HEADER PLANT PROTEIN 22-SEP-16 5GYL
TITLE STRUCTURE OF CICER ARIETINUM 11S GLOUBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEGUMIN-LIKE PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CICER ARIETINUM;
SOURCE 3 ORGANISM_TAXID: 3827;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS 11S GLOUBULIN, SEEDS, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ZHOU,F.ZHANG
REVDAT 4 29-NOV-23 5GYL 1 REMARK
REVDAT 3 14-SEP-22 5GYL 1 JRNL REMARK
REVDAT 2 07-FEB-18 5GYL 1 REMARK
REVDAT 1 04-OCT-17 5GYL 0
JRNL AUTH L.SUN,A.ZHOU,F.ZHANG
JRNL TITL CRYSTALLIZATION AND CRYSTALLOGRAPHIC STUDIES OF A NOVEL
JRNL TITL 2 CHICKPEA 11S GLOBULIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 78 324 2022
JRNL REFN ESSN 2053-230X
JRNL PMID 36048082
JRNL DOI 10.1107/S2053230X22007919
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 62994
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840
REMARK 3 FREE R VALUE TEST SET COUNT : 3050
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 41.0128 - 6.1579 0.98 2784 123 0.1825 0.1738
REMARK 3 2 6.1579 - 4.8903 0.97 2724 133 0.1570 0.1905
REMARK 3 3 4.8903 - 4.2728 0.99 2729 170 0.1353 0.1446
REMARK 3 4 4.2728 - 3.8825 0.99 2721 162 0.1528 0.1737
REMARK 3 5 3.8825 - 3.6044 0.99 2726 146 0.1863 0.2042
REMARK 3 6 3.6044 - 3.3920 0.99 2769 126 0.1964 0.2452
REMARK 3 7 3.3920 - 3.2222 1.00 2792 101 0.1968 0.2252
REMARK 3 8 3.2222 - 3.0820 1.00 2742 131 0.2033 0.2239
REMARK 3 9 3.0820 - 2.9634 1.00 2784 117 0.2102 0.2079
REMARK 3 10 2.9634 - 2.8611 1.00 2754 113 0.2175 0.2546
REMARK 3 11 2.8611 - 2.7717 1.00 2778 136 0.2162 0.2337
REMARK 3 12 2.7717 - 2.6925 1.00 2711 151 0.2123 0.2307
REMARK 3 13 2.6925 - 2.6216 1.00 2736 146 0.2260 0.2554
REMARK 3 14 2.6216 - 2.5577 1.00 2735 147 0.2268 0.2707
REMARK 3 15 2.5577 - 2.4995 1.00 2723 160 0.2341 0.2794
REMARK 3 16 2.4995 - 2.4463 1.00 2727 159 0.2296 0.2563
REMARK 3 17 2.4463 - 2.3974 1.00 2763 141 0.2263 0.2832
REMARK 3 18 2.3974 - 2.3522 1.00 2721 150 0.2425 0.3082
REMARK 3 19 2.3522 - 2.3102 1.00 2724 150 0.2588 0.2984
REMARK 3 20 2.3102 - 2.2710 0.95 2622 144 0.4137 0.4537
REMARK 3 21 2.2710 - 2.2344 0.99 2739 122 0.4970 0.5099
REMARK 3 22 2.2344 - 2.2000 0.90 2440 122 0.5136 0.5252
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.820
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 : 0.004 9179
REMARK 3 ANGLE : 0.689 12395
REMARK 3 CHIRALITY : 0.048 1329
REMARK 3 PLANARITY : 0.004 1662
REMARK 3 DIHEDRAL : 16.166 5567
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1026 0.4818 -17.1013
REMARK 3 T TENSOR
REMARK 3 T11: 0.3034 T22: 0.3032
REMARK 3 T33: 0.1633 T12: 0.0095
REMARK 3 T13: -0.0082 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.6767 L22: 1.0802
REMARK 3 L33: 0.4058 L12: -0.0275
REMARK 3 L13: -0.0200 L23: 0.0430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.1855 S13: -0.0001
REMARK 3 S21: -0.2949 S22: 0.0045 S23: -0.0222
REMARK 3 S31: 0.0054 S32: 0.0205 S33: -0.0121
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 5GYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1300001658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-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 : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63945
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 79.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.0000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1FXZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 3350, 0.1M MES PH7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
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 41.71811
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.19078
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.71811
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 50.30500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 65.19078
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 21
REMARK 465 LEU A 22
REMARK 465 ARG A 23
REMARK 465 ASP A 24
REMARK 465 GLN A 25
REMARK 465 PRO A 26
REMARK 465 GLU A 27
REMARK 465 GLN A 28
REMARK 465 GLU A 116
REMARK 465 SER A 117
REMARK 465 GLU A 118
REMARK 465 GLN A 119
REMARK 465 GLY A 120
REMARK 465 GLU A 121
REMARK 465 GLY A 122
REMARK 465 SER A 123
REMARK 465 LEU A 192
REMARK 465 ARG A 193
REMARK 465 TYR A 194
REMARK 465 GLN A 195
REMARK 465 GLN A 196
REMARK 465 GLU A 197
REMARK 465 GLY A 198
REMARK 465 SER A 199
REMARK 465 GLU A 200
REMARK 465 GLU A 201
REMARK 465 GLU A 202
REMARK 465 GLU A 203
REMARK 465 ASN A 204
REMARK 465 GLU A 205
REMARK 465 GLU A 258
REMARK 465 LYS A 259
REMARK 465 GLU A 260
REMARK 465 PRO A 261
REMARK 465 ARG A 262
REMARK 465 GLN A 263
REMARK 465 LYS A 264
REMARK 465 ARG A 265
REMARK 465 GLY A 266
REMARK 465 SER A 267
REMARK 465 ARG A 268
REMARK 465 GLN A 269
REMARK 465 GLU A 270
REMARK 465 GLU A 271
REMARK 465 ASP A 272
REMARK 465 GLU A 273
REMARK 465 ASP A 274
REMARK 465 GLU A 275
REMARK 465 ASP A 276
REMARK 465 GLU A 277
REMARK 465 LYS A 278
REMARK 465 ARG A 279
REMARK 465 GLN A 280
REMARK 465 PRO A 281
REMARK 465 HIS A 282
REMARK 465 ARG A 283
REMARK 465 HIS A 284
REMARK 465 SER A 285
REMARK 465 ARG A 286
REMARK 465 GLN A 287
REMARK 465 ASP A 288
REMARK 465 GLU A 289
REMARK 465 ASP A 290
REMARK 465 GLU A 291
REMARK 465 ASP A 292
REMARK 465 GLU A 293
REMARK 465 LYS A 294
REMARK 465 ARG A 295
REMARK 465 GLN A 296
REMARK 465 PRO A 297
REMARK 465 ARG A 298
REMARK 465 ARG A 299
REMARK 465 HIS A 300
REMARK 465 SER A 301
REMARK 465 ARG A 302
REMARK 465 GLY A 303
REMARK 465 GLY A 304
REMARK 465 SER A 305
REMARK 465 LYS A 306
REMARK 465 SER A 307
REMARK 465 GLN A 308
REMARK 465 ARG A 309
REMARK 465 ASP A 310
REMARK 465 ASN A 311
REMARK 465 GLY A 312
REMARK 465 PHE A 313
REMARK 465 GLU A 314
REMARK 465 GLU A 315
REMARK 465 THR A 316
REMARK 465 SER A 489
REMARK 465 ASP A 490
REMARK 465 SER A 491
REMARK 465 ASP A 492
REMARK 465 ASN A 493
REMARK 465 LYS A 494
REMARK 465 ALA A 495
REMARK 465 ALA A 496
REMARK 465 ALA A 497
REMARK 465 LEU A 498
REMARK 465 GLU A 499
REMARK 465 SER B 21
REMARK 465 LEU B 22
REMARK 465 ARG B 23
REMARK 465 ASP B 24
REMARK 465 GLN B 25
REMARK 465 PRO B 26
REMARK 465 GLU B 27
REMARK 465 GLN B 28
REMARK 465 GLU B 116
REMARK 465 SER B 117
REMARK 465 GLU B 118
REMARK 465 GLN B 119
REMARK 465 GLY B 120
REMARK 465 GLU B 121
REMARK 465 GLY B 122
REMARK 465 SER B 123
REMARK 465 TYR B 194
REMARK 465 GLN B 195
REMARK 465 GLN B 196
REMARK 465 GLU B 197
REMARK 465 GLY B 198
REMARK 465 SER B 199
REMARK 465 GLU B 200
REMARK 465 GLU B 201
REMARK 465 GLU B 202
REMARK 465 GLU B 203
REMARK 465 ASN B 204
REMARK 465 GLU B 205
REMARK 465 GLU B 258
REMARK 465 LYS B 259
REMARK 465 GLU B 260
REMARK 465 PRO B 261
REMARK 465 ARG B 262
REMARK 465 GLN B 263
REMARK 465 LYS B 264
REMARK 465 ARG B 265
REMARK 465 GLY B 266
REMARK 465 SER B 267
REMARK 465 ARG B 268
REMARK 465 GLN B 269
REMARK 465 GLU B 270
REMARK 465 GLU B 271
REMARK 465 ASP B 272
REMARK 465 GLU B 273
REMARK 465 ASP B 274
REMARK 465 GLU B 275
REMARK 465 ASP B 276
REMARK 465 GLU B 277
REMARK 465 LYS B 278
REMARK 465 ARG B 279
REMARK 465 GLN B 280
REMARK 465 PRO B 281
REMARK 465 HIS B 282
REMARK 465 ARG B 283
REMARK 465 HIS B 284
REMARK 465 SER B 285
REMARK 465 ARG B 286
REMARK 465 GLN B 287
REMARK 465 ASP B 288
REMARK 465 GLU B 289
REMARK 465 ASP B 290
REMARK 465 GLU B 291
REMARK 465 ASP B 292
REMARK 465 GLU B 293
REMARK 465 LYS B 294
REMARK 465 ARG B 295
REMARK 465 GLN B 296
REMARK 465 PRO B 297
REMARK 465 ARG B 298
REMARK 465 ARG B 299
REMARK 465 HIS B 300
REMARK 465 SER B 301
REMARK 465 ARG B 302
REMARK 465 GLY B 303
REMARK 465 GLY B 304
REMARK 465 SER B 305
REMARK 465 LYS B 306
REMARK 465 SER B 307
REMARK 465 GLN B 308
REMARK 465 ARG B 309
REMARK 465 ASP B 310
REMARK 465 ASN B 311
REMARK 465 GLY B 312
REMARK 465 PHE B 313
REMARK 465 GLU B 314
REMARK 465 GLU B 315
REMARK 465 THR B 316
REMARK 465 SER B 489
REMARK 465 ASP B 490
REMARK 465 SER B 491
REMARK 465 ASP B 492
REMARK 465 ASN B 493
REMARK 465 LYS B 494
REMARK 465 ALA B 495
REMARK 465 ALA B 496
REMARK 465 ALA B 497
REMARK 465 LEU B 498
REMARK 465 GLU B 499
REMARK 465 SER C 21
REMARK 465 LEU C 22
REMARK 465 ARG C 23
REMARK 465 ASP C 24
REMARK 465 GLN C 25
REMARK 465 PRO C 26
REMARK 465 GLU C 27
REMARK 465 GLN C 28
REMARK 465 GLU C 116
REMARK 465 SER C 117
REMARK 465 GLU C 118
REMARK 465 GLN C 119
REMARK 465 GLY C 120
REMARK 465 GLU C 121
REMARK 465 GLY C 122
REMARK 465 SER C 123
REMARK 465 TYR C 194
REMARK 465 GLN C 195
REMARK 465 GLN C 196
REMARK 465 GLU C 197
REMARK 465 GLY C 198
REMARK 465 SER C 199
REMARK 465 GLU C 200
REMARK 465 GLU C 201
REMARK 465 GLU C 202
REMARK 465 GLU C 203
REMARK 465 ASN C 204
REMARK 465 GLU C 205
REMARK 465 GLU C 258
REMARK 465 LYS C 259
REMARK 465 GLU C 260
REMARK 465 PRO C 261
REMARK 465 ARG C 262
REMARK 465 GLN C 263
REMARK 465 LYS C 264
REMARK 465 ARG C 265
REMARK 465 GLY C 266
REMARK 465 SER C 267
REMARK 465 ARG C 268
REMARK 465 GLN C 269
REMARK 465 GLU C 270
REMARK 465 GLU C 271
REMARK 465 ASP C 272
REMARK 465 GLU C 273
REMARK 465 ASP C 274
REMARK 465 GLU C 275
REMARK 465 ASP C 276
REMARK 465 GLU C 277
REMARK 465 LYS C 278
REMARK 465 ARG C 279
REMARK 465 GLN C 280
REMARK 465 PRO C 281
REMARK 465 HIS C 282
REMARK 465 ARG C 283
REMARK 465 HIS C 284
REMARK 465 SER C 285
REMARK 465 ARG C 286
REMARK 465 GLN C 287
REMARK 465 ASP C 288
REMARK 465 GLU C 289
REMARK 465 ASP C 290
REMARK 465 GLU C 291
REMARK 465 ASP C 292
REMARK 465 GLU C 293
REMARK 465 LYS C 294
REMARK 465 ARG C 295
REMARK 465 GLN C 296
REMARK 465 PRO C 297
REMARK 465 ARG C 298
REMARK 465 ARG C 299
REMARK 465 HIS C 300
REMARK 465 SER C 301
REMARK 465 ARG C 302
REMARK 465 GLY C 303
REMARK 465 GLY C 304
REMARK 465 SER C 305
REMARK 465 LYS C 306
REMARK 465 SER C 307
REMARK 465 GLN C 308
REMARK 465 ARG C 309
REMARK 465 ASP C 310
REMARK 465 ASN C 311
REMARK 465 GLY C 312
REMARK 465 PHE C 313
REMARK 465 GLU C 314
REMARK 465 GLU C 315
REMARK 465 THR C 316
REMARK 465 SER C 489
REMARK 465 ASP C 490
REMARK 465 SER C 491
REMARK 465 ASP C 492
REMARK 465 ASN C 493
REMARK 465 LYS C 494
REMARK 465 ALA C 495
REMARK 465 ALA C 496
REMARK 465 ALA C 497
REMARK 465 LEU C 498
REMARK 465 GLU C 499
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 488 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 488 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 488 CG CD NE CZ NH1 NH2
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 B 58 NH1 ARG B 63 1.90
REMARK 500 OG1 THR C 54 NH2 ARG C 193 2.12
REMARK 500 NH2 ARG C 80 OE2 GLU C 190 2.15
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 LEU A 174 -110.38 -96.13
REMARK 500 ASN A 186 53.65 -152.59
REMARK 500 ALA A 339 -47.69 -135.07
REMARK 500 ASN A 378 32.16 -140.24
REMARK 500 ASN A 418 -16.51 75.88
REMARK 500 ASN A 438 131.37 -170.26
REMARK 500 LEU B 174 -111.02 -96.48
REMARK 500 ASN B 186 51.57 -152.71
REMARK 500 ALA B 339 -49.23 -134.26
REMARK 500 ASN B 418 -16.30 76.41
REMARK 500 LEU C 174 -109.29 -96.17
REMARK 500 ASN C 186 52.48 -152.70
REMARK 500 PHE C 191 72.18 -111.10
REMARK 500 ALA C 339 -48.23 -134.44
REMARK 500 ASN C 378 30.92 -140.25
REMARK 500 ASN C 418 -15.45 75.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY EXIST.
DBREF 5GYL A 21 499 PDB 5GYL 5GYL 21 499
DBREF 5GYL B 21 499 PDB 5GYL 5GYL 21 499
DBREF 5GYL C 21 499 PDB 5GYL 5GYL 21 499
SEQRES 1 A 479 SER LEU ARG ASP GLN PRO GLU GLN ASN GLU CYS GLN LEU
SEQRES 2 A 479 GLU HIS LEU ASN ALA LEU GLU PRO ASP ASN ARG ILE LYS
SEQRES 3 A 479 SER GLU GLY GLY LEU ILE GLU THR TRP ASN PRO SER ASN
SEQRES 4 A 479 LYS GLN PHE ARG CYS ALA GLY VAL ALA LEU SER ARG ALA
SEQRES 5 A 479 THR LEU GLN PRO ASN SER LEU ARG ARG PRO PHE TYR THR
SEQRES 6 A 479 ASN ALA PRO GLN GLU ILE PHE ILE GLN GLN GLY ASN GLY
SEQRES 7 A 479 TYR PHE GLY MET VAL PHE PRO GLY CYS VAL GLU THR PHE
SEQRES 8 A 479 GLU GLU PRO ARG GLU SER GLU GLN GLY GLU GLY SER LYS
SEQRES 9 A 479 PHE ARG ASP SER HIS GLN LYS VAL ASN ARG PHE ARG GLU
SEQRES 10 A 479 GLY ASP ILE ILE ALA VAL PRO THR GLY VAL VAL PHE TRP
SEQRES 11 A 479 MET PHE ASN ASP GLN ASP THR PRO VAL ILE ALA VAL SER
SEQRES 12 A 479 LEU ILE ASP THR SER SER PHE GLN ASN GLN LEU ASP GLN
SEQRES 13 A 479 MET PRO ARG ARG PHE TYR LEU ALA GLY ASN HIS GLU GLN
SEQRES 14 A 479 GLU PHE LEU ARG TYR GLN GLN GLU GLY SER GLU GLU GLU
SEQRES 15 A 479 GLU ASN GLU GLY GLY ASN ILE PHE SER GLY PHE LYS ARG
SEQRES 16 A 479 ASP PHE LEU GLU ASP ALA LEU ASN VAL ASN ARG ARG ILE
SEQRES 17 A 479 VAL ASN LYS LEU GLN GLY ARG ASN GLU ASP GLU GLU LYS
SEQRES 18 A 479 GLY ALA ILE VAL LYS VAL LYS GLY GLY LEU SER ILE ILE
SEQRES 19 A 479 THR PRO PRO GLU LYS GLU PRO ARG GLN LYS ARG GLY SER
SEQRES 20 A 479 ARG GLN GLU GLU ASP GLU ASP GLU ASP GLU LYS ARG GLN
SEQRES 21 A 479 PRO HIS ARG HIS SER ARG GLN ASP GLU ASP GLU ASP GLU
SEQRES 22 A 479 LYS ARG GLN PRO ARG ARG HIS SER ARG GLY GLY SER LYS
SEQRES 23 A 479 SER GLN ARG ASP ASN GLY PHE GLU GLU THR ILE CYS THR
SEQRES 24 A 479 ALA ARG LEU HIS GLN ASN ILE GLY SER SER SER SER PRO
SEQRES 25 A 479 ASP ILE TYR ASN PRO GLN ALA GLY ARG ILE LYS THR VAL
SEQRES 26 A 479 THR SER PHE ASP LEU PRO ALA LEU ARG PHE LEU LYS LEU
SEQRES 27 A 479 SER ALA GLU PHE GLY SER LEU HIS LYS ASN ALA MET PHE
SEQRES 28 A 479 VAL PRO HIS TYR ASN LEU ASN ALA ASN SER ILE LEU TYR
SEQRES 29 A 479 ALA LEU LYS GLY ARG ALA ARG LEU GLN ILE VAL ASN CYS
SEQRES 30 A 479 LYS GLY ASN SER VAL PHE ASP GLY GLU LEU GLU ALA GLY
SEQRES 31 A 479 ARG ALA LEU ILE VAL PRO GLN ASN PHE ALA ILE ALA ALA
SEQRES 32 A 479 LYS SER LEU SER ASP ARG PHE SER TYR VAL ALA PHE LYS
SEQRES 33 A 479 THR ASN ASP ARG ALA ALA ILE GLY ARG LEU LEU GLY ALA
SEQRES 34 A 479 SER SER LEU ILE ASN GLY MET PRO GLU GLU VAL VAL ALA
SEQRES 35 A 479 ALA ALA PHE ASN MET GLU ARG ASN GLU ALA ARG GLN LEU
SEQRES 36 A 479 LYS PHE ASN SER PRO PHE SER PHE LEU VAL PRO PRO ARG
SEQRES 37 A 479 SER ASP SER ASP ASN LYS ALA ALA ALA LEU GLU
SEQRES 1 B 479 SER LEU ARG ASP GLN PRO GLU GLN ASN GLU CYS GLN LEU
SEQRES 2 B 479 GLU HIS LEU ASN ALA LEU GLU PRO ASP ASN ARG ILE LYS
SEQRES 3 B 479 SER GLU GLY GLY LEU ILE GLU THR TRP ASN PRO SER ASN
SEQRES 4 B 479 LYS GLN PHE ARG CYS ALA GLY VAL ALA LEU SER ARG ALA
SEQRES 5 B 479 THR LEU GLN PRO ASN SER LEU ARG ARG PRO PHE TYR THR
SEQRES 6 B 479 ASN ALA PRO GLN GLU ILE PHE ILE GLN GLN GLY ASN GLY
SEQRES 7 B 479 TYR PHE GLY MET VAL PHE PRO GLY CYS VAL GLU THR PHE
SEQRES 8 B 479 GLU GLU PRO ARG GLU SER GLU GLN GLY GLU GLY SER LYS
SEQRES 9 B 479 PHE ARG ASP SER HIS GLN LYS VAL ASN ARG PHE ARG GLU
SEQRES 10 B 479 GLY ASP ILE ILE ALA VAL PRO THR GLY VAL VAL PHE TRP
SEQRES 11 B 479 MET PHE ASN ASP GLN ASP THR PRO VAL ILE ALA VAL SER
SEQRES 12 B 479 LEU ILE ASP THR SER SER PHE GLN ASN GLN LEU ASP GLN
SEQRES 13 B 479 MET PRO ARG ARG PHE TYR LEU ALA GLY ASN HIS GLU GLN
SEQRES 14 B 479 GLU PHE LEU ARG TYR GLN GLN GLU GLY SER GLU GLU GLU
SEQRES 15 B 479 GLU ASN GLU GLY GLY ASN ILE PHE SER GLY PHE LYS ARG
SEQRES 16 B 479 ASP PHE LEU GLU ASP ALA LEU ASN VAL ASN ARG ARG ILE
SEQRES 17 B 479 VAL ASN LYS LEU GLN GLY ARG ASN GLU ASP GLU GLU LYS
SEQRES 18 B 479 GLY ALA ILE VAL LYS VAL LYS GLY GLY LEU SER ILE ILE
SEQRES 19 B 479 THR PRO PRO GLU LYS GLU PRO ARG GLN LYS ARG GLY SER
SEQRES 20 B 479 ARG GLN GLU GLU ASP GLU ASP GLU ASP GLU LYS ARG GLN
SEQRES 21 B 479 PRO HIS ARG HIS SER ARG GLN ASP GLU ASP GLU ASP GLU
SEQRES 22 B 479 LYS ARG GLN PRO ARG ARG HIS SER ARG GLY GLY SER LYS
SEQRES 23 B 479 SER GLN ARG ASP ASN GLY PHE GLU GLU THR ILE CYS THR
SEQRES 24 B 479 ALA ARG LEU HIS GLN ASN ILE GLY SER SER SER SER PRO
SEQRES 25 B 479 ASP ILE TYR ASN PRO GLN ALA GLY ARG ILE LYS THR VAL
SEQRES 26 B 479 THR SER PHE ASP LEU PRO ALA LEU ARG PHE LEU LYS LEU
SEQRES 27 B 479 SER ALA GLU PHE GLY SER LEU HIS LYS ASN ALA MET PHE
SEQRES 28 B 479 VAL PRO HIS TYR ASN LEU ASN ALA ASN SER ILE LEU TYR
SEQRES 29 B 479 ALA LEU LYS GLY ARG ALA ARG LEU GLN ILE VAL ASN CYS
SEQRES 30 B 479 LYS GLY ASN SER VAL PHE ASP GLY GLU LEU GLU ALA GLY
SEQRES 31 B 479 ARG ALA LEU ILE VAL PRO GLN ASN PHE ALA ILE ALA ALA
SEQRES 32 B 479 LYS SER LEU SER ASP ARG PHE SER TYR VAL ALA PHE LYS
SEQRES 33 B 479 THR ASN ASP ARG ALA ALA ILE GLY ARG LEU LEU GLY ALA
SEQRES 34 B 479 SER SER LEU ILE ASN GLY MET PRO GLU GLU VAL VAL ALA
SEQRES 35 B 479 ALA ALA PHE ASN MET GLU ARG ASN GLU ALA ARG GLN LEU
SEQRES 36 B 479 LYS PHE ASN SER PRO PHE SER PHE LEU VAL PRO PRO ARG
SEQRES 37 B 479 SER ASP SER ASP ASN LYS ALA ALA ALA LEU GLU
SEQRES 1 C 479 SER LEU ARG ASP GLN PRO GLU GLN ASN GLU CYS GLN LEU
SEQRES 2 C 479 GLU HIS LEU ASN ALA LEU GLU PRO ASP ASN ARG ILE LYS
SEQRES 3 C 479 SER GLU GLY GLY LEU ILE GLU THR TRP ASN PRO SER ASN
SEQRES 4 C 479 LYS GLN PHE ARG CYS ALA GLY VAL ALA LEU SER ARG ALA
SEQRES 5 C 479 THR LEU GLN PRO ASN SER LEU ARG ARG PRO PHE TYR THR
SEQRES 6 C 479 ASN ALA PRO GLN GLU ILE PHE ILE GLN GLN GLY ASN GLY
SEQRES 7 C 479 TYR PHE GLY MET VAL PHE PRO GLY CYS VAL GLU THR PHE
SEQRES 8 C 479 GLU GLU PRO ARG GLU SER GLU GLN GLY GLU GLY SER LYS
SEQRES 9 C 479 PHE ARG ASP SER HIS GLN LYS VAL ASN ARG PHE ARG GLU
SEQRES 10 C 479 GLY ASP ILE ILE ALA VAL PRO THR GLY VAL VAL PHE TRP
SEQRES 11 C 479 MET PHE ASN ASP GLN ASP THR PRO VAL ILE ALA VAL SER
SEQRES 12 C 479 LEU ILE ASP THR SER SER PHE GLN ASN GLN LEU ASP GLN
SEQRES 13 C 479 MET PRO ARG ARG PHE TYR LEU ALA GLY ASN HIS GLU GLN
SEQRES 14 C 479 GLU PHE LEU ARG TYR GLN GLN GLU GLY SER GLU GLU GLU
SEQRES 15 C 479 GLU ASN GLU GLY GLY ASN ILE PHE SER GLY PHE LYS ARG
SEQRES 16 C 479 ASP PHE LEU GLU ASP ALA LEU ASN VAL ASN ARG ARG ILE
SEQRES 17 C 479 VAL ASN LYS LEU GLN GLY ARG ASN GLU ASP GLU GLU LYS
SEQRES 18 C 479 GLY ALA ILE VAL LYS VAL LYS GLY GLY LEU SER ILE ILE
SEQRES 19 C 479 THR PRO PRO GLU LYS GLU PRO ARG GLN LYS ARG GLY SER
SEQRES 20 C 479 ARG GLN GLU GLU ASP GLU ASP GLU ASP GLU LYS ARG GLN
SEQRES 21 C 479 PRO HIS ARG HIS SER ARG GLN ASP GLU ASP GLU ASP GLU
SEQRES 22 C 479 LYS ARG GLN PRO ARG ARG HIS SER ARG GLY GLY SER LYS
SEQRES 23 C 479 SER GLN ARG ASP ASN GLY PHE GLU GLU THR ILE CYS THR
SEQRES 24 C 479 ALA ARG LEU HIS GLN ASN ILE GLY SER SER SER SER PRO
SEQRES 25 C 479 ASP ILE TYR ASN PRO GLN ALA GLY ARG ILE LYS THR VAL
SEQRES 26 C 479 THR SER PHE ASP LEU PRO ALA LEU ARG PHE LEU LYS LEU
SEQRES 27 C 479 SER ALA GLU PHE GLY SER LEU HIS LYS ASN ALA MET PHE
SEQRES 28 C 479 VAL PRO HIS TYR ASN LEU ASN ALA ASN SER ILE LEU TYR
SEQRES 29 C 479 ALA LEU LYS GLY ARG ALA ARG LEU GLN ILE VAL ASN CYS
SEQRES 30 C 479 LYS GLY ASN SER VAL PHE ASP GLY GLU LEU GLU ALA GLY
SEQRES 31 C 479 ARG ALA LEU ILE VAL PRO GLN ASN PHE ALA ILE ALA ALA
SEQRES 32 C 479 LYS SER LEU SER ASP ARG PHE SER TYR VAL ALA PHE LYS
SEQRES 33 C 479 THR ASN ASP ARG ALA ALA ILE GLY ARG LEU LEU GLY ALA
SEQRES 34 C 479 SER SER LEU ILE ASN GLY MET PRO GLU GLU VAL VAL ALA
SEQRES 35 C 479 ALA ALA PHE ASN MET GLU ARG ASN GLU ALA ARG GLN LEU
SEQRES 36 C 479 LYS PHE ASN SER PRO PHE SER PHE LEU VAL PRO PRO ARG
SEQRES 37 C 479 SER ASP SER ASP ASN LYS ALA ALA ALA LEU GLU
FORMUL 4 HOH *78(H2 O)
HELIX 1 AA1 ASN A 59 GLY A 66 1 8
HELIX 2 AA2 LYS A 214 ASN A 223 1 10
HELIX 3 AA3 ASN A 225 GLY A 234 1 10
HELIX 4 AA4 PRO A 351 LYS A 357 1 7
HELIX 5 AA5 PRO A 457 ASN A 466 1 10
HELIX 6 AA6 GLU A 468 ASN A 478 1 11
HELIX 7 AA7 ASN B 59 GLY B 66 1 8
HELIX 8 AA8 LYS B 214 ASN B 223 1 10
HELIX 9 AA9 ASN B 225 GLY B 234 1 10
HELIX 10 AB1 PRO B 351 LYS B 357 1 7
HELIX 11 AB2 PRO B 457 ASN B 466 1 10
HELIX 12 AB3 GLU B 468 ASN B 478 1 11
HELIX 13 AB4 ASN C 59 GLY C 66 1 8
HELIX 14 AB5 LYS C 214 ASN C 223 1 10
HELIX 15 AB6 ASN C 225 GLN C 233 1 9
HELIX 16 AB7 ALA C 352 LYS C 357 1 6
HELIX 17 AB8 PRO C 457 ASN C 466 1 10
HELIX 18 AB9 GLU C 468 ASN C 478 1 11
SHEET 1 AA1 7 ASN A 43 SER A 47 0
SHEET 2 AA1 7 GLY A 50 THR A 54 -1 O GLY A 50 N SER A 47
SHEET 3 AA1 7 ALA A 68 LEU A 74 -1 O THR A 73 N LEU A 51
SHEET 4 AA1 7 VAL A 159 ILE A 165 -1 O ILE A 165 N ALA A 68
SHEET 5 AA1 7 GLN A 89 GLN A 95 -1 N PHE A 92 O VAL A 162
SHEET 6 AA1 7 ASP A 139 VAL A 143 -1 O ILE A 141 N ILE A 91
SHEET 7 AA1 7 HIS A 323 ASN A 325 -1 O GLN A 324 N ILE A 140
SHEET 1 AA2 5 ASN A 133 PHE A 135 0
SHEET 2 AA2 5 GLY A 98 VAL A 103 -1 N PHE A 100 O ASN A 133
SHEET 3 AA2 5 VAL A 148 ASN A 153 -1 O PHE A 152 N TYR A 99
SHEET 4 AA2 5 SER A 78 TYR A 84 -1 N ARG A 80 O MET A 151
SHEET 5 AA2 5 PHE A 181 TYR A 182 -1 O PHE A 181 N TYR A 84
SHEET 1 AA3 5 ASN A 133 PHE A 135 0
SHEET 2 AA3 5 GLY A 98 VAL A 103 -1 N PHE A 100 O ASN A 133
SHEET 3 AA3 5 VAL A 148 ASN A 153 -1 O PHE A 152 N TYR A 99
SHEET 4 AA3 5 SER A 78 TYR A 84 -1 N ARG A 80 O MET A 151
SHEET 5 AA3 5 ILE A 244 LYS A 246 -1 O VAL A 245 N LEU A 79
SHEET 1 AA4 2 PHE A 111 GLU A 113 0
SHEET 2 AA4 2 ASP A 127 HIS A 129 -1 O HIS A 129 N PHE A 111
SHEET 1 AA5 6 ILE A 334 ASN A 336 0
SHEET 2 AA5 6 GLY A 340 VAL A 345 -1 O GLY A 340 N ASN A 336
SHEET 3 AA5 6 SER A 359 HIS A 366 -1 O PHE A 362 N LYS A 343
SHEET 4 AA5 6 ARG A 429 LYS A 436 -1 O PHE A 430 N LEU A 365
SHEET 5 AA5 6 SER A 381 LYS A 387 -1 N ILE A 382 O PHE A 435
SHEET 6 AA5 6 ALA A 412 VAL A 415 -1 O LEU A 413 N LEU A 383
SHEET 1 AA6 5 SER A 401 GLU A 408 0
SHEET 2 AA6 5 ARG A 389 VAL A 395 -1 N LEU A 392 O GLY A 405
SHEET 3 AA6 5 ALA A 420 SER A 425 -1 O LYS A 424 N ARG A 391
SHEET 4 AA6 5 MET A 370 ASN A 376 -1 N HIS A 374 O ILE A 421
SHEET 5 AA6 5 ILE A 443 ARG A 445 -1 O GLY A 444 N TYR A 375
SHEET 1 AA7 5 SER A 401 GLU A 408 0
SHEET 2 AA7 5 ARG A 389 VAL A 395 -1 N LEU A 392 O GLY A 405
SHEET 3 AA7 5 ALA A 420 SER A 425 -1 O LYS A 424 N ARG A 391
SHEET 4 AA7 5 MET A 370 ASN A 376 -1 N HIS A 374 O ILE A 421
SHEET 5 AA7 5 LEU A 484 VAL A 485 -1 O VAL A 485 N MET A 370
SHEET 1 AA8 7 ASN B 43 SER B 47 0
SHEET 2 AA8 7 GLY B 50 THR B 54 -1 O GLY B 50 N SER B 47
SHEET 3 AA8 7 ALA B 68 LEU B 74 -1 O THR B 73 N LEU B 51
SHEET 4 AA8 7 VAL B 159 ILE B 165 -1 O ILE B 165 N ALA B 68
SHEET 5 AA8 7 GLN B 89 GLN B 95 -1 N PHE B 92 O VAL B 162
SHEET 6 AA8 7 ASP B 139 VAL B 143 -1 O ILE B 141 N ILE B 91
SHEET 7 AA8 7 HIS B 323 ASN B 325 -1 O GLN B 324 N ILE B 140
SHEET 1 AA9 5 VAL B 132 ARG B 136 0
SHEET 2 AA9 5 ASN B 97 VAL B 103 -1 N PHE B 100 O ASN B 133
SHEET 3 AA9 5 VAL B 148 ASN B 153 -1 O PHE B 152 N TYR B 99
SHEET 4 AA9 5 SER B 78 THR B 85 -1 N ARG B 80 O MET B 151
SHEET 5 AA9 5 ARG B 180 TYR B 182 -1 O PHE B 181 N TYR B 84
SHEET 1 AB1 5 VAL B 132 ARG B 136 0
SHEET 2 AB1 5 ASN B 97 VAL B 103 -1 N PHE B 100 O ASN B 133
SHEET 3 AB1 5 VAL B 148 ASN B 153 -1 O PHE B 152 N TYR B 99
SHEET 4 AB1 5 SER B 78 THR B 85 -1 N ARG B 80 O MET B 151
SHEET 5 AB1 5 ILE B 244 LYS B 246 -1 O VAL B 245 N LEU B 79
SHEET 1 AB2 2 PHE B 111 GLU B 113 0
SHEET 2 AB2 2 ASP B 127 HIS B 129 -1 O HIS B 129 N PHE B 111
SHEET 1 AB3 6 ILE B 334 ASN B 336 0
SHEET 2 AB3 6 GLY B 340 VAL B 345 -1 O GLY B 340 N ASN B 336
SHEET 3 AB3 6 SER B 359 HIS B 366 -1 O PHE B 362 N LYS B 343
SHEET 4 AB3 6 ARG B 429 LYS B 436 -1 O PHE B 430 N LEU B 365
SHEET 5 AB3 6 SER B 381 LYS B 387 -1 N ILE B 382 O PHE B 435
SHEET 6 AB3 6 ALA B 412 VAL B 415 -1 O LEU B 413 N LEU B 383
SHEET 1 AB4 5 SER B 401 GLU B 408 0
SHEET 2 AB4 5 ARG B 389 VAL B 395 -1 N LEU B 392 O GLY B 405
SHEET 3 AB4 5 ALA B 420 SER B 425 -1 O LYS B 424 N ARG B 391
SHEET 4 AB4 5 MET B 370 ASN B 376 -1 N HIS B 374 O ILE B 421
SHEET 5 AB4 5 ILE B 443 ARG B 445 -1 O GLY B 444 N TYR B 375
SHEET 1 AB5 5 SER B 401 GLU B 408 0
SHEET 2 AB5 5 ARG B 389 VAL B 395 -1 N LEU B 392 O GLY B 405
SHEET 3 AB5 5 ALA B 420 SER B 425 -1 O LYS B 424 N ARG B 391
SHEET 4 AB5 5 MET B 370 ASN B 376 -1 N HIS B 374 O ILE B 421
SHEET 5 AB5 5 LEU B 484 VAL B 485 -1 O VAL B 485 N MET B 370
SHEET 1 AB6 7 ASN C 43 SER C 47 0
SHEET 2 AB6 7 GLY C 50 THR C 54 -1 O GLY C 50 N SER C 47
SHEET 3 AB6 7 ALA C 68 LEU C 74 -1 O ARG C 71 N GLU C 53
SHEET 4 AB6 7 VAL C 159 ILE C 165 -1 O ALA C 161 N ALA C 72
SHEET 5 AB6 7 GLN C 89 GLN C 95 -1 N PHE C 92 O VAL C 162
SHEET 6 AB6 7 ASP C 139 VAL C 143 -1 O ILE C 141 N ILE C 91
SHEET 7 AB6 7 HIS C 323 ASN C 325 -1 O GLN C 324 N ILE C 140
SHEET 1 AB7 5 VAL C 132 PHE C 135 0
SHEET 2 AB7 5 GLY C 98 VAL C 103 -1 N GLY C 98 O PHE C 135
SHEET 3 AB7 5 VAL C 148 ASN C 153 -1 O PHE C 152 N TYR C 99
SHEET 4 AB7 5 SER C 78 THR C 85 -1 N ARG C 80 O MET C 151
SHEET 5 AB7 5 ARG C 180 TYR C 182 -1 O PHE C 181 N TYR C 84
SHEET 1 AB8 5 VAL C 132 PHE C 135 0
SHEET 2 AB8 5 GLY C 98 VAL C 103 -1 N GLY C 98 O PHE C 135
SHEET 3 AB8 5 VAL C 148 ASN C 153 -1 O PHE C 152 N TYR C 99
SHEET 4 AB8 5 SER C 78 THR C 85 -1 N ARG C 80 O MET C 151
SHEET 5 AB8 5 ILE C 244 LYS C 246 -1 O VAL C 245 N LEU C 79
SHEET 1 AB9 2 PHE C 111 GLU C 113 0
SHEET 2 AB9 2 ASP C 127 HIS C 129 -1 O HIS C 129 N PHE C 111
SHEET 1 AC1 6 ILE C 334 ASN C 336 0
SHEET 2 AC1 6 GLY C 340 VAL C 345 -1 O GLY C 340 N ASN C 336
SHEET 3 AC1 6 SER C 359 HIS C 366 -1 O PHE C 362 N LYS C 343
SHEET 4 AC1 6 ARG C 429 LYS C 436 -1 O PHE C 430 N LEU C 365
SHEET 5 AC1 6 SER C 381 LYS C 387 -1 N ILE C 382 O PHE C 435
SHEET 6 AC1 6 ALA C 412 VAL C 415 -1 O LEU C 413 N LEU C 383
SHEET 1 AC2 5 SER C 401 GLU C 408 0
SHEET 2 AC2 5 ARG C 389 VAL C 395 -1 N ILE C 394 O VAL C 402
SHEET 3 AC2 5 ALA C 420 SER C 425 -1 O LYS C 424 N ARG C 391
SHEET 4 AC2 5 MET C 370 ASN C 376 -1 N HIS C 374 O ILE C 421
SHEET 5 AC2 5 ILE C 443 ARG C 445 -1 O GLY C 444 N TYR C 375
SHEET 1 AC3 5 SER C 401 GLU C 408 0
SHEET 2 AC3 5 ARG C 389 VAL C 395 -1 N ILE C 394 O VAL C 402
SHEET 3 AC3 5 ALA C 420 SER C 425 -1 O LYS C 424 N ARG C 391
SHEET 4 AC3 5 MET C 370 ASN C 376 -1 N HIS C 374 O ILE C 421
SHEET 5 AC3 5 LEU C 484 VAL C 485 -1 O VAL C 485 N MET C 370
SSBOND 1 CYS A 31 CYS A 64 1555 1555 2.04
SSBOND 2 CYS A 107 CYS A 318 1555 1555 2.03
SSBOND 3 CYS B 31 CYS B 64 1555 1555 2.04
SSBOND 4 CYS B 107 CYS B 318 1555 1555 2.03
SSBOND 5 CYS C 31 CYS C 64 1555 1555 2.04
SSBOND 6 CYS C 107 CYS C 318 1555 1555 2.03
CRYST1 97.370 100.610 131.124 90.00 96.10 90.00 I 1 2 1 12
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 0.010270 0.000000 0.001097 0.00000
SCALE2 0.000000 0.009939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007670 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
