HEADER IMMUNE SYSTEM 17-AUG-16 5GSR
TITLE MOUSE MHC CLASS I H-2KD WITH A MERS-COV-DERIVED PEPTIDE I5A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 3 CHAIN: D, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-D ALPHA CHAIN;
COMPND 7 CHAIN: A, C;
COMPND 8 FRAGMENT: UNP RESIDUES 22-295;
COMPND 9 SYNONYM: H-2K(D);
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: 9-MER PEPTIDE FROM SPIKE PROTEIN;
COMPND 13 CHAIN: P, Q;
COMPND 14 FRAGMENT: UNP RESIDUES 292-300;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: H2-K1, H2-K;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS;
SOURCE 18 ORGANISM_TAXID: 1335626
KEYWDS MOUSE, H-2KD, MERS-COV, T-CELL, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.LIU,Y.CHAI,J.QI,W.TAN,W.J.LIU,G.F.GAO
REVDAT 1 26-APR-17 5GSR 0
JRNL AUTH W.J.LIU,J.LAN,K.LIU,Y.DENG,Y.YAO,S.WU,H.CHEN,L.BAO,H.ZHANG,
JRNL AUTH 2 M.ZHAO,Q.WANG,L.HAN,Y.CHAI,J.QI,J.ZHAO,S.MENG,C.QIN,G.F.GAO,
JRNL AUTH 3 W.TAN
JRNL TITL PROTECTIVE T CELL RESPONSES FEATURED BY CONCORDANT
JRNL TITL 2 RECOGNITION OF MIDDLE EAST RESPIRATORY SYNDROME
JRNL TITL 3 CORONAVIRUS-DERIVED CD8+ T CELL EPITOPES AND HOST MHC.
JRNL REF J. IMMUNOL. V. 198 873 2017
JRNL REFN ESSN 1550-6606
JRNL PMID 27903740
JRNL DOI 10.4049/JIMMUNOL.1601542
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 48385
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 2390
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 31.8327 - 5.6430 0.96 2734 157 0.1826 0.1987
REMARK 3 2 5.6430 - 4.4830 0.96 2702 121 0.1592 0.2080
REMARK 3 3 4.4830 - 3.9175 0.98 2689 159 0.1668 0.1620
REMARK 3 4 3.9175 - 3.5598 0.99 2767 131 0.1897 0.2284
REMARK 3 5 3.5598 - 3.3050 0.99 2738 157 0.1987 0.2452
REMARK 3 6 3.3050 - 3.1103 1.00 2757 146 0.2103 0.2686
REMARK 3 7 3.1103 - 2.9546 1.00 2681 186 0.2314 0.2649
REMARK 3 8 2.9546 - 2.8261 0.99 2768 152 0.2341 0.2119
REMARK 3 9 2.8261 - 2.7174 0.99 2772 116 0.2397 0.2812
REMARK 3 10 2.7174 - 2.6237 0.99 2707 138 0.2346 0.3143
REMARK 3 11 2.6237 - 2.5417 0.99 2743 136 0.2336 0.2422
REMARK 3 12 2.5417 - 2.4690 0.98 2726 126 0.2398 0.3058
REMARK 3 13 2.4690 - 2.4041 0.99 2752 93 0.2246 0.3085
REMARK 3 14 2.4041 - 2.3454 0.99 2750 145 0.2318 0.2988
REMARK 3 15 2.3454 - 2.2921 0.99 2654 165 0.2324 0.2610
REMARK 3 16 2.2921 - 2.2433 0.97 2688 145 0.2307 0.2507
REMARK 3 17 2.2433 - 2.1985 0.86 2367 117 0.2392 0.2852
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.700
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 : 0.007 6530
REMARK 3 ANGLE : 0.773 8878
REMARK 3 CHIRALITY : 0.060 900
REMARK 3 PLANARITY : 0.003 1156
REMARK 3 DIHEDRAL : 21.545 2396
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5GSR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1300001375.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : 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) : 0.97944
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CNS
REMARK 200 DATA SCALING SOFTWARE : CNS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.198
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M SODIUM HEPES 7.5, 30 % V/V 2-PROPANOL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
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 39.82900
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, C, Q
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, P
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 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 O HOH C 385 O HOH C 400 1.82
REMARK 500 O HOH A 395 O HOH A 409 1.88
REMARK 500 O HOH C 390 O HOH C 392 1.89
REMARK 500 O HOH A 410 O HOH P 101 1.90
REMARK 500 O HOH D 241 O HOH A 421 1.90
REMARK 500 O HOH A 350 O HOH A 416 1.92
REMARK 500 O HOH D 234 O HOH C 345 1.92
REMARK 500 O HOH A 369 O HOH A 414 1.95
REMARK 500 O HOH A 408 O HOH A 418 1.95
REMARK 500 O HOH B 238 O HOH C 371 1.96
REMARK 500 O HOH A 362 O HOH A 408 1.97
REMARK 500 O HOH B 233 O HOH A 383 1.98
REMARK 500 OE1 GLU A 148 O HOH A 301 2.01
REMARK 500 O HOH B 208 O HOH B 228 2.06
REMARK 500 O HOH A 365 O HOH A 426 2.07
REMARK 500 O HOH C 344 O HOH C 378 2.07
REMARK 500 O HOH C 366 O HOH C 387 2.10
REMARK 500 O GLU B 89 O HOH B 201 2.17
REMARK 500 OD2 ASP A 102 O HOH A 302 2.17
REMARK 500 OG SER Q 8 O HOH Q 101 2.17
REMARK 500 O GLU A 177 O HOH A 303 2.18
REMARK 500 OE2 GLU D 56 O HOH D 201 2.18
REMARK 500 O HOH D 230 O HOH D 255 2.19
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 TRP D 80 -1.07 76.80
REMARK 500 TRP B 80 -0.27 78.21
REMARK 500 ARG B 117 12.54 -66.75
REMARK 500 ASP A 29 -121.75 55.83
REMARK 500 TRP A 51 7.85 -63.23
REMARK 500 TRP A 107 25.82 81.92
REMARK 500 ARG A 111 138.51 -170.03
REMARK 500 ASP A 227 31.06 -99.43
REMARK 500 ASP C 29 -123.12 56.53
REMARK 500 TRP C 107 40.67 72.88
REMARK 500 LYS C 131 -31.14 -136.73
REMARK 500 ARG C 194 -54.37 -127.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GSV RELATED DB: PDB
REMARK 900 RELATED ID: 5GSX RELATED DB: PDB
DBREF 5GSR D 20 119 UNP P61769 B2MG_HUMAN 20 119
DBREF 5GSR B 20 119 UNP P61769 B2MG_HUMAN 20 119
DBREF 5GSR A 1 274 UNP P01902 HA1D_MOUSE 22 295
DBREF 5GSR C 1 274 UNP P01902 HA1D_MOUSE 22 295
DBREF1 5GSR P 1 9 UNP A0A0U2W1D8_9BETC
DBREF2 5GSR P A0A0U2W1D8 292 300
DBREF1 5GSR Q 1 9 UNP A0A0U2W1D8_9BETC
DBREF2 5GSR Q A0A0U2W1D8 292 300
SEQADV 5GSR ALA P 5 UNP A0A0U2W1D ILE 296 ENGINEERED MUTATION
SEQADV 5GSR ALA Q 5 UNP A0A0U2W1D ILE 296 ENGINEERED MUTATION
SEQRES 1 D 100 ALA ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 D 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 D 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 D 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 D 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 D 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 D 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 D 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 B 100 ALA ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 A 274 GLY PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER
SEQRES 2 A 274 ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 274 ALA ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET
SEQRES 5 A 274 GLU GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN
SEQRES 6 A 274 ARG ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 A 274 ARG THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY
SEQRES 8 A 274 SER HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY
SEQRES 9 A 274 SER ASP TRP ARG LEU LEU ARG GLY TYR GLN GLN PHE ALA
SEQRES 10 A 274 TYR ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 A 274 LYS THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR
SEQRES 12 A 274 ARG ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR
SEQRES 13 A 274 ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG
SEQRES 14 A 274 ARG TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR
SEQRES 15 A 274 ASP SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER
SEQRES 16 A 274 GLN VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 A 274 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 A 274 GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 A 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 274 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS
SEQRES 21 A 274 VAL HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 A 274 TRP
SEQRES 1 C 274 GLY PRO HIS SER LEU ARG TYR PHE VAL THR ALA VAL SER
SEQRES 2 C 274 ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 C 274 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 C 274 ALA ASP ASN PRO ARG PHE GLU PRO ARG ALA PRO TRP MET
SEQRES 5 C 274 GLU GLN GLU GLY PRO GLU TYR TRP GLU GLU GLN THR GLN
SEQRES 6 C 274 ARG ALA LYS SER ASP GLU GLN TRP PHE ARG VAL SER LEU
SEQRES 7 C 274 ARG THR ALA GLN ARG TYR TYR ASN GLN SER LYS GLY GLY
SEQRES 8 C 274 SER HIS THR PHE GLN ARG MET PHE GLY CYS ASP VAL GLY
SEQRES 9 C 274 SER ASP TRP ARG LEU LEU ARG GLY TYR GLN GLN PHE ALA
SEQRES 10 C 274 TYR ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU
SEQRES 11 C 274 LYS THR TRP THR ALA ALA ASP THR ALA ALA LEU ILE THR
SEQRES 12 C 274 ARG ARG LYS TRP GLU GLN ALA GLY ASP ALA GLU TYR TYR
SEQRES 13 C 274 ARG ALA TYR LEU GLU GLY GLU CYS VAL GLU TRP LEU ARG
SEQRES 14 C 274 ARG TYR LEU GLU LEU GLY ASN GLU THR LEU LEU ARG THR
SEQRES 15 C 274 ASP SER PRO LYS ALA HIS VAL THR TYR HIS PRO ARG SER
SEQRES 16 C 274 GLN VAL ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE
SEQRES 17 C 274 TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY
SEQRES 18 C 274 GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG
SEQRES 19 C 274 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 C 274 VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS HIS
SEQRES 21 C 274 VAL HIS HIS LYS GLY LEU PRO GLU PRO LEU THR LEU ARG
SEQRES 22 C 274 TRP
SEQRES 1 P 9 TYR TYR SER ILE ALA PRO HIS SER ILE
SEQRES 1 Q 9 TYR TYR SER ILE ALA PRO HIS SER ILE
FORMUL 7 HOH *354(H2 O)
HELIX 1 AA1 ALA A 49 GLU A 53 5 5
HELIX 2 AA2 GLY A 56 TYR A 85 1 30
HELIX 3 AA3 ASP A 137 GLY A 151 1 15
HELIX 4 AA4 GLY A 151 GLY A 162 1 12
HELIX 5 AA5 GLY A 162 GLY A 175 1 14
HELIX 6 AA6 LYS A 253 GLN A 255 5 3
HELIX 7 AA7 ALA C 49 GLU C 53 5 5
HELIX 8 AA8 GLY C 56 TYR C 85 1 30
HELIX 9 AA9 ASP C 137 GLY C 151 1 15
HELIX 10 AB1 GLY C 151 GLY C 162 1 12
HELIX 11 AB2 GLY C 162 GLY C 175 1 14
HELIX 12 AB3 LYS C 253 GLN C 255 5 3
SHEET 1 AA1 4 LYS D 26 SER D 31 0
SHEET 2 AA1 4 ASN D 41 PHE D 50 -1 O ASN D 44 N TYR D 30
SHEET 3 AA1 4 PHE D 82 PHE D 90 -1 O LEU D 84 N VAL D 47
SHEET 4 AA1 4 GLU D 70 HIS D 71 -1 N GLU D 70 O TYR D 87
SHEET 1 AA2 4 LYS D 26 SER D 31 0
SHEET 2 AA2 4 ASN D 41 PHE D 50 -1 O ASN D 44 N TYR D 30
SHEET 3 AA2 4 PHE D 82 PHE D 90 -1 O LEU D 84 N VAL D 47
SHEET 4 AA2 4 SER D 75 PHE D 76 -1 N SER D 75 O TYR D 83
SHEET 1 AA3 4 GLU D 64 ARG D 65 0
SHEET 2 AA3 4 GLU D 56 LYS D 61 -1 N LYS D 61 O GLU D 64
SHEET 3 AA3 4 TYR D 98 ASN D 103 -1 O ALA D 99 N LEU D 60
SHEET 4 AA3 4 LYS D 111 LYS D 114 -1 O LYS D 111 N VAL D 102
SHEET 1 AA4 4 LYS B 26 SER B 31 0
SHEET 2 AA4 4 ASN B 41 PHE B 50 -1 O ASN B 44 N TYR B 30
SHEET 3 AA4 4 PHE B 82 PHE B 90 -1 O LEU B 84 N VAL B 47
SHEET 4 AA4 4 GLU B 70 HIS B 71 -1 N GLU B 70 O TYR B 87
SHEET 1 AA5 4 LYS B 26 SER B 31 0
SHEET 2 AA5 4 ASN B 41 PHE B 50 -1 O ASN B 44 N TYR B 30
SHEET 3 AA5 4 PHE B 82 PHE B 90 -1 O LEU B 84 N VAL B 47
SHEET 4 AA5 4 SER B 75 PHE B 76 -1 N SER B 75 O TYR B 83
SHEET 1 AA6 4 GLU B 64 ARG B 65 0
SHEET 2 AA6 4 GLU B 56 LYS B 61 -1 N LYS B 61 O GLU B 64
SHEET 3 AA6 4 TYR B 98 ASN B 103 -1 O ALA B 99 N LEU B 60
SHEET 4 AA6 4 LYS B 111 LYS B 114 -1 O LYS B 111 N VAL B 102
SHEET 1 AA7 8 GLU A 46 PRO A 47 0
SHEET 2 AA7 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA7 8 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31
SHEET 4 AA7 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AA7 8 THR A 94 VAL A 103 -1 O PHE A 99 N TYR A 7
SHEET 6 AA7 8 LEU A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 AA7 8 ARG A 121 LEU A 126 -1 O LEU A 126 N GLN A 114
SHEET 8 AA7 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 AA8 4 LYS A 186 PRO A 193 0
SHEET 2 AA8 4 ASP A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA8 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 AA8 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 AA9 4 LYS A 186 PRO A 193 0
SHEET 2 AA9 4 ASP A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 AA9 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 AA9 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 AB1 4 GLU A 222 ASP A 223 0
SHEET 2 AB1 4 ILE A 213 LEU A 219 -1 N LEU A 219 O GLU A 222
SHEET 3 AB1 4 TYR A 257 HIS A 263 -1 O HIS A 260 N THR A 216
SHEET 4 AB1 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 AB2 8 GLU C 46 PRO C 47 0
SHEET 2 AB2 8 THR C 31 ASP C 37 -1 N ARG C 35 O GLU C 46
SHEET 3 AB2 8 ARG C 21 VAL C 28 -1 N VAL C 28 O THR C 31
SHEET 4 AB2 8 HIS C 3 VAL C 12 -1 N ARG C 6 O TYR C 27
SHEET 5 AB2 8 THR C 94 VAL C 103 -1 O VAL C 103 N HIS C 3
SHEET 6 AB2 8 LEU C 109 TYR C 118 -1 O LEU C 110 N ASP C 102
SHEET 7 AB2 8 ARG C 121 LEU C 126 -1 O TYR C 123 N PHE C 116
SHEET 8 AB2 8 TRP C 133 ALA C 135 -1 O THR C 134 N ALA C 125
SHEET 1 AB3 4 LYS C 186 PRO C 193 0
SHEET 2 AB3 4 ASP C 198 PHE C 208 -1 O TRP C 204 N HIS C 188
SHEET 3 AB3 4 PHE C 241 PRO C 250 -1 O ALA C 245 N CYS C 203
SHEET 4 AB3 4 GLU C 229 LEU C 230 -1 N GLU C 229 O ALA C 246
SHEET 1 AB4 4 LYS C 186 PRO C 193 0
SHEET 2 AB4 4 ASP C 198 PHE C 208 -1 O TRP C 204 N HIS C 188
SHEET 3 AB4 4 PHE C 241 PRO C 250 -1 O ALA C 245 N CYS C 203
SHEET 4 AB4 4 ARG C 234 PRO C 235 -1 N ARG C 234 O GLN C 242
SHEET 1 AB5 4 GLU C 222 ASP C 223 0
SHEET 2 AB5 4 THR C 214 LEU C 219 -1 N LEU C 219 O GLU C 222
SHEET 3 AB5 4 TYR C 257 HIS C 262 -1 O HIS C 260 N THR C 216
SHEET 4 AB5 4 LEU C 270 LEU C 272 -1 O LEU C 272 N CYS C 259
SSBOND 1 CYS D 45 CYS D 100 1555 1555 2.02
SSBOND 2 CYS B 45 CYS B 100 1555 1555 2.03
SSBOND 3 CYS A 101 CYS A 164 1555 1555 2.04
SSBOND 4 CYS A 203 CYS A 259 1555 1555 2.03
SSBOND 5 CYS C 101 CYS C 164 1555 1555 2.04
SSBOND 6 CYS C 203 CYS C 259 1555 1555 2.03
CISPEP 1 HIS D 51 PRO D 52 0 1.60
CISPEP 2 HIS B 51 PRO B 52 0 1.39
CISPEP 3 GLY A 1 PRO A 2 0 -1.42
CISPEP 4 TYR A 209 PRO A 210 0 3.27
CISPEP 5 GLY C 1 PRO C 2 0 -0.78
CISPEP 6 TYR C 209 PRO C 210 0 1.80
CRYST1 50.353 79.658 122.706 90.00 90.30 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 0.019860 0.000000 0.000105 0.00000
SCALE2 0.000000 0.012554 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
