HEADER OXIDOREDUCTASE 10-JUL-15 5CHE
TITLE CRYSTAL STRUCTURE OF ARABIDOPSIS GLUTAMYL-TRNA REDUCTASE IN COMPLEX
TITLE 2 WITH ITS REGULATORY PROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 73-543;
COMPND 5 SYNONYM: GLUTR;
COMPND 6 EC: 1.2.1.70;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: GLUTAMYL-TRNA REDUCTASE-BINDING PROTEIN, CHLOROPLASTIC;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: UNP RESIDUES 42-317;
COMPND 12 SYNONYM: GLUTR-BINDING PROTEIN,PROTEIN PROTON GRADIENT REGULATION 7;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: PROTEIN FLUORESCENT IN BLUE LIGHT, CHLOROPLASTIC;
COMPND 16 CHAIN: E, F;
COMPND 17 FRAGMENT: UNP RESIDUES 195-316;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: HEMA1, HEMA, AT1G58290, F19C14.9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 10 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 11 ORGANISM_TAXID: 3702;
SOURCE 12 GENE: GLUTRBP, PGR7, AT3G21200, MXL8.5;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 17 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 18 ORGANISM_TAXID: 3702;
SOURCE 19 GENE: FLU, AT3G14110, MAG2.7;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLUTR, TERTIARY COMPLEX, REGULATORY PROTEINS, ANCHOR PROTEIN,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.FANG,L.LIU
REVDAT 3 08-NOV-23 5CHE 1 REMARK
REVDAT 2 27-SEP-17 5CHE 1 REMARK
REVDAT 1 03-FEB-16 5CHE 0
JRNL AUTH Y.FANG,S.ZHAO,F.ZHANG,A.ZHAO,W.ZHANG,M.ZHANG,L.LIU
JRNL TITL THE ARABIDOPSIS GLUTAMYL-TRNA REDUCTASE (GLUTR) FORMS A
JRNL TITL 2 TERNARY COMPLEX WITH FLU AND GLUTR-BINDING PROTEIN
JRNL REF SCI REP V. 6 19756 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 26794057
JRNL DOI 10.1038/SREP19756
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.2
REMARK 3 NUMBER OF REFLECTIONS : 32428
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1632
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 39.2682 - 7.3182 0.95 2935 188 0.1733 0.2204
REMARK 3 2 7.3182 - 5.8147 0.99 2947 169 0.2259 0.2771
REMARK 3 3 5.8147 - 5.0814 1.00 2953 150 0.2288 0.2555
REMARK 3 4 5.0814 - 4.6176 1.00 2921 176 0.1954 0.2687
REMARK 3 5 4.6176 - 4.2871 1.00 2943 133 0.2043 0.2627
REMARK 3 6 4.2871 - 4.0346 1.00 2909 149 0.2187 0.2941
REMARK 3 7 4.0346 - 3.8327 1.00 2877 161 0.2482 0.3073
REMARK 3 8 3.8327 - 3.6660 0.97 2887 125 0.2555 0.3569
REMARK 3 9 3.6660 - 3.5250 0.83 2433 110 0.2574 0.2640
REMARK 3 10 3.5250 - 3.4034 0.72 2119 103 0.2836 0.3701
REMARK 3 11 3.4034 - 3.2970 0.59 1696 95 0.2854 0.3400
REMARK 3 12 3.2970 - 3.2028 0.41 1176 73 0.2898 0.3798
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.75
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 : 0.006 12561
REMARK 3 ANGLE : 0.975 16948
REMARK 3 CHIRALITY : 0.062 1941
REMARK 3 PLANARITY : 0.004 2178
REMARK 3 DIHEDRAL : 10.720 4741
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 5CHE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-325
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36775
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.83100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4N7R, 4YVQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM MALONATE, LICL, MPD,
REMARK 280 PH 7.0, EVAPORATION, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 108.49700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.60550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 108.49700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.60550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 72
REMARK 465 ALA A 73
REMARK 465 ALA A 74
REMARK 465 SER A 75
REMARK 465 ILE A 76
REMARK 465 SER A 77
REMARK 465 ALA A 78
REMARK 465 LEU A 79
REMARK 465 GLU A 80
REMARK 465 GLN A 81
REMARK 465 LEU A 82
REMARK 465 LYS A 83
REMARK 465 ASN A 84
REMARK 465 SER A 85
REMARK 465 ALA A 86
REMARK 465 ALA A 87
REMARK 465 ASP A 88
REMARK 465 ARG A 89
REMARK 465 TYR A 90
REMARK 465 THR A 91
REMARK 465 LYS A 92
REMARK 465 GLU A 93
REMARK 465 ALA A 409
REMARK 465 ALA A 410
REMARK 465 ASN A 411
REMARK 465 LYS A 412
REMARK 465 GLY A 469
REMARK 465 ASP A 470
REMARK 465 ASP A 471
REMARK 465 ASP A 528
REMARK 465 ILE A 529
REMARK 465 LEU A 530
REMARK 465 GLU A 531
REMARK 465 GLU A 532
REMARK 465 LYS A 533
REMARK 465 LEU A 534
REMARK 465 LYS A 535
REMARK 465 ALA A 536
REMARK 465 MET A 537
REMARK 465 ALA A 538
REMARK 465 GLU A 539
REMARK 465 GLN A 540
REMARK 465 GLN A 541
REMARK 465 GLN A 542
REMARK 465 LYS A 543
REMARK 465 SER B 72
REMARK 465 ALA B 73
REMARK 465 ALA B 74
REMARK 465 SER B 75
REMARK 465 ILE B 76
REMARK 465 SER B 77
REMARK 465 ALA B 78
REMARK 465 LEU B 79
REMARK 465 GLU B 80
REMARK 465 GLN B 81
REMARK 465 LEU B 82
REMARK 465 LYS B 83
REMARK 465 ASN B 84
REMARK 465 SER B 85
REMARK 465 ALA B 86
REMARK 465 ALA B 87
REMARK 465 ASP B 88
REMARK 465 ARG B 89
REMARK 465 TYR B 90
REMARK 465 THR B 91
REMARK 465 LYS B 92
REMARK 465 GLU B 93
REMARK 465 VAL B 225
REMARK 465 ASN B 226
REMARK 465 GLY B 227
REMARK 465 SER B 274
REMARK 465 SER B 275
REMARK 465 ASN B 276
REMARK 465 GLU B 352
REMARK 465 ALA B 410
REMARK 465 ASN B 411
REMARK 465 GLY B 469
REMARK 465 ASP B 470
REMARK 465 ASP B 528
REMARK 465 ILE B 529
REMARK 465 LEU B 530
REMARK 465 GLU B 531
REMARK 465 GLU B 532
REMARK 465 LYS B 533
REMARK 465 LEU B 534
REMARK 465 LYS B 535
REMARK 465 ALA B 536
REMARK 465 MET B 537
REMARK 465 ALA B 538
REMARK 465 GLU B 539
REMARK 465 GLN B 540
REMARK 465 GLN B 541
REMARK 465 GLN B 542
REMARK 465 LYS B 543
REMARK 465 MET C 8
REMARK 465 GLY C 9
REMARK 465 SER C 10
REMARK 465 SER C 11
REMARK 465 HIS C 12
REMARK 465 HIS C 13
REMARK 465 HIS C 14
REMARK 465 HIS C 15
REMARK 465 HIS C 16
REMARK 465 HIS C 17
REMARK 465 SER C 18
REMARK 465 SER C 19
REMARK 465 GLY C 20
REMARK 465 LEU C 21
REMARK 465 VAL C 22
REMARK 465 PRO C 23
REMARK 465 ARG C 24
REMARK 465 GLY C 25
REMARK 465 SER C 26
REMARK 465 HIS C 27
REMARK 465 MET C 28
REMARK 465 ALA C 29
REMARK 465 SER C 30
REMARK 465 MET C 31
REMARK 465 THR C 32
REMARK 465 GLY C 33
REMARK 465 GLY C 34
REMARK 465 GLN C 35
REMARK 465 GLN C 36
REMARK 465 MET C 37
REMARK 465 GLY C 38
REMARK 465 ARG C 39
REMARK 465 GLY C 40
REMARK 465 SER C 41
REMARK 465 CYS C 42
REMARK 465 SER C 43
REMARK 465 VAL C 44
REMARK 465 SER C 45
REMARK 465 THR C 46
REMARK 465 THR C 47
REMARK 465 LEU C 48
REMARK 465 ASP C 49
REMARK 465 THR C 50
REMARK 465 PRO C 51
REMARK 465 ALA C 52
REMARK 465 THR C 53
REMARK 465 ALA C 54
REMARK 465 SER C 55
REMARK 465 VAL C 306
REMARK 465 GLY C 307
REMARK 465 SER C 308
REMARK 465 SER C 309
REMARK 465 HIS C 310
REMARK 465 SER C 311
REMARK 465 HIS C 312
REMARK 465 LYS C 313
REMARK 465 GLY C 314
REMARK 465 GLY C 315
REMARK 465 GLY C 316
REMARK 465 GLN C 317
REMARK 465 MET D 8
REMARK 465 GLY D 9
REMARK 465 SER D 10
REMARK 465 SER D 11
REMARK 465 HIS D 12
REMARK 465 HIS D 13
REMARK 465 HIS D 14
REMARK 465 HIS D 15
REMARK 465 HIS D 16
REMARK 465 HIS D 17
REMARK 465 SER D 18
REMARK 465 SER D 19
REMARK 465 GLY D 20
REMARK 465 LEU D 21
REMARK 465 VAL D 22
REMARK 465 PRO D 23
REMARK 465 ARG D 24
REMARK 465 GLY D 25
REMARK 465 SER D 26
REMARK 465 HIS D 27
REMARK 465 MET D 28
REMARK 465 ALA D 29
REMARK 465 SER D 30
REMARK 465 MET D 31
REMARK 465 THR D 32
REMARK 465 GLY D 33
REMARK 465 GLY D 34
REMARK 465 GLN D 35
REMARK 465 GLN D 36
REMARK 465 MET D 37
REMARK 465 GLY D 38
REMARK 465 ARG D 39
REMARK 465 GLY D 40
REMARK 465 SER D 41
REMARK 465 CYS D 42
REMARK 465 SER D 43
REMARK 465 VAL D 44
REMARK 465 SER D 45
REMARK 465 THR D 46
REMARK 465 THR D 47
REMARK 465 LEU D 48
REMARK 465 ASP D 49
REMARK 465 THR D 50
REMARK 465 PRO D 51
REMARK 465 ALA D 52
REMARK 465 THR D 53
REMARK 465 ALA D 54
REMARK 465 SER D 55
REMARK 465 PRO D 140
REMARK 465 GLY D 141
REMARK 465 SER D 308
REMARK 465 SER D 309
REMARK 465 HIS D 310
REMARK 465 SER D 311
REMARK 465 HIS D 312
REMARK 465 LYS D 313
REMARK 465 GLY D 314
REMARK 465 GLY D 315
REMARK 465 GLY D 316
REMARK 465 GLN D 317
REMARK 465 MET E 159
REMARK 465 LYS E 160
REMARK 465 TYR E 161
REMARK 465 LEU E 162
REMARK 465 LEU E 163
REMARK 465 PRO E 164
REMARK 465 THR E 165
REMARK 465 ALA E 166
REMARK 465 ALA E 167
REMARK 465 ALA E 168
REMARK 465 GLY E 169
REMARK 465 LEU E 170
REMARK 465 LEU E 171
REMARK 465 LEU E 172
REMARK 465 LEU E 173
REMARK 465 ALA E 174
REMARK 465 ALA E 175
REMARK 465 GLN E 176
REMARK 465 PRO E 177
REMARK 465 ALA E 178
REMARK 465 MET E 179
REMARK 465 ALA E 180
REMARK 465 MET E 181
REMARK 465 ASP E 182
REMARK 465 ILE E 183
REMARK 465 GLY E 184
REMARK 465 ILE E 185
REMARK 465 ASN E 186
REMARK 465 SER E 187
REMARK 465 ASP E 188
REMARK 465 PRO E 189
REMARK 465 HIS E 190
REMARK 465 HIS E 191
REMARK 465 HIS E 192
REMARK 465 HIS E 193
REMARK 465 HIS E 194
REMARK 465 HIS E 195
REMARK 465 ILE E 196
REMARK 465 VAL E 197
REMARK 465 ASP E 317
REMARK 465 MET F 159
REMARK 465 LYS F 160
REMARK 465 TYR F 161
REMARK 465 LEU F 162
REMARK 465 LEU F 163
REMARK 465 PRO F 164
REMARK 465 THR F 165
REMARK 465 ALA F 166
REMARK 465 ALA F 167
REMARK 465 ALA F 168
REMARK 465 GLY F 169
REMARK 465 LEU F 170
REMARK 465 LEU F 171
REMARK 465 LEU F 172
REMARK 465 LEU F 173
REMARK 465 ALA F 174
REMARK 465 ALA F 175
REMARK 465 GLN F 176
REMARK 465 PRO F 177
REMARK 465 ALA F 178
REMARK 465 MET F 179
REMARK 465 ALA F 180
REMARK 465 MET F 181
REMARK 465 ASP F 182
REMARK 465 ILE F 183
REMARK 465 GLY F 184
REMARK 465 ILE F 185
REMARK 465 ASN F 186
REMARK 465 SER F 187
REMARK 465 ASP F 188
REMARK 465 PRO F 189
REMARK 465 HIS F 190
REMARK 465 HIS F 191
REMARK 465 HIS F 192
REMARK 465 HIS F 193
REMARK 465 HIS F 194
REMARK 465 HIS F 195
REMARK 465 ILE F 196
REMARK 465 VAL F 197
REMARK 465 GLU F 198
REMARK 465 PRO F 199
REMARK 465 ASP F 317
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 ASP A 502 CG OD1 OD2
REMARK 470 ASP A 505 CG OD1 OD2
REMARK 470 LYS A 527 CG CD CE NZ
REMARK 470 GLU B 208 CG CD OE1 OE2
REMARK 470 SER B 254 OG
REMARK 470 LYS B 300 CG CD CE NZ
REMARK 470 SER B 381 OG
REMARK 470 GLU B 406 CG CD OE1 OE2
REMARK 470 VAL B 407 CG1 CG2
REMARK 470 GLU B 462 CG CD OE1 OE2
REMARK 470 ASP B 502 CG OD1 OD2
REMARK 470 GLU B 526 CG CD OE1 OE2
REMARK 470 SER C 108 OG
REMARK 470 ARG C 148 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 182 CG CD OE1 OE2
REMARK 470 GLN F 202 CG CD OE1 NE2
REMARK 470 GLU F 203 CG CD OE1 OE2
REMARK 470 GLU F 242 CG CD OE1 OE2
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 CYS A 130 O HOH A 601 2.15
REMARK 500 OD1 ASP E 292 OH TYR E 307 2.18
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 TYR A 186 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 ASP A 502 N - CA - C ANGL. DEV. = -24.0 DEGREES
REMARK 500 ASN B 187 CB - CA - C ANGL. DEV. = 20.0 DEGREES
REMARK 500 LYS B 188 N - CA - CB ANGL. DEV. = -15.5 DEGREES
REMARK 500 PRO D 111 C - N - CA ANGL. DEV. = 11.1 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 ASN A 187 -89.33 -154.59
REMARK 500 GLN A 273 -1.90 -58.79
REMARK 500 SER A 275 70.02 73.23
REMARK 500 VAL A 407 25.76 48.59
REMARK 500 ASN A 473 -87.59 -153.50
REMARK 500 LYS A 474 -117.92 50.88
REMARK 500 SER A 504 -138.11 50.28
REMARK 500 ASP A 505 60.61 60.43
REMARK 500 SER A 506 -26.09 -38.93
REMARK 500 ALA B 116 99.37 -69.86
REMARK 500 ASN B 187 -117.43 55.66
REMARK 500 SER B 203 -169.92 51.01
REMARK 500 ASN B 251 44.78 -79.35
REMARK 500 SER B 278 -154.91 63.65
REMARK 500 ALA B 279 33.86 70.39
REMARK 500 GLU B 413 -81.02 -156.84
REMARK 500 SER B 504 -121.85 -107.23
REMARK 500 ASP B 505 110.31 56.23
REMARK 500 LEU C 126 -45.13 -131.35
REMARK 500 ASP C 143 -153.37 -138.12
REMARK 500 CYS D 124 19.07 57.15
REMARK 500 GLN E 218 45.68 -93.29
REMARK 500 GLN F 218 51.70 34.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5CHE A 73 543 UNP P42804 HEM11_ARATH 73 543
DBREF 5CHE B 73 543 UNP P42804 HEM11_ARATH 73 543
DBREF 5CHE C 42 317 UNP Q9LU39 GLUBP_ARATH 42 317
DBREF 5CHE D 42 317 UNP Q9LU39 GLUBP_ARATH 42 317
DBREF 5CHE E 196 317 UNP Q940U6 FLU_ARATH 195 316
DBREF 5CHE F 196 317 UNP Q940U6 FLU_ARATH 195 316
SEQADV 5CHE SER A 72 UNP P42804 EXPRESSION TAG
SEQADV 5CHE SER B 72 UNP P42804 EXPRESSION TAG
SEQADV 5CHE MET C 8 UNP Q9LU39 INITIATING METHIONINE
SEQADV 5CHE GLY C 9 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 10 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 11 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 12 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 13 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 14 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 15 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 16 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 17 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 18 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 19 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY C 20 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE LEU C 21 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE VAL C 22 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE PRO C 23 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE ARG C 24 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY C 25 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 26 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS C 27 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET C 28 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE ALA C 29 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 30 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET C 31 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE THR C 32 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY C 33 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY C 34 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLN C 35 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLN C 36 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET C 37 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY C 38 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE ARG C 39 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY C 40 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER C 41 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET D 8 UNP Q9LU39 INITIATING METHIONINE
SEQADV 5CHE GLY D 9 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 10 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 11 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 12 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 13 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 14 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 15 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 16 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 17 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 18 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 19 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY D 20 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE LEU D 21 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE VAL D 22 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE PRO D 23 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE ARG D 24 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY D 25 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 26 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE HIS D 27 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET D 28 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE ALA D 29 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 30 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET D 31 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE THR D 32 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY D 33 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY D 34 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLN D 35 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLN D 36 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET D 37 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY D 38 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE ARG D 39 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE GLY D 40 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE SER D 41 UNP Q9LU39 EXPRESSION TAG
SEQADV 5CHE MET E 159 UNP Q940U6 INITIATING METHIONINE
SEQADV 5CHE LYS E 160 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE TYR E 161 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU E 162 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU E 163 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE PRO E 164 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE THR E 165 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 166 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 167 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 168 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE GLY E 169 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU E 170 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU E 171 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU E 172 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU E 173 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 174 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 175 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE GLN E 176 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE PRO E 177 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 178 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE MET E 179 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA E 180 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE MET E 181 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ASP E 182 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ILE E 183 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE GLY E 184 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ILE E 185 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ASN E 186 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE SER E 187 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ASP E 188 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE PRO E 189 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS E 190 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS E 191 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS E 192 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS E 193 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS E 194 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS E 195 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE MET F 159 UNP Q940U6 INITIATING METHIONINE
SEQADV 5CHE LYS F 160 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE TYR F 161 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU F 162 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU F 163 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE PRO F 164 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE THR F 165 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 166 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 167 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 168 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE GLY F 169 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU F 170 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU F 171 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU F 172 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE LEU F 173 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 174 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 175 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE GLN F 176 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE PRO F 177 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 178 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE MET F 179 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ALA F 180 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE MET F 181 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ASP F 182 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ILE F 183 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE GLY F 184 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ILE F 185 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ASN F 186 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE SER F 187 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE ASP F 188 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE PRO F 189 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS F 190 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS F 191 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS F 192 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS F 193 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS F 194 UNP Q940U6 EXPRESSION TAG
SEQADV 5CHE HIS F 195 UNP Q940U6 EXPRESSION TAG
SEQRES 1 A 472 SER ALA ALA SER ILE SER ALA LEU GLU GLN LEU LYS ASN
SEQRES 2 A 472 SER ALA ALA ASP ARG TYR THR LYS GLU ARG SER SER ILE
SEQRES 3 A 472 VAL VAL ILE GLY LEU SER ILE HIS THR ALA PRO VAL GLU
SEQRES 4 A 472 MET ARG GLU LYS LEU ALA ILE PRO GLU ALA GLU TRP PRO
SEQRES 5 A 472 ARG ALA ILE ALA GLU LEU CYS GLY LEU ASN HIS ILE GLU
SEQRES 6 A 472 GLU ALA ALA VAL LEU SER THR CYS ASN ARG MET GLU ILE
SEQRES 7 A 472 TYR VAL LEU ALA LEU SER GLN HIS ARG GLY VAL LYS GLU
SEQRES 8 A 472 VAL THR GLU TRP MET SER LYS THR SER GLY ILE PRO VAL
SEQRES 9 A 472 SER GLU ILE CYS GLN HIS ARG PHE LEU LEU TYR ASN LYS
SEQRES 10 A 472 ASP ALA THR GLN HIS ILE PHE GLU VAL SER ALA GLY LEU
SEQRES 11 A 472 ASP SER LEU VAL LEU GLY GLU GLY GLN ILE LEU ALA GLN
SEQRES 12 A 472 VAL LYS GLN VAL VAL LYS VAL GLY GLN GLY VAL ASN GLY
SEQRES 13 A 472 PHE GLY ARG ASN ILE SER GLY LEU PHE LYS HIS ALA ILE
SEQRES 14 A 472 THR VAL GLY LYS ARG VAL ARG THR GLU THR ASN ILE ALA
SEQRES 15 A 472 SER GLY ALA VAL SER VAL SER SER ALA ALA VAL GLU LEU
SEQRES 16 A 472 ALA LEU MET LYS LEU PRO GLN SER SER ASN VAL SER ALA
SEQRES 17 A 472 ARG MET CYS VAL ILE GLY ALA GLY LYS MET GLY LYS LEU
SEQRES 18 A 472 VAL ILE LYS HIS LEU MET ALA LYS GLY CYS THR LYS VAL
SEQRES 19 A 472 VAL VAL VAL ASN ARG SER GLU GLU ARG VAL SER ALA ILE
SEQRES 20 A 472 ARG GLU GLU MET PRO GLY ILE GLU ILE ILE TYR ARG PRO
SEQRES 21 A 472 LEU ASP GLU MET LEU ALA CYS ALA SER GLU ALA ASP VAL
SEQRES 22 A 472 VAL PHE THR SER THR ALA SER GLU THR PRO LEU PHE LEU
SEQRES 23 A 472 LYS GLU HIS VAL GLU ASN LEU PRO GLN ALA SER PRO GLU
SEQRES 24 A 472 VAL GLY GLY LEU ARG HIS PHE VAL ASP ILE SER VAL PRO
SEQRES 25 A 472 ARG ASN VAL GLY SER CYS VAL GLY GLU VAL GLU THR ALA
SEQRES 26 A 472 ARG VAL TYR ASN VAL ASP ASP LEU LYS GLU VAL VAL ALA
SEQRES 27 A 472 ALA ASN LYS GLU ASP ARG MET ARG LYS ALA MET GLU ALA
SEQRES 28 A 472 GLN THR ILE ILE THR GLU GLU SER THR GLN PHE GLU ALA
SEQRES 29 A 472 TRP ARG ASP SER LEU GLU THR VAL PRO THR ILE LYS LYS
SEQRES 30 A 472 LEU ARG ALA TYR ALA GLU ARG ILE ARG VAL ALA GLU LEU
SEQRES 31 A 472 GLU LYS CYS MET SER LYS MET GLY ASP ASP ILE ASN LYS
SEQRES 32 A 472 LYS THR THR ARG ALA VAL ASP ASP LEU SER ARG GLY ILE
SEQRES 33 A 472 VAL ASN ARG PHE LEU HIS GLY PRO MET GLN HIS LEU ARG
SEQRES 34 A 472 CYS ASP GLY SER ASP SER ARG THR LEU SER GLU THR LEU
SEQRES 35 A 472 GLU ASN MET HIS ALA LEU ASN ARG MET TYR GLY LEU GLU
SEQRES 36 A 472 LYS ASP ILE LEU GLU GLU LYS LEU LYS ALA MET ALA GLU
SEQRES 37 A 472 GLN GLN GLN LYS
SEQRES 1 B 472 SER ALA ALA SER ILE SER ALA LEU GLU GLN LEU LYS ASN
SEQRES 2 B 472 SER ALA ALA ASP ARG TYR THR LYS GLU ARG SER SER ILE
SEQRES 3 B 472 VAL VAL ILE GLY LEU SER ILE HIS THR ALA PRO VAL GLU
SEQRES 4 B 472 MET ARG GLU LYS LEU ALA ILE PRO GLU ALA GLU TRP PRO
SEQRES 5 B 472 ARG ALA ILE ALA GLU LEU CYS GLY LEU ASN HIS ILE GLU
SEQRES 6 B 472 GLU ALA ALA VAL LEU SER THR CYS ASN ARG MET GLU ILE
SEQRES 7 B 472 TYR VAL LEU ALA LEU SER GLN HIS ARG GLY VAL LYS GLU
SEQRES 8 B 472 VAL THR GLU TRP MET SER LYS THR SER GLY ILE PRO VAL
SEQRES 9 B 472 SER GLU ILE CYS GLN HIS ARG PHE LEU LEU TYR ASN LYS
SEQRES 10 B 472 ASP ALA THR GLN HIS ILE PHE GLU VAL SER ALA GLY LEU
SEQRES 11 B 472 ASP SER LEU VAL LEU GLY GLU GLY GLN ILE LEU ALA GLN
SEQRES 12 B 472 VAL LYS GLN VAL VAL LYS VAL GLY GLN GLY VAL ASN GLY
SEQRES 13 B 472 PHE GLY ARG ASN ILE SER GLY LEU PHE LYS HIS ALA ILE
SEQRES 14 B 472 THR VAL GLY LYS ARG VAL ARG THR GLU THR ASN ILE ALA
SEQRES 15 B 472 SER GLY ALA VAL SER VAL SER SER ALA ALA VAL GLU LEU
SEQRES 16 B 472 ALA LEU MET LYS LEU PRO GLN SER SER ASN VAL SER ALA
SEQRES 17 B 472 ARG MET CYS VAL ILE GLY ALA GLY LYS MET GLY LYS LEU
SEQRES 18 B 472 VAL ILE LYS HIS LEU MET ALA LYS GLY CYS THR LYS VAL
SEQRES 19 B 472 VAL VAL VAL ASN ARG SER GLU GLU ARG VAL SER ALA ILE
SEQRES 20 B 472 ARG GLU GLU MET PRO GLY ILE GLU ILE ILE TYR ARG PRO
SEQRES 21 B 472 LEU ASP GLU MET LEU ALA CYS ALA SER GLU ALA ASP VAL
SEQRES 22 B 472 VAL PHE THR SER THR ALA SER GLU THR PRO LEU PHE LEU
SEQRES 23 B 472 LYS GLU HIS VAL GLU ASN LEU PRO GLN ALA SER PRO GLU
SEQRES 24 B 472 VAL GLY GLY LEU ARG HIS PHE VAL ASP ILE SER VAL PRO
SEQRES 25 B 472 ARG ASN VAL GLY SER CYS VAL GLY GLU VAL GLU THR ALA
SEQRES 26 B 472 ARG VAL TYR ASN VAL ASP ASP LEU LYS GLU VAL VAL ALA
SEQRES 27 B 472 ALA ASN LYS GLU ASP ARG MET ARG LYS ALA MET GLU ALA
SEQRES 28 B 472 GLN THR ILE ILE THR GLU GLU SER THR GLN PHE GLU ALA
SEQRES 29 B 472 TRP ARG ASP SER LEU GLU THR VAL PRO THR ILE LYS LYS
SEQRES 30 B 472 LEU ARG ALA TYR ALA GLU ARG ILE ARG VAL ALA GLU LEU
SEQRES 31 B 472 GLU LYS CYS MET SER LYS MET GLY ASP ASP ILE ASN LYS
SEQRES 32 B 472 LYS THR THR ARG ALA VAL ASP ASP LEU SER ARG GLY ILE
SEQRES 33 B 472 VAL ASN ARG PHE LEU HIS GLY PRO MET GLN HIS LEU ARG
SEQRES 34 B 472 CYS ASP GLY SER ASP SER ARG THR LEU SER GLU THR LEU
SEQRES 35 B 472 GLU ASN MET HIS ALA LEU ASN ARG MET TYR GLY LEU GLU
SEQRES 36 B 472 LYS ASP ILE LEU GLU GLU LYS LEU LYS ALA MET ALA GLU
SEQRES 37 B 472 GLN GLN GLN LYS
SEQRES 1 C 310 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 310 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 C 310 GLY GLN GLN MET GLY ARG GLY SER CYS SER VAL SER THR
SEQRES 4 C 310 THR LEU ASP THR PRO ALA THR ALA SER THR HIS LYS PRO
SEQRES 5 C 310 PHE PRO ALA GLU VAL SER ARG SER ILE MET GLU LEU SER
SEQRES 6 C 310 SER VAL GLY THR LEU SER THR LEU THR HIS ASP GLY TRP
SEQRES 7 C 310 PRO LEU GLY VAL GLY VAL ARG PHE ALA VAL ASP LYS ASP
SEQRES 8 C 310 GLY THR PRO VAL LEU CYS LEU ASN ARG SER VAL SER PRO
SEQRES 9 C 310 ASP LYS ARG SER ALA LEU HIS VAL GLN LEU GLU GLN CYS
SEQRES 10 C 310 GLY LEU ARG THR PRO GLN CYS THR ILE GLN GLY SER ILE
SEQRES 11 C 310 GLY ARG PRO GLY ASP ASP THR VAL LEU LYS ARG LEU SER
SEQRES 12 C 310 ALA THR TRP ARG GLU LYS PHE GLY GLU GLU VAL LYS GLU
SEQRES 13 C 310 ASP SER LEU TYR VAL VAL ALA VAL ASP ARG VAL LEU GLN
SEQRES 14 C 310 MET GLU ASP PHE MET GLU ASP GLY ILE TRP VAL ALA SER
SEQRES 15 C 310 SER ASP TYR LYS ASN ALA SER PRO ASP PRO LEU ARG ASP
SEQRES 16 C 310 ILE ALA GLU ASP ILE VAL ASN GLN ILE ASN ALA ASN ASN
SEQRES 17 C 310 MET GLU ASP ILE PHE ARG PHE CYS ASN VAL TYR VAL ASP
SEQRES 18 C 310 LEU ASP PHE VAL VAL SER GLU THR LYS MET ILE TRP MET
SEQRES 19 C 310 ASP ARG LEU GLY PHE ASP LEU ARG VAL TRP SER PRO ARG
SEQRES 20 C 310 GLY VAL TYR ASP VAL ARG ILE PRO PHE PRO MET GLU VAL
SEQRES 21 C 310 THR ASP GLU LYS GLY ALA LYS SER SER PHE ASN GLY MET
SEQRES 22 C 310 SER GLN LEU ALA TRP GLU VAL GLU LYS SER TYR CYS PRO
SEQRES 23 C 310 ALA ASP PHE ASN LYS VAL LYS LEU LEU LYS GLN VAL VAL
SEQRES 24 C 310 GLY SER SER HIS SER HIS LYS GLY GLY GLY GLN
SEQRES 1 D 310 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 310 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 D 310 GLY GLN GLN MET GLY ARG GLY SER CYS SER VAL SER THR
SEQRES 4 D 310 THR LEU ASP THR PRO ALA THR ALA SER THR HIS LYS PRO
SEQRES 5 D 310 PHE PRO ALA GLU VAL SER ARG SER ILE MET GLU LEU SER
SEQRES 6 D 310 SER VAL GLY THR LEU SER THR LEU THR HIS ASP GLY TRP
SEQRES 7 D 310 PRO LEU GLY VAL GLY VAL ARG PHE ALA VAL ASP LYS ASP
SEQRES 8 D 310 GLY THR PRO VAL LEU CYS LEU ASN ARG SER VAL SER PRO
SEQRES 9 D 310 ASP LYS ARG SER ALA LEU HIS VAL GLN LEU GLU GLN CYS
SEQRES 10 D 310 GLY LEU ARG THR PRO GLN CYS THR ILE GLN GLY SER ILE
SEQRES 11 D 310 GLY ARG PRO GLY ASP ASP THR VAL LEU LYS ARG LEU SER
SEQRES 12 D 310 ALA THR TRP ARG GLU LYS PHE GLY GLU GLU VAL LYS GLU
SEQRES 13 D 310 ASP SER LEU TYR VAL VAL ALA VAL ASP ARG VAL LEU GLN
SEQRES 14 D 310 MET GLU ASP PHE MET GLU ASP GLY ILE TRP VAL ALA SER
SEQRES 15 D 310 SER ASP TYR LYS ASN ALA SER PRO ASP PRO LEU ARG ASP
SEQRES 16 D 310 ILE ALA GLU ASP ILE VAL ASN GLN ILE ASN ALA ASN ASN
SEQRES 17 D 310 MET GLU ASP ILE PHE ARG PHE CYS ASN VAL TYR VAL ASP
SEQRES 18 D 310 LEU ASP PHE VAL VAL SER GLU THR LYS MET ILE TRP MET
SEQRES 19 D 310 ASP ARG LEU GLY PHE ASP LEU ARG VAL TRP SER PRO ARG
SEQRES 20 D 310 GLY VAL TYR ASP VAL ARG ILE PRO PHE PRO MET GLU VAL
SEQRES 21 D 310 THR ASP GLU LYS GLY ALA LYS SER SER PHE ASN GLY MET
SEQRES 22 D 310 SER GLN LEU ALA TRP GLU VAL GLU LYS SER TYR CYS PRO
SEQRES 23 D 310 ALA ASP PHE ASN LYS VAL LYS LEU LEU LYS GLN VAL VAL
SEQRES 24 D 310 GLY SER SER HIS SER HIS LYS GLY GLY GLY GLN
SEQRES 1 E 159 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU
SEQRES 2 E 159 LEU LEU ALA ALA GLN PRO ALA MET ALA MET ASP ILE GLY
SEQRES 3 E 159 ILE ASN SER ASP PRO HIS HIS HIS HIS HIS HIS ILE VAL
SEQRES 4 E 159 GLU PRO LYS LYS GLN GLU LEU ILE SER LYS LEU LYS THR
SEQRES 5 E 159 GLY LYS THR PHE LEU ARG ASN GLN GLU PRO GLU LYS ALA
SEQRES 6 E 159 TYR THR GLU PHE LYS ILE ALA LEU GLU LEU ALA GLN SER
SEQRES 7 E 159 LEU LYS ASP PRO THR GLU GLU LYS LYS ALA ALA ARG GLY
SEQRES 8 E 159 LEU GLY ALA SER LEU GLN ARG GLN GLY LYS TYR ARG GLU
SEQRES 9 E 159 ALA ILE GLN TYR HIS SER MET VAL LEU ALA ILE SER LYS
SEQRES 10 E 159 ARG GLU SER GLU ASP SER GLY ILE THR GLU ALA TYR GLY
SEQRES 11 E 159 ALA ILE ALA ASP CYS TYR THR GLU LEU GLY ASP LEU GLU
SEQRES 12 E 159 LYS ALA GLY LYS PHE TYR ASP THR TYR ILE ALA ARG LEU
SEQRES 13 E 159 GLU THR ASP
SEQRES 1 F 159 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU
SEQRES 2 F 159 LEU LEU ALA ALA GLN PRO ALA MET ALA MET ASP ILE GLY
SEQRES 3 F 159 ILE ASN SER ASP PRO HIS HIS HIS HIS HIS HIS ILE VAL
SEQRES 4 F 159 GLU PRO LYS LYS GLN GLU LEU ILE SER LYS LEU LYS THR
SEQRES 5 F 159 GLY LYS THR PHE LEU ARG ASN GLN GLU PRO GLU LYS ALA
SEQRES 6 F 159 TYR THR GLU PHE LYS ILE ALA LEU GLU LEU ALA GLN SER
SEQRES 7 F 159 LEU LYS ASP PRO THR GLU GLU LYS LYS ALA ALA ARG GLY
SEQRES 8 F 159 LEU GLY ALA SER LEU GLN ARG GLN GLY LYS TYR ARG GLU
SEQRES 9 F 159 ALA ILE GLN TYR HIS SER MET VAL LEU ALA ILE SER LYS
SEQRES 10 F 159 ARG GLU SER GLU ASP SER GLY ILE THR GLU ALA TYR GLY
SEQRES 11 F 159 ALA ILE ALA ASP CYS TYR THR GLU LEU GLY ASP LEU GLU
SEQRES 12 F 159 LYS ALA GLY LYS PHE TYR ASP THR TYR ILE ALA ARG LEU
SEQRES 13 F 159 GLU THR ASP
FORMUL 7 HOH *6(H2 O)
HELIX 1 AA1 PRO A 108 GLU A 113 1 6
HELIX 2 AA2 LYS A 114 ALA A 116 5 3
HELIX 3 AA3 PRO A 118 ALA A 120 5 3
HELIX 4 AA4 GLU A 121 GLY A 131 1 11
HELIX 5 AA5 HIS A 157 GLY A 172 1 16
HELIX 6 AA6 PRO A 174 GLN A 180 1 7
HELIX 7 AA7 ASN A 187 ALA A 199 1 13
HELIX 8 AA8 GLY A 209 GLY A 222 1 14
HELIX 9 AA9 GLY A 229 THR A 250 1 22
HELIX 10 AB1 ASN A 251 SER A 254 5 4
HELIX 11 AB2 SER A 258 LEU A 271 1 14
HELIX 12 AB3 GLY A 287 ALA A 299 1 13
HELIX 13 AB4 SER A 311 GLU A 320 1 10
HELIX 14 AB5 PRO A 331 ASP A 333 5 3
HELIX 15 AB6 GLU A 334 SER A 340 1 7
HELIX 16 AB7 LEU A 357 ASN A 363 1 7
HELIX 17 AB8 ASN A 400 GLU A 406 5 7
HELIX 18 AB9 MET A 416 SER A 439 1 24
HELIX 19 AC1 THR A 442 SER A 466 1 25
HELIX 20 AC2 LYS A 474 HIS A 498 1 25
HELIX 21 AC3 ASP A 505 GLY A 524 1 20
HELIX 22 AC4 PRO B 108 GLU B 113 1 6
HELIX 23 AC5 LYS B 114 ALA B 116 5 3
HELIX 24 AC6 PRO B 118 ALA B 120 5 3
HELIX 25 AC7 GLU B 121 GLY B 131 1 11
HELIX 26 AC8 SER B 155 GLY B 172 1 18
HELIX 27 AC9 PRO B 174 GLN B 180 1 7
HELIX 28 AD1 ASN B 187 ALA B 199 1 13
HELIX 29 AD2 GLY B 209 VAL B 221 1 13
HELIX 30 AD3 GLY B 229 THR B 250 1 22
HELIX 31 AD4 ASN B 251 SER B 254 5 4
HELIX 32 AD5 SER B 258 LEU B 271 1 14
HELIX 33 AD6 GLY B 287 ALA B 299 1 13
HELIX 34 AD7 SER B 311 GLU B 320 1 10
HELIX 35 AD8 PRO B 331 ASP B 333 5 3
HELIX 36 AD9 GLU B 334 SER B 340 1 7
HELIX 37 AE1 LEU B 357 ASN B 363 1 7
HELIX 38 AE2 ASN B 400 GLU B 406 5 7
HELIX 39 AE3 MET B 416 SER B 439 1 24
HELIX 40 AE4 THR B 442 SER B 466 1 25
HELIX 41 AE5 THR B 476 HIS B 498 1 23
HELIX 42 AE6 ARG B 507 GLY B 524 1 18
HELIX 43 AE7 PHE C 60 SER C 72 1 13
HELIX 44 AE8 ASP C 143 PHE C 157 1 15
HELIX 45 AE9 SER C 189 ALA C 195 1 7
HELIX 46 AF1 LEU C 200 ASN C 215 1 16
HELIX 47 AF2 ASN C 215 TYR C 226 1 12
HELIX 48 AF3 ASP C 269 LYS C 289 1 21
HELIX 49 AF4 PHE D 60 SER D 72 1 13
HELIX 50 AF5 ASP D 143 GLY D 158 1 16
HELIX 51 AF6 LYS D 162 LEU D 166 5 5
HELIX 52 AF7 SER D 189 ALA D 195 1 7
HELIX 53 AF8 LEU D 200 ASN D 215 1 16
HELIX 54 AF9 ASN D 215 TYR D 226 1 12
HELIX 55 AG1 ASP D 269 LYS D 289 1 21
HELIX 56 AG2 PRO E 199 ASN E 217 1 19
HELIX 57 AG3 GLU E 219 LEU E 237 1 19
HELIX 58 AG4 ASP E 239 GLN E 257 1 19
HELIX 59 AG5 LYS E 259 SER E 268 1 10
HELIX 60 AG6 SER E 268 SER E 278 1 11
HELIX 61 AG7 GLY E 282 LEU E 297 1 16
HELIX 62 AG8 ASP E 299 LEU E 314 1 16
HELIX 63 AG9 LYS F 201 ASN F 217 1 17
HELIX 64 AH1 GLU F 219 LEU F 237 1 19
HELIX 65 AH2 ASP F 239 ARG F 256 1 18
HELIX 66 AH3 LYS F 259 SER F 268 1 10
HELIX 67 AH4 SER F 268 SER F 278 1 11
HELIX 68 AH5 GLY F 282 LEU F 297 1 16
HELIX 69 AH6 ASP F 299 GLU F 315 1 17
SHEET 1 AA1 4 ILE A 135 THR A 143 0
SHEET 2 AA1 4 ARG A 146 ALA A 153 -1 O GLU A 148 N LEU A 141
SHEET 3 AA1 4 SER A 96 SER A 103 -1 N ILE A 100 O ILE A 149
SHEET 4 AA1 4 PHE A 183 LEU A 185 -1 O PHE A 183 N GLY A 101
SHEET 1 AA2 6 GLU A 326 ARG A 330 0
SHEET 2 AA2 6 LYS A 304 VAL A 308 1 N VAL A 307 O ILE A 328
SHEET 3 AA2 6 MET A 281 ILE A 284 1 N VAL A 283 O VAL A 306
SHEET 4 AA2 6 VAL A 344 THR A 347 1 O PHE A 346 N CYS A 282
SHEET 5 AA2 6 ARG A 375 ASP A 379 1 O VAL A 378 N THR A 347
SHEET 6 AA2 6 ALA A 396 TYR A 399 1 O TYR A 399 N ASP A 379
SHEET 1 AA3 4 ILE B 135 THR B 143 0
SHEET 2 AA3 4 ARG B 146 ALA B 153 -1 O GLU B 148 N LEU B 141
SHEET 3 AA3 4 SER B 96 SER B 103 -1 N ILE B 100 O ILE B 149
SHEET 4 AA3 4 PHE B 183 TYR B 186 -1 O PHE B 183 N GLY B 101
SHEET 1 AA4 6 GLU B 326 ARG B 330 0
SHEET 2 AA4 6 LYS B 304 VAL B 308 1 N VAL B 305 O GLU B 326
SHEET 3 AA4 6 MET B 281 ILE B 284 1 N VAL B 283 O VAL B 306
SHEET 4 AA4 6 VAL B 344 THR B 347 1 O PHE B 346 N CYS B 282
SHEET 5 AA4 6 ARG B 375 ASP B 379 1 O VAL B 378 N THR B 347
SHEET 6 AA4 6 ALA B 396 TYR B 399 1 O ARG B 397 N PHE B 377
SHEET 1 AA5 8 ILE C 185 ALA C 188 0
SHEET 2 AA5 8 TYR C 167 MET C 177 -1 N GLN C 176 O ILE C 185
SHEET 3 AA5 8 GLN C 130 GLY C 138 -1 N SER C 136 O ALA C 170
SHEET 4 AA5 8 ARG C 114 GLN C 120 -1 N LEU C 117 O ILE C 133
SHEET 5 AA5 8 VAL C 74 LEU C 80 -1 N SER C 78 O ALA C 116
SHEET 6 AA5 8 PRO C 86 VAL C 95 -1 O LEU C 87 N THR C 79
SHEET 7 AA5 8 PRO C 101 LEU C 103 -1 O VAL C 102 N ALA C 94
SHEET 8 AA5 8 TYR C 167 MET C 177 -1 O TYR C 167 N LEU C 103
SHEET 1 AA6 3 GLU C 235 ASP C 242 0
SHEET 2 AA6 3 GLY C 245 TRP C 251 -1 O TRP C 251 N GLU C 235
SHEET 3 AA6 3 VAL C 256 PRO C 262 -1 O TYR C 257 N VAL C 250
SHEET 1 AA7 8 ILE D 185 ALA D 188 0
SHEET 2 AA7 8 TYR D 167 MET D 177 -1 N VAL D 174 O VAL D 187
SHEET 3 AA7 8 GLN D 130 GLY D 138 -1 N SER D 136 O ALA D 170
SHEET 4 AA7 8 ARG D 114 GLN D 120 -1 N LEU D 117 O ILE D 133
SHEET 5 AA7 8 VAL D 74 LEU D 80 -1 N SER D 78 O ALA D 116
SHEET 6 AA7 8 PRO D 86 VAL D 95 -1 O VAL D 89 N LEU D 77
SHEET 7 AA7 8 PRO D 101 LEU D 103 -1 O VAL D 102 N ALA D 94
SHEET 8 AA7 8 TYR D 167 MET D 177 -1 O TYR D 167 N LEU D 103
SHEET 1 AA8 3 THR D 236 ASP D 242 0
SHEET 2 AA8 3 GLY D 245 TRP D 251 -1 O ARG D 249 N LYS D 237
SHEET 3 AA8 3 VAL D 256 PRO D 262 -1 O VAL D 259 N LEU D 248
CISPEP 1 SER A 203 LEU A 204 0 -8.92
CISPEP 2 VAL A 382 PRO A 383 0 -0.71
CISPEP 3 VAL B 277 SER B 278 0 0.67
CISPEP 4 VAL B 382 PRO B 383 0 -1.04
CISPEP 5 GLY B 387 SER B 388 0 3.15
CISPEP 6 VAL B 407 VAL B 408 0 7.52
CISPEP 7 ILE B 472 ASN B 473 0 4.84
CISPEP 8 SER C 108 VAL C 109 0 -9.91
CISPEP 9 VAL C 109 SER C 110 0 -1.85
CISPEP 10 GLU E 315 THR E 316 0 3.62
CRYST1 216.994 53.211 203.763 90.00 108.36 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004608 0.000000 0.001529 0.00000
SCALE2 0.000000 0.018793 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005171 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
