HEADER PROTEIN BINDING 27-JUL-16 5GOI
TITLE LYS48-LINKED DI-UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: D-UBIQUITIN;
COMPND 7 CHAIN: C, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_TAXID: 9606
KEYWDS POLYUBIQUITIN CHAINS, QUASI-RACEMIC CRYSTAL, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GAO,M.PAN,Y.ZHENG,L.LIU
REVDAT 5 15-NOV-23 5GOI 1 REMARK
REVDAT 4 08-NOV-23 5GOI 1 REMARK
REVDAT 3 09-FEB-22 5GOI 1 REMARK LINK
REVDAT 2 16-NOV-16 5GOI 1 JRNL
REVDAT 1 02-NOV-16 5GOI 0
JRNL AUTH S.GAO,M.PAN,Y.ZHENG,Y.HUANG,Q.ZHENG,D.SUN,L.LU,X.TAN,X.TAN,
JRNL AUTH 2 H.LAN,J.WANG,T.WANG,J.WANG,L.LIU
JRNL TITL MONOMER/OLIGOMER QUASI-RACEMIC PROTEIN CRYSTALLOGRAPHY
JRNL REF J.AM.CHEM.SOC. V. 138 14497 2016
JRNL REFN ESSN 1520-5126
JRNL PMID 27768314
JRNL DOI 10.1021/JACS.6B09545
REMARK 2
REMARK 2 RESOLUTION. 1.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.2
REMARK 3 NUMBER OF REFLECTIONS : 23422
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.267
REMARK 3 R VALUE (WORKING SET) : 0.264
REMARK 3 FREE R VALUE : 0.311
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.840
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
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 38.3622 - 3.1865 0.91 3092 146 0.2210 0.2552
REMARK 3 2 3.1865 - 2.5294 0.93 3141 173 0.2632 0.3293
REMARK 3 3 2.5294 - 2.2097 0.94 3196 158 0.2724 0.3369
REMARK 3 4 2.2097 - 2.0077 0.94 3179 171 0.2810 0.3306
REMARK 3 5 2.0077 - 1.8638 0.95 3168 154 0.3107 0.3456
REMARK 3 6 1.8638 - 1.7539 0.92 3143 161 0.3227 0.3727
REMARK 3 7 1.7539 - 1.6661 0.58 1990 93 0.3519 0.3553
REMARK 3 8 1.6661 - 1.5935 0.41 1379 78 0.3444 0.3693
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.660
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 2432
REMARK 3 ANGLE : 0.783 3271
REMARK 3 CHIRALITY : 0.053 389
REMARK 3 PLANARITY : 0.003 421
REMARK 3 DIHEDRAL : 18.279 1245
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2690 7.8524 21.0567
REMARK 3 T TENSOR
REMARK 3 T11: 0.2981 T22: 0.1714
REMARK 3 T33: 0.2282 T12: -0.0509
REMARK 3 T13: 0.1254 T23: -0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 0.0719 L22: 0.0079
REMARK 3 L33: 0.1132 L12: -0.0224
REMARK 3 L13: 0.0889 L23: -0.0282
REMARK 3 S TENSOR
REMARK 3 S11: 0.1243 S12: -0.0399 S13: 0.1131
REMARK 3 S21: -0.0131 S22: 0.0560 S23: -0.0048
REMARK 3 S31: -0.0774 S32: 0.0013 S33: 0.0823
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1524 9.5458 22.5753
REMARK 3 T TENSOR
REMARK 3 T11: 0.2026 T22: 0.2290
REMARK 3 T33: 0.2209 T12: -0.0328
REMARK 3 T13: 0.0151 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0210
REMARK 3 L33: 0.0752 L12: -0.0035
REMARK 3 L13: -0.0057 L23: 0.0352
REMARK 3 S TENSOR
REMARK 3 S11: 0.1124 S12: -0.0231 S13: -0.0071
REMARK 3 S21: 0.0640 S22: 0.0035 S23: -0.1359
REMARK 3 S31: -0.0310 S32: 0.0184 S33: 0.0143
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 35 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2114 2.8376 15.8387
REMARK 3 T TENSOR
REMARK 3 T11: 0.1988 T22: 0.2263
REMARK 3 T33: 0.1545 T12: 0.0346
REMARK 3 T13: 0.0451 T23: 0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 0.0181 L22: 0.0199
REMARK 3 L33: 0.0039 L12: -0.0061
REMARK 3 L13: -0.0163 L23: 0.0060
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: -0.0480 S13: 0.0561
REMARK 3 S21: -0.0325 S22: -0.1080 S23: -0.0544
REMARK 3 S31: 0.1017 S32: -0.0324 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 57 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3881 9.5470 13.3365
REMARK 3 T TENSOR
REMARK 3 T11: 0.3422 T22: 0.1764
REMARK 3 T33: 0.1865 T12: 0.0438
REMARK 3 T13: 0.0926 T23: 0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 0.0289 L22: 0.0284
REMARK 3 L33: 0.0185 L12: 0.0297
REMARK 3 L13: 0.0048 L23: -0.0095
REMARK 3 S TENSOR
REMARK 3 S11: 0.0590 S12: 0.0418 S13: 0.0273
REMARK 3 S21: -0.0215 S22: -0.0585 S23: 0.0612
REMARK 3 S31: -0.0817 S32: 0.0517 S33: -0.0177
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 72 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4556 -9.8031 20.6050
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.2393
REMARK 3 T33: 0.2394 T12: 0.0062
REMARK 3 T13: 0.0388 T23: 0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 0.0333 L22: 0.0668
REMARK 3 L33: 0.0155 L12: 0.0447
REMARK 3 L13: -0.0172 L23: -0.0152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.0279 S13: 0.0296
REMARK 3 S21: -0.0448 S22: 0.0050 S23: 0.0203
REMARK 3 S31: -0.0084 S32: -0.0382 S33: -0.0004
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7447 -5.2499 3.7904
REMARK 3 T TENSOR
REMARK 3 T11: 0.2772 T22: 0.1674
REMARK 3 T33: 0.2303 T12: -0.0096
REMARK 3 T13: -0.0257 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.0467 L22: 0.0191
REMARK 3 L33: 0.2177 L12: 0.0309
REMARK 3 L13: -0.0910 L23: -0.0592
REMARK 3 S TENSOR
REMARK 3 S11: 0.0566 S12: -0.0214 S13: -0.0078
REMARK 3 S21: 0.0110 S22: 0.1603 S23: -0.1539
REMARK 3 S31: 0.0319 S32: -0.1397 S33: 0.0242
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2887 -4.6164 6.6317
REMARK 3 T TENSOR
REMARK 3 T11: 0.0582 T22: 0.3289
REMARK 3 T33: 0.1994 T12: 0.1220
REMARK 3 T13: 0.0040 T23: 0.0826
REMARK 3 L TENSOR
REMARK 3 L11: 0.0039 L22: 0.0302
REMARK 3 L33: 0.0009 L12: 0.0099
REMARK 3 L13: -0.0020 L23: -0.0059
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.0134 S13: -0.0241
REMARK 3 S21: -0.0023 S22: -0.0062 S23: 0.0304
REMARK 3 S31: 0.0075 S32: -0.0314 S33: -0.0104
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2687 -14.6774 1.2940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1738 T22: 0.1648
REMARK 3 T33: 0.2023 T12: 0.0095
REMARK 3 T13: -0.0815 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.0119 L22: 0.0327
REMARK 3 L33: 0.0271 L12: 0.0079
REMARK 3 L13: 0.0141 L23: 0.0295
REMARK 3 S TENSOR
REMARK 3 S11: -0.0301 S12: 0.1287 S13: 0.0528
REMARK 3 S21: -0.0347 S22: -0.0032 S23: 0.0045
REMARK 3 S31: 0.0071 S32: -0.0390 S33: -0.0397
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0223 -12.8221 13.7959
REMARK 3 T TENSOR
REMARK 3 T11: 0.1161 T22: 0.2286
REMARK 3 T33: 0.1752 T12: -0.0603
REMARK 3 T13: -0.0583 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 0.0885 L22: 0.0393
REMARK 3 L33: 0.0208 L12: -0.0161
REMARK 3 L13: -0.0274 L23: 0.0254
REMARK 3 S TENSOR
REMARK 3 S11: -0.0142 S12: -0.0306 S13: -0.0592
REMARK 3 S21: 0.0662 S22: -0.0259 S23: 0.0159
REMARK 3 S31: 0.0107 S32: 0.0407 S33: -0.0673
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 57 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4874 -2.6925 13.4164
REMARK 3 T TENSOR
REMARK 3 T11: 0.0352 T22: 0.2404
REMARK 3 T33: 0.1797 T12: -0.0533
REMARK 3 T13: -0.0512 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 0.0103 L22: 0.0036
REMARK 3 L33: 0.0120 L12: -0.0030
REMARK 3 L13: 0.0049 L23: 0.0012
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: -0.0258 S13: -0.0343
REMARK 3 S21: 0.0029 S22: 0.0335 S23: 0.0147
REMARK 3 S31: -0.0352 S32: -0.0153 S33: -0.0021
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 66 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9601 -18.7425 6.2328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1827 T22: 0.1817
REMARK 3 T33: 0.1585 T12: -0.0102
REMARK 3 T13: 0.0001 T23: -0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 0.0939 L22: 0.0158
REMARK 3 L33: 0.1002 L12: -0.0173
REMARK 3 L13: 0.0629 L23: -0.0338
REMARK 3 S TENSOR
REMARK 3 S11: -0.0725 S12: 0.0294 S13: 0.0059
REMARK 3 S21: 0.0045 S22: -0.0342 S23: 0.0230
REMARK 3 S31: 0.0172 S32: -0.0683 S33: -0.0797
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 10 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3973 11.4625 -6.5215
REMARK 3 T TENSOR
REMARK 3 T11: 0.3105 T22: -0.1547
REMARK 3 T33: -0.1285 T12: 0.2268
REMARK 3 T13: 0.2626 T23: -0.2854
REMARK 3 L TENSOR
REMARK 3 L11: 0.1819 L22: 0.1493
REMARK 3 L33: 0.0508 L12: 0.1200
REMARK 3 L13: 0.0621 L23: 0.0189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 0.0726 S13: -0.1542
REMARK 3 S21: -0.0586 S22: 0.0765 S23: -0.2171
REMARK 3 S31: -0.0768 S32: -0.0522 S33: 0.0796
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 10 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5128 -5.8367 -18.1573
REMARK 3 T TENSOR
REMARK 3 T11: 0.2163 T22: 0.1203
REMARK 3 T33: 0.1620 T12: -0.0051
REMARK 3 T13: 0.0261 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.1738 L22: 0.0480
REMARK 3 L33: 0.0146 L12: 0.0350
REMARK 3 L13: -0.0089 L23: -0.0092
REMARK 3 S TENSOR
REMARK 3 S11: -0.0211 S12: 0.0837 S13: -0.1137
REMARK 3 S21: 0.0422 S22: 0.0933 S23: -0.0245
REMARK 3 S31: 0.0882 S32: -0.0887 S33: 0.0153
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 5GOI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1300001145.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-E
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23441
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.594
REMARK 200 RESOLUTION RANGE LOW (A) : 38.351
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.0
REMARK 200 DATA REDUNDANCY : 1.690
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 1.62
REMARK 200 R MERGE FOR SHELL (I) : 1.08600
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: NULL
REMARK 200 STARTING MODEL: 1UBQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 23.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE TRIBASIC DEHYDRATE
REMARK 280 PH5.6, 20% 2-PROPANOL, 20%PEG 4000, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR B 12 O HOH B 101 1.90
REMARK 500 ND1 DHI C 68 O HOH C 201 1.92
REMARK 500 O HOH C 245 O HOH C 252 1.97
REMARK 500 O HOH A 104 O HOH B 145 2.02
REMARK 500 O HOH A 139 O HOH A 142 2.06
REMARK 500 OE2 DGL C 51 O HOH C 202 2.06
REMARK 500 O HOH A 145 O HOH A 148 2.13
REMARK 500 O HOH D 131 O HOH D 138 2.13
REMARK 500 OE2 GLU B 24 O HOH B 102 2.15
REMARK 500 O HOH C 244 O HOH D 149 2.16
REMARK 500 NZ LYS B 48 O HOH B 103 2.17
REMARK 500 NZ LYS B 6 O HOH B 104 2.17
REMARK 500 O HOH B 134 O HOH B 149 2.18
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 O HOH A 114 O HOH D 111 1666 1.86
REMARK 500 O HOH A 138 O HOH D 123 1556 1.88
REMARK 500 O HOH A 147 O HOH A 155 1455 1.93
REMARK 500 O HOH B 128 O HOH C 211 1545 1.96
REMARK 500 O HOH A 133 O HOH D 101 1666 2.05
REMARK 500 O HOH A 149 O HOH B 151 1565 2.05
REMARK 500 O HOH A 145 O HOH D 101 1666 2.12
REMARK 500 O HOH C 228 O HOH D 102 1565 2.16
REMARK 500 O HOH A 153 O HOH B 141 1455 2.18
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 GLN A 62 -169.52 -114.37
REMARK 500 DGN C 62 167.13 125.44
REMARK 500 DGL D 64 -16.55 -55.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GO7 RELATED DB: PDB
REMARK 900 RELATED ID: 5GO8 RELATED DB: PDB
REMARK 900 RELATED ID: 5GOB RELATED DB: PDB
REMARK 900 RELATED ID: 5GOC RELATED DB: PDB
REMARK 900 RELATED ID: 5GOD RELATED DB: PDB
REMARK 900 RELATED ID: 5GOG RELATED DB: PDB
REMARK 900 RELATED ID: 5GOH RELATED DB: PDB
REMARK 900 RELATED ID: 5GOJ RELATED DB: PDB
REMARK 900 RELATED ID: 5GOK RELATED DB: PDB
DBREF 5GOI A 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5GOI B 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5GOI C 1 76 PDB 5GOI 5GOI 1 76
DBREF 5GOI D 1 76 PDB 5GOI 5GOI 1 76
SEQRES 1 A 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 A 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 A 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 A 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 A 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 A 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 C 76 DNE DGN DIL DPN DVA DLY DTH DLE DTH GLY DLY DTH DIL
SEQRES 2 C 76 DTH DLE DGL DVA DGL DPR DSN DAS DTH DIL DGL DSG DVA
SEQRES 3 C 76 DLY DAL DLY DIL DGN DAS DLY DGL GLY DIL DPR DPR DAS
SEQRES 4 C 76 DGN DGN DAR DLE DIL DPN DAL GLY DLY DGN DLE DGL DAS
SEQRES 5 C 76 GLY DAR DTH DLE DSN DAS DTY DSG DIL DGN DLY DGL DSN
SEQRES 6 C 76 DTH DLE DHI DLE DVA DLE DAR DLE DAR GLY GLY
SEQRES 1 D 76 DNE DGN DIL DPN DVA DLY DTH DLE DTH GLY DLY DTH DIL
SEQRES 2 D 76 DTH DLE DGL DVA DGL DPR DSN DAS DTH DIL DGL DSG DVA
SEQRES 3 D 76 DLY DAL DLY DIL DGN DAS DLY DGL GLY DIL DPR DPR DAS
SEQRES 4 D 76 DGN DGN DAR DLE DIL DPN DAL GLY DLY DGN DLE DGL DAS
SEQRES 5 D 76 GLY DAR DTH DLE DSN DAS DTY DSG DIL DGN DLY DGL DSN
SEQRES 6 D 76 DTH DLE DHI DLE DVA DLE DAR DLE DAR GLY GLY
HET DNE C 1 8
HET DGN C 2 9
HET DIL C 3 8
HET DPN C 4 11
HET DVA C 5 7
HET DLY C 6 9
HET DTH C 7 7
HET DLE C 8 8
HET DTH C 9 7
HET DLY C 11 9
HET DTH C 12 7
HET DIL C 13 8
HET DTH C 14 7
HET DLE C 15 8
HET DGL C 16 9
HET DVA C 17 7
HET DGL C 18 9
HET DPR C 19 7
HET DSN C 20 6
HET DAS C 21 8
HET DTH C 22 7
HET DIL C 23 8
HET DGL C 24 9
HET DSG C 25 8
HET DVA C 26 7
HET DLY C 27 9
HET DAL C 28 5
HET DLY C 29 9
HET DIL C 30 8
HET DGN C 31 9
HET DAS C 32 8
HET DLY C 33 9
HET DGL C 34 9
HET DIL C 36 8
HET DPR C 37 7
HET DPR C 38 7
HET DAS C 39 8
HET DGN C 40 9
HET DGN C 41 9
HET DAR C 42 11
HET DLE C 43 8
HET DIL C 44 8
HET DPN C 45 11
HET DAL C 46 5
HET DLY C 48 9
HET DGN C 49 9
HET DLE C 50 8
HET DGL C 51 9
HET DAS C 52 8
HET DAR C 54 11
HET DTH C 55 7
HET DLE C 56 8
HET DSN C 57 6
HET DAS C 58 8
HET DTY C 59 12
HET DSG C 60 8
HET DIL C 61 8
HET DGN C 62 9
HET DLY C 63 9
HET DGL C 64 9
HET DSN C 65 6
HET DTH C 66 7
HET DLE C 67 8
HET DHI C 68 10
HET DLE C 69 8
HET DVA C 70 7
HET DLE C 71 8
HET DAR C 72 11
HET DLE C 73 8
HET DAR C 74 11
HET DNE D 1 8
HET DGN D 2 9
HET DIL D 3 8
HET DPN D 4 11
HET DVA D 5 7
HET DLY D 6 9
HET DTH D 7 7
HET DLE D 8 8
HET DTH D 9 7
HET DLY D 11 9
HET DTH D 12 7
HET DIL D 13 8
HET DTH D 14 7
HET DLE D 15 8
HET DGL D 16 9
HET DVA D 17 7
HET DGL D 18 9
HET DPR D 19 7
HET DSN D 20 6
HET DAS D 21 8
HET DTH D 22 7
HET DIL D 23 8
HET DGL D 24 9
HET DSG D 25 8
HET DVA D 26 7
HET DLY D 27 9
HET DAL D 28 5
HET DLY D 29 9
HET DIL D 30 8
HET DGN D 31 9
HET DAS D 32 8
HET DLY D 33 9
HET DGL D 34 9
HET DIL D 36 8
HET DPR D 37 7
HET DPR D 38 7
HET DAS D 39 8
HET DGN D 40 9
HET DGN D 41 9
HET DAR D 42 11
HET DLE D 43 8
HET DIL D 44 8
HET DPN D 45 11
HET DAL D 46 5
HET DLY D 48 9
HET DGN D 49 9
HET DLE D 50 8
HET DGL D 51 9
HET DAS D 52 8
HET DAR D 54 11
HET DTH D 55 7
HET DLE D 56 8
HET DSN D 57 6
HET DAS D 58 8
HET DTY D 59 12
HET DSG D 60 8
HET DIL D 61 8
HET DGN D 62 9
HET DLY D 63 9
HET DGL D 64 9
HET DSN D 65 6
HET DTH D 66 7
HET DLE D 67 8
HET DHI D 68 10
HET DLE D 69 8
HET DVA D 70 7
HET DLE D 71 8
HET DAR D 72 11
HET DLE D 73 8
HET DAR D 74 11
HETNAM DNE D-NORLEUCINE
HETNAM DGN D-GLUTAMINE
HETNAM DIL D-ISOLEUCINE
HETNAM DPN D-PHENYLALANINE
HETNAM DVA D-VALINE
HETNAM DLY D-LYSINE
HETNAM DTH D-THREONINE
HETNAM DLE D-LEUCINE
HETNAM DGL D-GLUTAMIC ACID
HETNAM DPR D-PROLINE
HETNAM DSN D-SERINE
HETNAM DAS D-ASPARTIC ACID
HETNAM DSG D-ASPARAGINE
HETNAM DAL D-ALANINE
HETNAM DAR D-ARGININE
HETNAM DTY D-TYROSINE
HETNAM DHI D-HISTIDINE
FORMUL 3 DNE 2(C6 H13 N O2)
FORMUL 3 DGN 12(C5 H10 N2 O3)
FORMUL 3 DIL 14(C6 H13 N O2)
FORMUL 3 DPN 4(C9 H11 N O2)
FORMUL 3 DVA 8(C5 H11 N O2)
FORMUL 3 DLY 14(C6 H14 N2 O2)
FORMUL 3 DTH 14(C4 H9 N O3)
FORMUL 3 DLE 18(C6 H13 N O2)
FORMUL 3 DGL 12(C5 H9 N O4)
FORMUL 3 DPR 6(C5 H9 N O2)
FORMUL 3 DSN 6(C3 H7 N O3)
FORMUL 3 DAS 10(C4 H7 N O4)
FORMUL 3 DSG 4(C4 H8 N2 O3)
FORMUL 3 DAL 4(C3 H7 N O2)
FORMUL 3 DAR 8(C6 H15 N4 O2 1+)
FORMUL 3 DTY 2(C9 H11 N O3)
FORMUL 3 DHI 2(C6 H10 N3 O2 1+)
FORMUL 5 HOH *221(H2 O)
HELIX 1 AA1 THR A 22 GLY A 35 1 14
HELIX 2 AA2 PRO A 37 ASP A 39 5 3
HELIX 3 AA3 LEU A 56 ASN A 60 5 5
HELIX 4 AA4 THR B 22 GLY B 35 1 14
HELIX 5 AA5 PRO B 37 ASP B 39 5 3
HELIX 6 AA6 LEU B 56 ASN B 60 5 5
HELIX 7 AA7 DTH C 22 GLY C 35 1 14
HELIX 8 AA8 DPR C 37 DAS C 39 5 3
HELIX 9 AA9 DTH C 55 DSG C 60 5 6
HELIX 10 AB1 DTH D 22 GLY D 35 1 14
HELIX 11 AB2 DPR D 37 DAS D 39 5 3
HELIX 12 AB3 DLE D 56 DSG D 60 5 5
SHEET 1 AA1 5 THR A 12 GLU A 16 0
SHEET 2 AA1 5 GLN A 2 THR A 7 -1 N VAL A 5 O ILE A 13
SHEET 3 AA1 5 THR A 66 LEU A 71 1 O LEU A 69 N LYS A 6
SHEET 4 AA1 5 GLN A 41 PHE A 45 -1 N ARG A 42 O VAL A 70
SHEET 5 AA1 5 LYS A 48 GLN A 49 -1 O LYS A 48 N PHE A 45
SHEET 1 AA2 5 THR B 12 GLU B 16 0
SHEET 2 AA2 5 GLN B 2 THR B 7 -1 N VAL B 5 O ILE B 13
SHEET 3 AA2 5 THR B 66 LEU B 71 1 O LEU B 69 N LYS B 6
SHEET 4 AA2 5 GLN B 41 PHE B 45 -1 N ILE B 44 O HIS B 68
SHEET 5 AA2 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
SHEET 1 AA3 5 DTH C 12 DGL C 16 0
SHEET 2 AA3 5 DGN C 2 DLY C 6 -1 N DVA C 5 O DIL C 13
SHEET 3 AA3 5 DTH C 66 DLE C 71 1 O DLE C 67 N DPN C 4
SHEET 4 AA3 5 DGN C 41 DPN C 45 -1 N DIL C 44 O DHI C 68
SHEET 5 AA3 5 DLY C 48 DGN C 49 -1 O DLY C 48 N DPN C 45
SHEET 1 AA4 5 DTH D 12 DGL D 16 0
SHEET 2 AA4 5 DGN D 2 DTH D 7 -1 N DVA D 5 O DIL D 13
SHEET 3 AA4 5 DTH D 66 DLE D 71 1 O DLE D 67 N DPN D 4
SHEET 4 AA4 5 DGN D 41 DPN D 45 -1 N DIL D 44 O DHI D 68
SHEET 5 AA4 5 DLY D 48 DGN D 49 -1 O DLY D 48 N DPN D 45
LINK C DNE C 1 N DGN C 2 1555 1555 1.33
LINK C DGN C 2 N DIL C 3 1555 1555 1.33
LINK C DIL C 3 N DPN C 4 1555 1555 1.33
LINK C DPN C 4 N DVA C 5 1555 1555 1.33
LINK C DVA C 5 N DLY C 6 1555 1555 1.33
LINK C DLY C 6 N DTH C 7 1555 1555 1.33
LINK C DTH C 7 N DLE C 8 1555 1555 1.33
LINK C DLE C 8 N DTH C 9 1555 1555 1.33
LINK C DTH C 9 N GLY C 10 1555 1555 1.33
LINK C GLY C 10 N DLY C 11 1555 1555 1.33
LINK C DLY C 11 N DTH C 12 1555 1555 1.33
LINK C DTH C 12 N DIL C 13 1555 1555 1.33
LINK C DIL C 13 N DTH C 14 1555 1555 1.32
LINK C DTH C 14 N DLE C 15 1555 1555 1.33
LINK C DLE C 15 N DGL C 16 1555 1555 1.33
LINK C DGL C 16 N DVA C 17 1555 1555 1.33
LINK C DVA C 17 N DGL C 18 1555 1555 1.33
LINK C DGL C 18 N DPR C 19 1555 1555 1.34
LINK C DPR C 19 N DSN C 20 1555 1555 1.33
LINK C DSN C 20 N DAS C 21 1555 1555 1.33
LINK C DAS C 21 N DTH C 22 1555 1555 1.33
LINK C DTH C 22 N DIL C 23 1555 1555 1.33
LINK C DIL C 23 N DGL C 24 1555 1555 1.33
LINK C DGL C 24 N DSG C 25 1555 1555 1.33
LINK C DSG C 25 N DVA C 26 1555 1555 1.33
LINK C DVA C 26 N DLY C 27 1555 1555 1.33
LINK C DLY C 27 N DAL C 28 1555 1555 1.33
LINK C DAL C 28 N DLY C 29 1555 1555 1.33
LINK C DLY C 29 N DIL C 30 1555 1555 1.33
LINK C DIL C 30 N DGN C 31 1555 1555 1.33
LINK C DGN C 31 N DAS C 32 1555 1555 1.33
LINK C DAS C 32 N DLY C 33 1555 1555 1.33
LINK C DLY C 33 N DGL C 34 1555 1555 1.33
LINK C DGL C 34 N GLY C 35 1555 1555 1.33
LINK C GLY C 35 N DIL C 36 1555 1555 1.33
LINK C DIL C 36 N DPR C 37 1555 1555 1.34
LINK C DPR C 37 N DPR C 38 1555 1555 1.34
LINK C DPR C 38 N DAS C 39 1555 1555 1.33
LINK C DAS C 39 N DGN C 40 1555 1555 1.33
LINK C DGN C 40 N DGN C 41 1555 1555 1.33
LINK C DGN C 41 N DAR C 42 1555 1555 1.33
LINK C DAR C 42 N DLE C 43 1555 1555 1.33
LINK C DLE C 43 N DIL C 44 1555 1555 1.33
LINK C DIL C 44 N DPN C 45 1555 1555 1.32
LINK C DPN C 45 N DAL C 46 1555 1555 1.33
LINK C DAL C 46 N GLY C 47 1555 1555 1.33
LINK C GLY C 47 N DLY C 48 1555 1555 1.33
LINK C DLY C 48 N DGN C 49 1555 1555 1.33
LINK C DGN C 49 N DLE C 50 1555 1555 1.33
LINK C DLE C 50 N DGL C 51 1555 1555 1.33
LINK C DGL C 51 N DAS C 52 1555 1555 1.33
LINK C DAS C 52 N GLY C 53 1555 1555 1.33
LINK C GLY C 53 N DAR C 54 1555 1555 1.33
LINK C DAR C 54 N DTH C 55 1555 1555 1.32
LINK C DTH C 55 N DLE C 56 1555 1555 1.33
LINK C DLE C 56 N DSN C 57 1555 1555 1.33
LINK C DSN C 57 N DAS C 58 1555 1555 1.33
LINK C DAS C 58 N DTY C 59 1555 1555 1.33
LINK C DTY C 59 N DSG C 60 1555 1555 1.33
LINK C DSG C 60 N DIL C 61 1555 1555 1.33
LINK C DIL C 61 N DGN C 62 1555 1555 1.33
LINK C DGN C 62 N DLY C 63 1555 1555 1.33
LINK NE2 DGN C 62 CD DLY D 6 1555 1455 1.43
LINK C DLY C 63 N DGL C 64 1555 1555 1.33
LINK C DGL C 64 N DSN C 65 1555 1555 1.33
LINK C DSN C 65 N DTH C 66 1555 1555 1.33
LINK C DTH C 66 N DLE C 67 1555 1555 1.33
LINK C DLE C 67 N DHI C 68 1555 1555 1.33
LINK C DHI C 68 N DLE C 69 1555 1555 1.33
LINK C DLE C 69 N DVA C 70 1555 1555 1.33
LINK C DVA C 70 N DLE C 71 1555 1555 1.33
LINK C DLE C 71 N DAR C 72 1555 1555 1.33
LINK C DAR C 72 N DLE C 73 1555 1555 1.33
LINK C DLE C 73 N DAR C 74 1555 1555 1.33
LINK C DAR C 74 N GLY C 75 1555 1555 1.33
LINK C DNE D 1 N DGN D 2 1555 1555 1.33
LINK C DGN D 2 N DIL D 3 1555 1555 1.33
LINK C DIL D 3 N DPN D 4 1555 1555 1.33
LINK C DPN D 4 N DVA D 5 1555 1555 1.33
LINK C DVA D 5 N DLY D 6 1555 1555 1.33
LINK C DLY D 6 N DTH D 7 1555 1555 1.33
LINK C DTH D 7 N DLE D 8 1555 1555 1.33
LINK C DLE D 8 N DTH D 9 1555 1555 1.33
LINK C DTH D 9 N GLY D 10 1555 1555 1.33
LINK C GLY D 10 N DLY D 11 1555 1555 1.33
LINK C DLY D 11 N DTH D 12 1555 1555 1.33
LINK C DTH D 12 N DIL D 13 1555 1555 1.33
LINK C DIL D 13 N DTH D 14 1555 1555 1.33
LINK C DTH D 14 N DLE D 15 1555 1555 1.33
LINK C DLE D 15 N DGL D 16 1555 1555 1.33
LINK C DGL D 16 N DVA D 17 1555 1555 1.33
LINK C DVA D 17 N DGL D 18 1555 1555 1.33
LINK C DGL D 18 N DPR D 19 1555 1555 1.34
LINK C DPR D 19 N DSN D 20 1555 1555 1.33
LINK C DSN D 20 N DAS D 21 1555 1555 1.33
LINK C DAS D 21 N DTH D 22 1555 1555 1.33
LINK C DTH D 22 N DIL D 23 1555 1555 1.33
LINK C DIL D 23 N DGL D 24 1555 1555 1.33
LINK C DGL D 24 N DSG D 25 1555 1555 1.33
LINK C DSG D 25 N DVA D 26 1555 1555 1.33
LINK C DVA D 26 N DLY D 27 1555 1555 1.33
LINK C DLY D 27 N DAL D 28 1555 1555 1.33
LINK C DAL D 28 N DLY D 29 1555 1555 1.33
LINK C DLY D 29 N DIL D 30 1555 1555 1.33
LINK C DIL D 30 N DGN D 31 1555 1555 1.33
LINK C DGN D 31 N DAS D 32 1555 1555 1.33
LINK C DAS D 32 N DLY D 33 1555 1555 1.33
LINK C DLY D 33 N DGL D 34 1555 1555 1.33
LINK C DGL D 34 N GLY D 35 1555 1555 1.33
LINK C GLY D 35 N DIL D 36 1555 1555 1.33
LINK C DIL D 36 N DPR D 37 1555 1555 1.34
LINK C DPR D 37 N DPR D 38 1555 1555 1.34
LINK C DPR D 38 N DAS D 39 1555 1555 1.33
LINK C DAS D 39 N DGN D 40 1555 1555 1.33
LINK C DGN D 40 N DGN D 41 1555 1555 1.33
LINK C DGN D 41 N DAR D 42 1555 1555 1.33
LINK C DAR D 42 N DLE D 43 1555 1555 1.33
LINK C DLE D 43 N DIL D 44 1555 1555 1.33
LINK C DIL D 44 N DPN D 45 1555 1555 1.33
LINK C DPN D 45 N DAL D 46 1555 1555 1.33
LINK C DAL D 46 N GLY D 47 1555 1555 1.33
LINK C GLY D 47 N DLY D 48 1555 1555 1.33
LINK C DLY D 48 N DGN D 49 1555 1555 1.33
LINK C DGN D 49 N DLE D 50 1555 1555 1.33
LINK C DLE D 50 N DGL D 51 1555 1555 1.33
LINK C DGL D 51 N DAS D 52 1555 1555 1.33
LINK C DAS D 52 N GLY D 53 1555 1555 1.33
LINK C GLY D 53 N DAR D 54 1555 1555 1.33
LINK C DAR D 54 N DTH D 55 1555 1555 1.33
LINK C DTH D 55 N DLE D 56 1555 1555 1.33
LINK C DLE D 56 N DSN D 57 1555 1555 1.33
LINK C DSN D 57 N DAS D 58 1555 1555 1.33
LINK C DAS D 58 N DTY D 59 1555 1555 1.33
LINK C DTY D 59 N DSG D 60 1555 1555 1.33
LINK C DSG D 60 N DIL D 61 1555 1555 1.33
LINK C DIL D 61 N DGN D 62 1555 1555 1.33
LINK C DGN D 62 N DLY D 63 1555 1555 1.33
LINK C DLY D 63 N DGL D 64 1555 1555 1.33
LINK C DGL D 64 N DSN D 65 1555 1555 1.33
LINK C DSN D 65 N DTH D 66 1555 1555 1.33
LINK C DTH D 66 N DLE D 67 1555 1555 1.33
LINK C DLE D 67 N DHI D 68 1555 1555 1.33
LINK C DHI D 68 N DLE D 69 1555 1555 1.33
LINK C DLE D 69 N DVA D 70 1555 1555 1.33
LINK C DVA D 70 N DLE D 71 1555 1555 1.33
LINK C DLE D 71 N DAR D 72 1555 1555 1.33
LINK C DAR D 72 N DLE D 73 1555 1555 1.33
LINK C DLE D 73 N DAR D 74 1555 1555 1.33
LINK C DAR D 74 N GLY D 75 1555 1555 1.33
CISPEP 1 GLY B 75 GLY B 76 0 0.51
CRYST1 28.010 40.800 52.160 98.45 100.90 105.94 P 1 2
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 0.035702 0.010197 0.009230 0.00000
SCALE2 0.000000 0.025490 0.005492 0.00000
SCALE3 0.000000 0.000000 0.019972 0.00000
(ATOM LINES ARE NOT SHOWN.)
END