SSBOND 13 CYS G 137 CYS G 187 1555 1555 2.05
SSBOND 14 CYS G 162 CYS H 168 1555 1555 2.04
SSBOND 15 CYS H 23 CYS H 91 1555 1555 2.04
SSBOND 16 CYS H 142 CYS H 207 1555 1555 2.02
LINK ND2 ASN A 20 C1 NAG A 301 1555 1555 1.45
LINK ND2 ASN A 42 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN A 165 C1 NAG J 1 1555 1555 1.43
LINK ND2 ASN E 20 C1 NAG E 301 1555 1555 1.45
LINK ND2 ASN E 42 C1 NAG E 302 1555 1555 1.45
LINK ND2 ASN E 165 C1 NAG K 1 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
CISPEP 1 SER A 89 PRO A 90 0 9.40
CISPEP 2 TYR A 94 PRO A 95 0 -5.43
CISPEP 3 TYR A 214 PRO A 215 0 -3.31
CISPEP 4 HIS B 31 PRO B 32 0 -0.29
CISPEP 5 SER C 7 PRO C 8 0 -4.66
CISPEP 6 THR C 28 PRO C 29 0 -10.97
CISPEP 7 SER D 7 PRO D 8 0 -4.45
CISPEP 8 TYR D 148 PRO D 149 0 4.50
CISPEP 9 SER E 89 PRO E 90 0 9.60
CISPEP 10 TYR E 94 PRO E 95 0 -3.21
CISPEP 11 TYR E 214 PRO E 215 0 -3.78
CISPEP 12 HIS F 31 PRO F 32 0 0.77
CISPEP 13 SER G 7 PRO G 8 0 -7.96
CISPEP 14 THR G 28 PRO G 29 0 -7.58
CISPEP 15 SER H 7 PRO H 8 0 -5.60
CISPEP 16 TYR H 148 PRO H 149 0 1.99
CRYST1 79.417 150.379 102.490 90.00 96.38 90.00 P 1 21 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 0.012592 0.000000 0.001407 0.00000
SCALE2 0.000000 0.006650 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009818 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.997043 0.041398 0.064737 40.81194 1
MTRIX2 2 -0.041125 -0.999139 0.005554 -36.77849 1
MTRIX3 2 0.064912 0.002876 0.997887 -2.33907 1
MTRIX1 3 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 3 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 3 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 4 -0.995314 0.056389 0.078557 40.95880 1
MTRIX2 4 -0.057122 -0.998342 -0.007124 -36.31078 1
MTRIX3 4 0.078025 -0.011578 0.996884 -3.08952 1
MTRIX1 5 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 5 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 5 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 6 -0.999613 0.002857 0.027687 40.28025 1
MTRIX2 6 -0.003041 -0.999974 -0.006609 -37.93292 1
MTRIX3 6 0.027667 -0.006690 0.999595 -1.69107 1
MTRIX1 7 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 7 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 7 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 8 -0.999839 0.007597 0.016282 40.23067 1
MTRIX2 8 -0.007633 -0.999969 -0.002158 -37.58942 1
MTRIX3 8 0.016265 -0.002281 0.999865 -1.03432 1
MTRIX1 9 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 9 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 9 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 10 -0.997757 0.049491 0.045079 41.59468 1
MTRIX2 10 -0.050664 -0.998396 -0.025261 -35.80098 1
MTRIX3 10 0.043757 -0.027488 0.998664 -3.00205 1
(ATOM LINES ARE NOT SHOWN.)
END
