HEADER IMMUNE SYSTEM 18-NOV-15 5EUO
TITLE PF6-M1-HLA-A2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: UNP RESIDUES 25-299;
COMPND 5 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: UNP RESIDUES 21-119;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: PF6 TCR ALPHA CHAIN;
COMPND 14 CHAIN: E, G;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: PF6 TCR BETA CHAIN;
COMPND 18 CHAIN: F, H;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: MATRIX PROTEIN 1;
COMPND 22 CHAIN: I, J;
COMPND 23 SYNONYM: M1;
COMPND 24 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: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET26B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET26B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_TAXID: 9606;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PET26B;
SOURCE 29 MOL_ID: 4;
SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 31 ORGANISM_TAXID: 9606;
SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 34 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 36 EXPRESSION_SYSTEM_PLASMID: PET26B;
SOURCE 37 MOL_ID: 5;
SOURCE 38 SYNTHETIC: YES;
SOURCE 39 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE 40 ORGANISM_TAXID: 211044
KEYWDS TCR, FLU, MHC, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR X.YANG
REVDAT 2 27-SEP-23 5EUO 1 REMARK
REVDAT 1 23-NOV-16 5EUO 0
JRNL AUTH X.YANG,R.A.MARIUZZA
JRNL TITL CRYSTAL STRUCTURE OF PF6-M1-HLA-A2 COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 120.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 113045
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.750
REMARK 3 FREE R VALUE TEST SET COUNT : 1983
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1120.6711 - 5.0612 0.99 8230 144 0.1831 0.2185
REMARK 3 2 5.0612 - 4.0172 1.00 8015 144 0.1744 0.2032
REMARK 3 3 4.0172 - 3.5093 1.00 7996 140 0.2062 0.2739
REMARK 3 4 3.5093 - 3.1884 1.00 7916 136 0.2316 0.3086
REMARK 3 5 3.1884 - 2.9599 1.00 7976 144 0.2464 0.2926
REMARK 3 6 2.9599 - 2.7854 1.00 7908 142 0.2521 0.3588
REMARK 3 7 2.7854 - 2.6459 1.00 7915 143 0.2611 0.3368
REMARK 3 8 2.6459 - 2.5307 1.00 7897 143 0.2672 0.3253
REMARK 3 9 2.5307 - 2.4332 1.00 7895 141 0.2727 0.3372
REMARK 3 10 2.4332 - 2.3493 1.00 7848 143 0.2883 0.3353
REMARK 3 11 2.3493 - 2.2758 1.00 7898 135 0.3052 0.3425
REMARK 3 12 2.2758 - 2.2107 1.00 7883 145 0.3049 0.3349
REMARK 3 13 2.2107 - 2.1525 1.00 7839 142 0.3173 0.3620
REMARK 3 14 2.1525 - 2.1000 1.00 7846 141 0.3498 0.3963
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.36
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 : 0.009 13401
REMARK 3 ANGLE : 1.203 18159
REMARK 3 CHIRALITY : 0.047 1908
REMARK 3 PLANARITY : 0.006 2376
REMARK 3 DIHEDRAL : 15.678 4873
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 5EUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113120
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 133.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 1.75700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 1OGA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, IMIDAZOLE, PH 7, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 27.04100
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H, I
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 MET A 0
REMARK 465 GLU A 275
REMARK 465 MET C 0
REMARK 465 MET E 1
REMARK 465 THR E 2
REMARK 465 GLN E 3
REMARK 465 SER E 194
REMARK 465 ILE E 195
REMARK 465 ILE E 196
REMARK 465 PRO E 197
REMARK 465 GLU E 198
REMARK 465 ASP E 199
REMARK 465 THR E 200
REMARK 465 PHE E 201
REMARK 465 PHE E 202
REMARK 465 PRO E 203
REMARK 465 SER E 204
REMARK 465 PRO E 205
REMARK 465 GLU E 206
REMARK 465 SER E 207
REMARK 465 SER E 208
REMARK 465 ASP F 240
REMARK 465 MET G 1
REMARK 465 THR G 2
REMARK 465 GLN G 3
REMARK 465 ILE G 195
REMARK 465 ILE G 196
REMARK 465 PRO G 197
REMARK 465 GLU G 198
REMARK 465 ASP G 199
REMARK 465 THR G 200
REMARK 465 PHE G 201
REMARK 465 PHE G 202
REMARK 465 PRO G 203
REMARK 465 SER G 204
REMARK 465 PRO G 205
REMARK 465 GLU G 206
REMARK 465 SER G 207
REMARK 465 SER G 208
REMARK 465 ARG H 238
REMARK 465 ALA H 239
REMARK 465 ASP H 240
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 SER A 195 N HIS A 197 1.79
REMARK 500 OG1 THR F 110 OD2 ASP F 181 1.90
REMARK 500 OD2 ASP G 128 O HOH G 401 1.91
REMARK 500 O ASP A 196 N GLU A 198 1.95
REMARK 500 O HOH C 442 O HOH C 491 2.12
REMARK 500 OG SER E 149 O ASN E 193 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 220 CB ARG H 201 16412 1.62
REMARK 500 NH2 ARG A 131 OE2 GLU A 198 15511 1.62
REMARK 500 OD2 ASP A 220 CA ARG H 201 16412 1.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 194 CA - C - N ANGL. DEV. = 13.7 DEGREES
REMARK 500 VAL A 194 O - C - N ANGL. DEV. = -14.0 DEGREES
REMARK 500 ASP A 196 O - C - N ANGL. DEV. = -14.7 DEGREES
REMARK 500 HIS A 197 C - N - CA ANGL. DEV. = -15.1 DEGREES
REMARK 500 HIS A 197 CA - C - N ANGL. DEV. = -18.5 DEGREES
REMARK 500 HIS A 197 O - C - N ANGL. DEV. = 18.4 DEGREES
REMARK 500 LEU E 164 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 14 72.86 -114.61
REMARK 500 ARG A 17 68.17 -100.71
REMARK 500 ASP A 29 -119.05 52.64
REMARK 500 TYR A 84 -16.02 -48.39
REMARK 500 ASP A 106 2.89 -67.78
REMARK 500 TYR A 123 -64.50 -109.64
REMARK 500 ASP A 137 -169.53 -126.11
REMARK 500 THR A 178 -46.74 -136.61
REMARK 500 ALA A 193 79.31 -112.93
REMARK 500 VAL A 194 -153.81 -77.32
REMARK 500 SER A 195 89.64 -63.97
REMARK 500 ASP A 196 -67.56 27.08
REMARK 500 SER A 207 47.95 38.81
REMARK 500 ARG A 219 -158.32 -107.46
REMARK 500 GLU A 222 -163.33 -120.54
REMARK 500 ASP A 227 18.92 56.39
REMARK 500 GLN A 255 10.68 -65.65
REMARK 500 TRP B 60 -4.14 75.19
REMARK 500 HIS B 84 148.54 -172.19
REMARK 500 ARG C 17 28.00 -140.03
REMARK 500 ASP C 29 -120.50 47.94
REMARK 500 HIS C 114 108.35 -165.23
REMARK 500 ASP C 122 129.94 -38.94
REMARK 500 TYR C 123 -70.32 -111.04
REMARK 500 ARG C 131 -34.33 -130.56
REMARK 500 HIS C 151 51.07 39.17
REMARK 500 SER C 195 -150.73 157.90
REMARK 500 SER C 251 -2.83 -58.55
REMARK 500 LYS D 48 72.67 -102.76
REMARK 500 TRP D 60 -1.77 80.50
REMARK 500 GLU E 16 157.95 -47.69
REMARK 500 SER E 28 -148.39 -112.87
REMARK 500 VAL E 51 -30.69 -138.60
REMARK 500 LYS E 60 -127.11 50.91
REMARK 500 PRO F 226 65.11 -68.92
REMARK 500 SER G 28 -145.00 -115.24
REMARK 500 VAL G 51 -35.61 -136.89
REMARK 500 LYS G 60 -113.57 54.74
REMARK 500 ASN G 98 68.95 -118.12
REMARK 500 ASN G 118 70.71 -115.12
REMARK 500 SER G 129 -18.89 -47.74
REMARK 500 SER G 131 -162.66 -120.63
REMARK 500 SER G 132 -42.89 -130.29
REMARK 500 ASP G 170 51.35 33.94
REMARK 500 SER G 175 142.93 -174.75
REMARK 500 PHE G 185 109.45 -55.67
REMARK 500 HIS H 150 77.39 -102.79
REMARK 500 ASN H 202 125.38 -37.28
REMARK 500 GLU H 215 0.72 -66.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 196 -27.13
REMARK 500 LYS G 134 -13.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E 329 DISTANCE = 6.77 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD G 301
DBREF 5EUO A 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 5EUO B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5EUO C 1 275 UNP P01892 1A02_HUMAN 25 299
DBREF 5EUO D 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 5EUO E 1 208 PDB 5EUO 5EUO 1 208
DBREF 5EUO F 1 240 PDB 5EUO 5EUO 1 240
DBREF 5EUO G 1 208 PDB 5EUO 5EUO 1 208
DBREF 5EUO H 1 240 PDB 5EUO 5EUO 1 240
DBREF 5EUO I 1 9 UNP P03485 M1_I34A1 58 66
DBREF 5EUO J 1 9 UNP P03485 M1_I34A1 58 66
SEQADV 5EUO MET A 0 UNP P01892 INITIATING METHIONINE
SEQADV 5EUO MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 5EUO MET C 0 UNP P01892 INITIATING METHIONINE
SEQADV 5EUO MET D 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 276 MET GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL
SEQRES 2 A 276 SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL
SEQRES 3 A 276 GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER
SEQRES 4 A 276 ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP
SEQRES 5 A 276 ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR
SEQRES 6 A 276 ARG LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP
SEQRES 7 A 276 LEU GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA
SEQRES 8 A 276 GLY SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL
SEQRES 9 A 276 GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR
SEQRES 10 A 276 ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP
SEQRES 11 A 276 LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR
SEQRES 12 A 276 THR LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN
SEQRES 13 A 276 LEU ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU
SEQRES 14 A 276 ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG
SEQRES 15 A 276 THR ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL
SEQRES 16 A 276 SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER
SEQRES 17 A 276 PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP
SEQRES 18 A 276 GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR
SEQRES 19 A 276 ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA
SEQRES 20 A 276 VAL VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS
SEQRES 21 A 276 HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU
SEQRES 22 A 276 ARG TRP GLU
SEQRES 1 B 100 MET 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 C 276 MET GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL
SEQRES 2 C 276 SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL
SEQRES 3 C 276 GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER
SEQRES 4 C 276 ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP
SEQRES 5 C 276 ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR
SEQRES 6 C 276 ARG LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP
SEQRES 7 C 276 LEU GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA
SEQRES 8 C 276 GLY SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL
SEQRES 9 C 276 GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR
SEQRES 10 C 276 ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP
SEQRES 11 C 276 LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR
SEQRES 12 C 276 THR LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN
SEQRES 13 C 276 LEU ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU
SEQRES 14 C 276 ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG
SEQRES 15 C 276 THR ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL
SEQRES 16 C 276 SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER
SEQRES 17 C 276 PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP
SEQRES 18 C 276 GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR
SEQRES 19 C 276 ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA
SEQRES 20 C 276 VAL VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS
SEQRES 21 C 276 HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU
SEQRES 22 C 276 ARG TRP GLU
SEQRES 1 D 100 MET 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 E 208 MET THR GLN LEU LEU GLU GLN SER PRO GLN PHE LEU SER
SEQRES 2 E 208 ILE GLN GLU GLY GLU ASN LEU THR VAL TYR CYS ASN SER
SEQRES 3 E 208 SER SER VAL PHE SER SER LEU GLN TRP TYR ARG GLN GLU
SEQRES 4 E 208 PRO GLY GLU GLY PRO VAL LEU LEU VAL THR VAL VAL THR
SEQRES 5 E 208 GLY GLY GLU VAL LYS LYS LEU LYS ARG LEU THR PHE GLN
SEQRES 6 E 208 PHE GLY ASP ALA ARG LYS ASP SER SER LEU HIS ILE THR
SEQRES 7 E 208 ALA ALA GLN PRO GLY ASP THR GLY LEU TYR LEU CYS ALA
SEQRES 8 E 208 GLY ALA ILE GLY PRO SER ASN THR GLY LYS LEU ILE PHE
SEQRES 9 E 208 GLY LYS GLY THR LYS LEU SER VAL LYS PRO ASN ILE GLN
SEQRES 10 E 208 ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS
SEQRES 11 E 208 SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP
SEQRES 12 E 208 SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL
SEQRES 13 E 208 TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET
SEQRES 14 E 208 ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS
SEQRES 15 E 208 SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE
SEQRES 16 E 208 ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 F 240 GLY ILE THR GLN SER PRO LYS TYR LEU PHE ARG LYS GLU
SEQRES 2 F 240 GLY GLN ASN VAL THR LEU SER CYS GLU GLN ASN LEU ASN
SEQRES 3 F 240 HIS ASP ALA MET TYR TRP TYR ARG GLN ASP PRO GLY GLN
SEQRES 4 F 240 GLY LEU ARG LEU ILE TYR TYR SER GLN ILE VAL ASN ASP
SEQRES 5 F 240 PHE GLN LYS GLY ASP ILE ALA GLU GLY TYR SER VAL SER
SEQRES 6 F 240 ARG GLU LYS LYS GLU SER PHE PRO LEU THR VAL THR SER
SEQRES 7 F 240 ALA GLN ALA ASN PRO THR ALA PHE TYR LEU CYS ALA SER
SEQRES 8 F 240 SER ILE ARG SER SER TYR GLU GLN TYR PHE GLY PRO GLY
SEQRES 9 F 240 THR ARG LEU THR VAL THR GLU ASP LEU LYS ASN VAL PHE
SEQRES 10 F 240 PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU ALA GLU
SEQRES 11 F 240 ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS LEU ALA
SEQRES 12 F 240 THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER TRP TRP
SEQRES 13 F 240 VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS THR ASP
SEQRES 14 F 240 PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN ASP SER
SEQRES 15 F 240 ARG TYR SER LEU SER SER ARG LEU ARG VAL SER ALA THR
SEQRES 16 F 240 PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS GLN VAL
SEQRES 17 F 240 GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP THR GLN
SEQRES 18 F 240 ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER ALA GLU
SEQRES 19 F 240 ALA TRP GLY ARG ALA ASP
SEQRES 1 G 208 MET THR GLN LEU LEU GLU GLN SER PRO GLN PHE LEU SER
SEQRES 2 G 208 ILE GLN GLU GLY GLU ASN LEU THR VAL TYR CYS ASN SER
SEQRES 3 G 208 SER SER VAL PHE SER SER LEU GLN TRP TYR ARG GLN GLU
SEQRES 4 G 208 PRO GLY GLU GLY PRO VAL LEU LEU VAL THR VAL VAL THR
SEQRES 5 G 208 GLY GLY GLU VAL LYS LYS LEU LYS ARG LEU THR PHE GLN
SEQRES 6 G 208 PHE GLY ASP ALA ARG LYS ASP SER SER LEU HIS ILE THR
SEQRES 7 G 208 ALA ALA GLN PRO GLY ASP THR GLY LEU TYR LEU CYS ALA
SEQRES 8 G 208 GLY ALA ILE GLY PRO SER ASN THR GLY LYS LEU ILE PHE
SEQRES 9 G 208 GLY LYS GLY THR LYS LEU SER VAL LYS PRO ASN ILE GLN
SEQRES 10 G 208 ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER LYS
SEQRES 11 G 208 SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE ASP
SEQRES 12 G 208 SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP VAL
SEQRES 13 G 208 TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER MET
SEQRES 14 G 208 ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN LYS
SEQRES 15 G 208 SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER ILE
SEQRES 16 G 208 ILE PRO GLU ASP THR PHE PHE PRO SER PRO GLU SER SER
SEQRES 1 H 240 GLY ILE THR GLN SER PRO LYS TYR LEU PHE ARG LYS GLU
SEQRES 2 H 240 GLY GLN ASN VAL THR LEU SER CYS GLU GLN ASN LEU ASN
SEQRES 3 H 240 HIS ASP ALA MET TYR TRP TYR ARG GLN ASP PRO GLY GLN
SEQRES 4 H 240 GLY LEU ARG LEU ILE TYR TYR SER GLN ILE VAL ASN ASP
SEQRES 5 H 240 PHE GLN LYS GLY ASP ILE ALA GLU GLY TYR SER VAL SER
SEQRES 6 H 240 ARG GLU LYS LYS GLU SER PHE PRO LEU THR VAL THR SER
SEQRES 7 H 240 ALA GLN ALA ASN PRO THR ALA PHE TYR LEU CYS ALA SER
SEQRES 8 H 240 SER ILE ARG SER SER TYR GLU GLN TYR PHE GLY PRO GLY
SEQRES 9 H 240 THR ARG LEU THR VAL THR GLU ASP LEU LYS ASN VAL PHE
SEQRES 10 H 240 PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU ALA GLU
SEQRES 11 H 240 ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS LEU ALA
SEQRES 12 H 240 THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER TRP TRP
SEQRES 13 H 240 VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS THR ASP
SEQRES 14 H 240 PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN ASP SER
SEQRES 15 H 240 ARG TYR SER LEU SER SER ARG LEU ARG VAL SER ALA THR
SEQRES 16 H 240 PHE TRP GLN ASN PRO ARG ASN HIS PHE ARG CYS GLN VAL
SEQRES 17 H 240 GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP THR GLN
SEQRES 18 H 240 ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER ALA GLU
SEQRES 19 H 240 ALA TRP GLY ARG ALA ASP
SEQRES 1 I 9 GLY ILE LEU GLY PHE VAL PHE THR LEU
SEQRES 1 J 9 GLY ILE LEU GLY PHE VAL PHE THR LEU
HET IMD C 301 5
HET IMD G 301 5
HETNAM IMD IMIDAZOLE
FORMUL 11 IMD 2(C3 H5 N2 1+)
FORMUL 13 HOH *397(H2 O)
HELIX 1 AA1 ALA A 49 GLU A 55 5 7
HELIX 2 AA2 GLY A 56 TYR A 85 1 30
HELIX 3 AA3 ASP A 137 ALA A 150 1 14
HELIX 4 AA4 HIS A 151 GLU A 161 1 11
HELIX 5 AA5 GLY A 162 GLY A 175 1 14
HELIX 6 AA6 GLY A 175 GLN A 180 1 6
HELIX 7 AA7 GLN A 253 TYR A 257 5 5
HELIX 8 AA8 ALA C 49 GLU C 55 5 7
HELIX 9 AA9 GLY C 56 TYR C 85 1 30
HELIX 10 AB1 ASP C 137 ALA C 150 1 14
HELIX 11 AB2 HIS C 151 GLY C 162 1 12
HELIX 12 AB3 GLY C 162 GLY C 175 1 14
HELIX 13 AB4 GLY C 175 GLN C 180 1 6
HELIX 14 AB5 GLN C 253 GLN C 255 5 3
HELIX 15 AB6 PRO E 96 ASN E 98 5 3
HELIX 16 AB7 ASP F 112 VAL F 116 5 5
HELIX 17 AB8 SER F 127 GLN F 135 1 9
HELIX 18 AB9 ALA F 194 GLN F 198 1 5
HELIX 19 AC1 GLN G 81 THR G 85 5 5
HELIX 20 AC2 ALA G 186 ALA G 190 5 5
HELIX 21 AC3 ASP H 112 VAL H 116 5 5
HELIX 22 AC4 SER H 127 THR H 134 1 8
HELIX 23 AC5 ALA H 194 GLN H 198 1 5
SHEET 1 AA1 8 GLU A 46 PRO A 47 0
SHEET 2 AA1 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 AA1 8 ARG A 21 VAL A 28 -1 N VAL A 28 O THR A 31
SHEET 4 AA1 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 AA1 8 THR A 94 VAL A 103 -1 O VAL A 103 N HIS A 3
SHEET 6 AA1 8 PHE A 109 TYR A 118 -1 O ARG A 111 N ASP A 102
SHEET 7 AA1 8 LYS A 121 LEU A 126 -1 O LEU A 126 N HIS A 114
SHEET 8 AA1 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 AA2 4 HIS A 188 ALA A 193 0
SHEET 2 AA2 4 GLU A 198 PHE A 208 -1 O ARG A 202 N THR A 190
SHEET 3 AA2 4 PHE A 241 PRO A 250 -1 O VAL A 249 N ALA A 199
SHEET 4 AA2 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 AA3 4 HIS A 188 ALA A 193 0
SHEET 2 AA3 4 GLU A 198 PHE A 208 -1 O ARG A 202 N THR A 190
SHEET 3 AA3 4 PHE A 241 PRO A 250 -1 O VAL A 249 N ALA A 199
SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 AA4 3 THR A 214 THR A 216 0
SHEET 2 AA4 3 CYS A 259 GLN A 262 -1 O GLN A 262 N THR A 214
SHEET 3 AA4 3 LEU A 270 LEU A 272 -1 O LEU A 270 N VAL A 261
SHEET 1 AA5 4 LYS 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 PHE B 70 N ASN B 21
SHEET 4 AA5 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 AA6 4 LYS 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 PHE B 70 N ASN B 21
SHEET 4 AA6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 AA7 4 GLU B 44 ARG B 45 0
SHEET 2 AA7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 AA7 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38
SHEET 4 AA7 4 LYS B 91 LYS B 94 -1 O VAL B 93 N CYS B 80
SHEET 1 AA8 8 GLU C 46 PRO C 47 0
SHEET 2 AA8 8 THR C 31 ASP C 37 -1 N ARG C 35 O GLU C 46
SHEET 3 AA8 8 ARG C 21 VAL C 28 -1 N VAL C 28 O THR C 31
SHEET 4 AA8 8 HIS C 3 VAL C 12 -1 N ARG C 6 O TYR C 27
SHEET 5 AA8 8 THR C 94 VAL C 103 -1 O VAL C 103 N HIS C 3
SHEET 6 AA8 8 PHE C 109 TYR C 118 -1 O LEU C 110 N ASP C 102
SHEET 7 AA8 8 LYS C 121 LEU C 126 -1 O ILE C 124 N TYR C 116
SHEET 8 AA8 8 TRP C 133 ALA C 135 -1 O THR C 134 N ALA C 125
SHEET 1 AA9 4 LYS C 186 ALA C 193 0
SHEET 2 AA9 4 GLU C 198 PHE C 208 -1 O TRP C 204 N HIS C 188
SHEET 3 AA9 4 PHE C 241 PRO C 250 -1 O LYS C 243 N ALA C 205
SHEET 4 AA9 4 THR C 228 LEU C 230 -1 N GLU C 229 O ALA C 246
SHEET 1 AB1 4 LYS C 186 ALA C 193 0
SHEET 2 AB1 4 GLU C 198 PHE C 208 -1 O TRP C 204 N HIS C 188
SHEET 3 AB1 4 PHE C 241 PRO C 250 -1 O LYS C 243 N ALA C 205
SHEET 4 AB1 4 ARG C 234 PRO C 235 -1 N ARG C 234 O GLN C 242
SHEET 1 AB2 4 GLU C 222 ASP C 223 0
SHEET 2 AB2 4 THR C 214 ARG C 219 -1 N ARG C 219 O GLU C 222
SHEET 3 AB2 4 TYR C 257 GLN C 262 -1 O HIS C 260 N THR C 216
SHEET 4 AB2 4 LEU C 270 LEU C 272 -1 O LEU C 272 N CYS C 259
SHEET 1 AB3 4 LYS D 6 SER D 11 0
SHEET 2 AB3 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB3 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 AB3 4 GLU D 50 HIS D 51 -1 N GLU D 50 O TYR D 67
SHEET 1 AB4 4 LYS D 6 SER D 11 0
SHEET 2 AB4 4 ASN D 21 PHE D 30 -1 O ASN D 24 N TYR D 10
SHEET 3 AB4 4 PHE D 62 PHE D 70 -1 O TYR D 66 N CYS D 25
SHEET 4 AB4 4 SER D 55 PHE D 56 -1 N SER D 55 O TYR D 63
SHEET 1 AB5 4 GLU D 44 ARG D 45 0
SHEET 2 AB5 4 GLU D 36 LYS D 41 -1 N LYS D 41 O GLU D 44
SHEET 3 AB5 4 TYR D 78 ASN D 83 -1 O ALA D 79 N LEU D 40
SHEET 4 AB5 4 LYS D 91 LYS D 94 -1 O VAL D 93 N CYS D 80
SHEET 1 AB6 5 GLU E 6 SER E 8 0
SHEET 2 AB6 5 LEU E 20 ASN E 25 -1 O TYR E 23 N SER E 8
SHEET 3 AB6 5 ASP E 72 ILE E 77 -1 O LEU E 75 N VAL E 22
SHEET 4 AB6 5 LEU E 62 PHE E 66 -1 N THR E 63 O HIS E 76
SHEET 5 AB6 5 VAL E 56 LEU E 59 -1 N LYS E 57 O PHE E 64
SHEET 1 AB7 5 PHE E 11 GLN E 15 0
SHEET 2 AB7 5 THR E 108 LYS E 113 1 O SER E 111 N ILE E 14
SHEET 3 AB7 5 GLY E 86 ILE E 94 -1 N TYR E 88 O THR E 108
SHEET 4 AB7 5 PHE E 30 GLN E 38 -1 N GLN E 34 O ALA E 91
SHEET 5 AB7 5 VAL E 45 VAL E 50 -1 O VAL E 45 N ARG E 37
SHEET 1 AB8 4 PHE E 11 GLN E 15 0
SHEET 2 AB8 4 THR E 108 LYS E 113 1 O SER E 111 N ILE E 14
SHEET 3 AB8 4 GLY E 86 ILE E 94 -1 N TYR E 88 O THR E 108
SHEET 4 AB8 4 ILE E 103 PHE E 104 -1 O ILE E 103 N GLY E 92
SHEET 1 AB9 4 ALA E 122 ARG E 127 0
SHEET 2 AB9 4 SER E 135 THR E 140 -1 O LEU E 138 N TYR E 124
SHEET 3 AB9 4 PHE E 171 SER E 180 -1 O ALA E 178 N CYS E 137
SHEET 4 AB9 4 VAL E 156 ILE E 158 -1 N TYR E 157 O TRP E 179
SHEET 1 AC1 4 ALA E 122 ARG E 127 0
SHEET 2 AC1 4 SER E 135 THR E 140 -1 O LEU E 138 N TYR E 124
SHEET 3 AC1 4 PHE E 171 SER E 180 -1 O ALA E 178 N CYS E 137
SHEET 4 AC1 4 CYS E 162 MET E 166 -1 N LEU E 164 O SER E 173
SHEET 1 AC2 2 ILE F 2 THR F 3 0
SHEET 2 AC2 2 GLU F 22 GLN F 23 -1 O GLU F 22 N THR F 3
SHEET 1 AC3 6 TYR F 8 LYS F 12 0
SHEET 2 AC3 6 THR F 105 THR F 110 1 O THR F 108 N LEU F 9
SHEET 3 AC3 6 ALA F 85 SER F 92 -1 N TYR F 87 O THR F 105
SHEET 4 AC3 6 ALA F 29 GLN F 35 -1 N TYR F 33 O LEU F 88
SHEET 5 AC3 6 ARG F 42 ILE F 49 -1 O SER F 47 N MET F 30
SHEET 6 AC3 6 ASP F 52 LYS F 55 -1 O GLN F 54 N TYR F 46
SHEET 1 AC4 4 TYR F 8 LYS F 12 0
SHEET 2 AC4 4 THR F 105 THR F 110 1 O THR F 108 N LEU F 9
SHEET 3 AC4 4 ALA F 85 SER F 92 -1 N TYR F 87 O THR F 105
SHEET 4 AC4 4 TYR F 100 PHE F 101 -1 O TYR F 100 N SER F 91
SHEET 1 AC5 3 VAL F 17 LEU F 19 0
SHEET 2 AC5 3 LEU F 74 VAL F 76 -1 O LEU F 74 N LEU F 19
SHEET 3 AC5 3 TYR F 62 VAL F 64 -1 N SER F 63 O THR F 75
SHEET 1 AC6 4 GLU F 120 PHE F 124 0
SHEET 2 AC6 4 LYS F 136 PHE F 146 -1 O VAL F 140 N PHE F 124
SHEET 3 AC6 4 TYR F 184 SER F 193 -1 O VAL F 192 N ALA F 137
SHEET 4 AC6 4 VAL F 166 THR F 168 -1 N CYS F 167 O ARG F 189
SHEET 1 AC7 4 GLU F 120 PHE F 124 0
SHEET 2 AC7 4 LYS F 136 PHE F 146 -1 O VAL F 140 N PHE F 124
SHEET 3 AC7 4 TYR F 184 SER F 193 -1 O VAL F 192 N ALA F 137
SHEET 4 AC7 4 LEU F 173 LYS F 174 -1 N LEU F 173 O SER F 185
SHEET 1 AC8 4 LYS F 160 VAL F 162 0
SHEET 2 AC8 4 VAL F 151 VAL F 157 -1 N VAL F 157 O LYS F 160
SHEET 3 AC8 4 HIS F 203 PHE F 210 -1 O ARG F 205 N TRP F 156
SHEET 4 AC8 4 GLN F 229 TRP F 236 -1 O GLN F 229 N PHE F 210
SHEET 1 AC9 5 GLU G 6 SER G 8 0
SHEET 2 AC9 5 LEU G 20 ASN G 25 -1 O TYR G 23 N SER G 8
SHEET 3 AC9 5 ASP G 72 ILE G 77 -1 O LEU G 75 N VAL G 22
SHEET 4 AC9 5 LEU G 62 PHE G 66 -1 N THR G 63 O HIS G 76
SHEET 5 AC9 5 VAL G 56 LEU G 59 -1 N LYS G 57 O PHE G 64
SHEET 1 AD1 5 PHE G 11 GLN G 15 0
SHEET 2 AD1 5 THR G 108 LYS G 113 1 O SER G 111 N ILE G 14
SHEET 3 AD1 5 GLY G 86 ILE G 94 -1 N GLY G 86 O LEU G 110
SHEET 4 AD1 5 PHE G 30 GLN G 38 -1 N TYR G 36 O LEU G 89
SHEET 5 AD1 5 VAL G 45 VAL G 50 -1 O LEU G 47 N TRP G 35
SHEET 1 AD2 4 PHE G 11 GLN G 15 0
SHEET 2 AD2 4 THR G 108 LYS G 113 1 O SER G 111 N ILE G 14
SHEET 3 AD2 4 GLY G 86 ILE G 94 -1 N GLY G 86 O LEU G 110
SHEET 4 AD2 4 ILE G 103 PHE G 104 -1 O ILE G 103 N GLY G 92
SHEET 1 AD3 8 TYR G 157 ILE G 158 0
SHEET 2 AD3 8 PHE G 171 TRP G 179 -1 O TRP G 179 N TYR G 157
SHEET 3 AD3 8 SER G 135 THR G 140 -1 N PHE G 139 O ALA G 176
SHEET 4 AD3 8 ALA G 122 ASP G 128 -1 N TYR G 124 O LEU G 138
SHEET 5 AD3 8 GLU H 120 GLU H 125 -1 O GLU H 125 N ARG G 127
SHEET 6 AD3 8 LYS H 136 PHE H 146 -1 O VAL H 140 N PHE H 124
SHEET 7 AD3 8 TYR H 184 SER H 193 -1 O SER H 188 N CYS H 141
SHEET 8 AD3 8 VAL H 166 THR H 168 -1 N CYS H 167 O ARG H 189
SHEET 1 AD4 8 CYS G 162 MET G 166 0
SHEET 2 AD4 8 PHE G 171 TRP G 179 -1 O PHE G 171 N MET G 166
SHEET 3 AD4 8 SER G 135 THR G 140 -1 N PHE G 139 O ALA G 176
SHEET 4 AD4 8 ALA G 122 ASP G 128 -1 N TYR G 124 O LEU G 138
SHEET 5 AD4 8 GLU H 120 GLU H 125 -1 O GLU H 125 N ARG G 127
SHEET 6 AD4 8 LYS H 136 PHE H 146 -1 O VAL H 140 N PHE H 124
SHEET 7 AD4 8 TYR H 184 SER H 193 -1 O SER H 188 N CYS H 141
SHEET 8 AD4 8 LEU H 173 LYS H 174 -1 N LEU H 173 O SER H 185
SHEET 1 AD5 4 ILE H 2 SER H 5 0
SHEET 2 AD5 4 VAL H 17 GLN H 23 -1 O GLU H 22 N THR H 3
SHEET 3 AD5 4 LEU H 74 VAL H 76 -1 O LEU H 74 N LEU H 19
SHEET 4 AD5 4 TYR H 62 VAL H 64 -1 N SER H 63 O THR H 75
SHEET 1 AD6 6 TYR H 8 LYS H 12 0
SHEET 2 AD6 6 THR H 105 THR H 110 1 O ARG H 106 N LEU H 9
SHEET 3 AD6 6 ALA H 85 SER H 92 -1 N TYR H 87 O THR H 105
SHEET 4 AD6 6 ALA H 29 GLN H 35 -1 N TYR H 33 O LEU H 88
SHEET 5 AD6 6 LEU H 41 SER H 47 -1 O ILE H 44 N TRP H 32
SHEET 6 AD6 6 GLN H 54 LYS H 55 -1 O GLN H 54 N TYR H 46
SHEET 1 AD7 4 TYR H 8 LYS H 12 0
SHEET 2 AD7 4 THR H 105 THR H 110 1 O ARG H 106 N LEU H 9
SHEET 3 AD7 4 ALA H 85 SER H 92 -1 N TYR H 87 O THR H 105
SHEET 4 AD7 4 TYR H 100 PHE H 101 -1 O TYR H 100 N SER H 91
SHEET 1 AD8 4 LYS H 160 VAL H 162 0
SHEET 2 AD8 4 VAL H 151 VAL H 157 -1 N TRP H 155 O VAL H 162
SHEET 3 AD8 4 HIS H 203 PHE H 210 -1 O GLN H 207 N SER H 154
SHEET 4 AD8 4 GLN H 229 TRP H 236 -1 O ALA H 235 N PHE H 204
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.05
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.04
SSBOND 4 CYS C 101 CYS C 164 1555 1555 2.07
SSBOND 5 CYS C 203 CYS C 259 1555 1555 2.04
SSBOND 6 CYS D 25 CYS D 80 1555 1555 2.03
SSBOND 7 CYS E 24 CYS E 90 1555 1555 2.04
SSBOND 8 CYS E 137 CYS E 187 1555 1555 2.03
SSBOND 9 CYS E 162 CYS F 167 1555 1555 1.97
SSBOND 10 CYS F 21 CYS F 89 1555 1555 2.03
SSBOND 11 CYS F 141 CYS F 206 1555 1555 2.02
SSBOND 12 CYS G 24 CYS G 90 1555 1555 2.03
SSBOND 13 CYS G 137 CYS G 187 1555 1555 2.04
SSBOND 14 CYS G 162 CYS H 167 1555 1555 2.03
SSBOND 15 CYS H 21 CYS H 89 1555 1555 2.03
SSBOND 16 CYS H 141 CYS H 206 1555 1555 2.01
LINK NE2 HIS A 192 OD2 ASP B 98 1555 1555 1.27
LINK NZ LYS G 134 OD1 ASN G 181 1555 1555 1.25
CISPEP 1 TYR A 209 PRO A 210 0 1.85
CISPEP 2 HIS B 31 PRO B 32 0 -0.09
CISPEP 3 TYR C 209 PRO C 210 0 2.55
CISPEP 4 HIS D 31 PRO D 32 0 5.74
CISPEP 5 SER E 8 PRO E 9 0 -10.01
CISPEP 6 SER F 5 PRO F 6 0 -4.07
CISPEP 7 TYR F 147 PRO F 148 0 2.11
CISPEP 8 SER G 8 PRO G 9 0 -1.30
CISPEP 9 SER H 5 PRO H 6 0 -8.38
CISPEP 10 TYR H 147 PRO H 148 0 -1.53
CISPEP 11 PRO H 200 ARG H 201 0 2.24
SITE 1 AC1 2 GLU C 166 TRP C 167
SITE 1 AC2 4 GLN G 38 GLN H 35 GLN H 39 GLY H 40
CRYST1 134.744 54.082 149.296 90.00 116.61 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 0.007421 0.000000 0.003718 0.00000
SCALE2 0.000000 0.018490 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007492 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
