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HEADER HYDROLASE 30-JAN-13 4J0D
TITLE TANNIN ACYL HYDROLASE FROM LACTOBACILLUS PLANTARUM (CADMIUM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANNASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590;
SOURCE 4 GENE: TANLPL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TANNIN, HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.REN,M.WU,Q.WANG,X.PENG,H.WEN,Q.CHEN,W.J.MCKINSTRY
REVDAT 1 22-MAY-13 4J0D 0
JRNL AUTH B.REN,M.WU,Q.WANG,X.PENG,H.WEN,W.J.MCKINSTRY,Q.CHEN
JRNL TITL CRYSTAL STRUCTURE OF TANNASE FROM LACTOBACILLUS PLANTARUM
JRNL REF J.MOL.BIOL. 2013
JRNL REFN ESSN 1089-8638
JRNL PMID 23648840
JRNL DOI 10.1016/J.JMB.2013.04.032
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 109373
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.690
REMARK 3 FREE R VALUE TEST SET COUNT : 1849
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 20.0191 - 3.7544 0.98 8710 157 0.1559 0.1534
REMARK 3 2 3.7544 - 2.9832 0.98 8659 148 0.1388 0.1777
REMARK 3 3 2.9832 - 2.6070 0.97 8619 152 0.1374 0.1585
REMARK 3 4 2.6070 - 2.3690 0.97 8659 146 0.1268 0.1707
REMARK 3 5 2.3690 - 2.1995 0.97 8620 149 0.1284 0.1473
REMARK 3 6 2.1995 - 2.0699 0.97 8593 146 0.1277 0.1902
REMARK 3 7 2.0699 - 1.9664 0.96 8525 149 0.1329 0.1901
REMARK 3 8 1.9664 - 1.8808 0.96 8510 147 0.1326 0.1804
REMARK 3 9 1.8808 - 1.8085 0.96 8519 154 0.1407 0.1982
REMARK 3 10 1.8085 - 1.7461 0.95 8476 142 0.1552 0.1940
REMARK 3 11 1.7461 - 1.6915 0.95 8476 150 0.1635 0.2218
REMARK 3 12 1.6915 - 1.6432 0.83 7451 113 0.1880 0.2326
REMARK 3 13 1.6432 - 1.6000 0.64 5707 96 0.2359 0.2578
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.42
REMARK 3 B_SOL : 68.59
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.78550
REMARK 3 B22 (A**2) : -3.98410
REMARK 3 B33 (A**2) : 0.19850
REMARK 3 B12 (A**2) : 0.10050
REMARK 3 B13 (A**2) : 0.52440
REMARK 3 B23 (A**2) : -1.31310
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 : 0.019 7583
REMARK 3 ANGLE : 1.596 10311
REMARK 3 CHIRALITY : 0.112 1153
REMARK 3 PLANARITY : 0.008 1346
REMARK 3 DIHEDRAL : 13.771 2745
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4401 114.8576 87.5528
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.0223
REMARK 3 T33: 0.0892 T12: 0.0088
REMARK 3 T13: -0.0112 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.3674 L22: 1.0014
REMARK 3 L33: 1.3020 L12: -0.3672
REMARK 3 L13: 0.0154 L23: -0.0357
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: -0.0201 S13: 0.0749
REMARK 3 S21: 0.1700 S22: 0.0200 S23: -0.0448
REMARK 3 S31: -0.3990 S32: 0.0311 S33: 0.0083
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6680 106.1467 84.9272
REMARK 3 T TENSOR
REMARK 3 T11: 0.1744 T22: 0.0785
REMARK 3 T33: 0.0866 T12: 0.0234
REMARK 3 T13: -0.0121 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.5542 L22: 0.9107
REMARK 3 L33: 1.9464 L12: -0.0186
REMARK 3 L13: 0.2456 L23: -0.1599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: 0.0143 S13: 0.0887
REMARK 3 S21: 0.1042 S22: -0.0109 S23: 0.0048
REMARK 3 S31: -0.3430 S32: -0.1047 S33: 0.0550
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 128:229)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2521 98.3851 73.8774
REMARK 3 T TENSOR
REMARK 3 T11: 0.0812 T22: 0.0870
REMARK 3 T33: 0.0611 T12: 0.0128
REMARK 3 T13: -0.0002 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 0.1832 L22: 1.1118
REMARK 3 L33: 1.1995 L12: -0.0608
REMARK 3 L13: -0.0928 L23: 0.2411
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0471 S13: 0.0512
REMARK 3 S21: -0.0556 S22: -0.0420 S23: -0.0380
REMARK 3 S31: -0.1433 S32: 0.0795 S33: 0.0412
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 230:242)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2283 102.9172 75.6911
REMARK 3 T TENSOR
REMARK 3 T11: 0.2308 T22: 0.8438
REMARK 3 T33: 0.7823 T12: -0.0057
REMARK 3 T13: 0.0668 T23: -0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 4.3678 L22: 1.3650
REMARK 3 L33: 4.3857 L12: 0.7272
REMARK 3 L13: 2.3782 L23: -1.4334
REMARK 3 S TENSOR
REMARK 3 S11: -0.0738 S12: -0.6061 S13: 0.4516
REMARK 3 S21: 0.2112 S22: 0.0271 S23: -0.0014
REMARK 3 S31: -0.3878 S32: -0.0973 S33: 0.1325
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 243:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1581 80.6447 62.8756
REMARK 3 T TENSOR
REMARK 3 T11: 0.1561 T22: 0.1558
REMARK 3 T33: 0.0947 T12: 0.0305
REMARK 3 T13: 0.0086 T23: -0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 0.8116 L22: 1.5573
REMARK 3 L33: 1.8368 L12: 0.5714
REMARK 3 L13: -0.1341 L23: 0.0532
REMARK 3 S TENSOR
REMARK 3 S11: -0.1196 S12: -0.1954 S13: 0.1791
REMARK 3 S21: -0.0207 S22: 0.0089 S23: 0.1340
REMARK 3 S31: 0.0499 S32: -0.2442 S33: 0.0726
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3164 84.5031 71.4144
REMARK 3 T TENSOR
REMARK 3 T11: 0.1038 T22: 0.1041
REMARK 3 T33: 0.0629 T12: 0.0110
REMARK 3 T13: -0.0013 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.4590 L22: 0.7829
REMARK 3 L33: 1.1540 L12: 0.1191
REMARK 3 L13: -0.0175 L23: -0.0220
REMARK 3 S TENSOR
REMARK 3 S11: -0.0214 S12: 0.0522 S13: 0.0041
REMARK 3 S21: -0.0110 S22: 0.0108 S23: -0.0074
REMARK 3 S31: 0.1351 S32: -0.0294 S33: 0.0113
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain A and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6558 92.5704 93.4555
REMARK 3 T TENSOR
REMARK 3 T11: 0.2050 T22: 0.1386
REMARK 3 T33: 0.1024 T12: 0.0114
REMARK 3 T13: -0.0472 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 3.1518 L22: 1.6398
REMARK 3 L33: 2.5240 L12: -0.1959
REMARK 3 L13: 0.3829 L23: -0.0022
REMARK 3 S TENSOR
REMARK 3 S11: -0.1049 S12: -0.3488 S13: 0.0608
REMARK 3 S21: 0.2587 S22: 0.1134 S23: -0.2541
REMARK 3 S31: -0.1342 S32: 0.3040 S33: 0.0474
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain B and resid 1:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4024 34.8377 28.1532
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: 0.0670
REMARK 3 T33: 0.1120 T12: -0.0049
REMARK 3 T13: 0.0127 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.0860 L22: 1.0466
REMARK 3 L33: 0.9396 L12: 0.1710
REMARK 3 L13: -0.3761 L23: -0.0563
REMARK 3 S TENSOR
REMARK 3 S11: -0.0387 S12: 0.0670 S13: -0.1221
REMARK 3 S21: -0.1122 S22: -0.0023 S23: -0.0144
REMARK 3 S31: 0.1435 S32: -0.0206 S33: 0.0515
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain B and resid 52:127)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7807 44.3494 29.2714
REMARK 3 T TENSOR
REMARK 3 T11: 0.0527 T22: 0.0537
REMARK 3 T33: 0.0974 T12: 0.0043
REMARK 3 T13: 0.0022 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.1298 L22: 1.1411
REMARK 3 L33: 0.9726 L12: -0.1439
REMARK 3 L13: -0.5502 L23: 0.3148
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: 0.0644 S13: -0.0631
REMARK 3 S21: -0.1268 S22: -0.0220 S23: -0.0005
REMARK 3 S31: 0.0038 S32: -0.0437 S33: -0.0131
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 128:229)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2629 51.2398 41.7136
REMARK 3 T TENSOR
REMARK 3 T11: 0.0289 T22: 0.0734
REMARK 3 T33: 0.0768 T12: -0.0085
REMARK 3 T13: -0.0059 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.2143 L22: 0.7823
REMARK 3 L33: 0.4398 L12: -0.0361
REMARK 3 L13: -0.0864 L23: 0.3117
REMARK 3 S TENSOR
REMARK 3 S11: 0.0141 S12: -0.0287 S13: -0.0498
REMARK 3 S21: 0.0094 S22: -0.0379 S23: -0.0118
REMARK 3 S31: 0.0273 S32: -0.0176 S33: 0.0204
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 230:242)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5425 56.4497 21.4242
REMARK 3 T TENSOR
REMARK 3 T11: 0.7658 T22: 0.3922
REMARK 3 T33: 0.5716 T12: -0.0234
REMARK 3 T13: -0.3306 T23: -0.1098
REMARK 3 L TENSOR
REMARK 3 L11: 0.3767 L22: 2.2469
REMARK 3 L33: 2.7411 L12: -0.1069
REMARK 3 L13: -0.4411 L23: 1.0926
REMARK 3 S TENSOR
REMARK 3 S11: 0.2006 S12: 0.7463 S13: -0.6450
REMARK 3 S21: -0.2002 S22: 0.0397 S23: -0.0799
REMARK 3 S31: 0.8209 S32: 0.0313 S33: -0.3491
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 243:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1798 72.0370 45.2122
REMARK 3 T TENSOR
REMARK 3 T11: 0.0530 T22: 0.0689
REMARK 3 T33: 0.0605 T12: -0.0075
REMARK 3 T13: -0.0021 T23: -0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 1.2588 L22: 1.1958
REMARK 3 L33: 1.6861 L12: -0.3093
REMARK 3 L13: 0.3642 L23: 0.2574
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: 0.0739 S13: 0.0207
REMARK 3 S21: -0.1016 S22: -0.0589 S23: 0.0964
REMARK 3 S31: -0.0860 S32: -0.0687 S33: 0.0632
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (chain B and resid 283:461)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7197 66.8293 40.5754
REMARK 3 T TENSOR
REMARK 3 T11: 0.0505 T22: 0.0667
REMARK 3 T33: 0.0637 T12: -0.0014
REMARK 3 T13: 0.0025 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.6935 L22: 0.8964
REMARK 3 L33: 0.4198 L12: -0.0579
REMARK 3 L13: -0.0140 L23: 0.1260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0140 S12: -0.0427 S13: 0.0400
REMARK 3 S21: -0.0991 S22: -0.0066 S23: -0.0210
REMARK 3 S31: -0.0739 S32: -0.0040 S33: -0.0078
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (chain B and resid 462:469)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.2465 53.4444 31.9711
REMARK 3 T TENSOR
REMARK 3 T11: 0.0583 T22: 0.1135
REMARK 3 T33: 0.1920 T12: 0.0086
REMARK 3 T13: 0.0375 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 2.5967 L22: 0.5606
REMARK 3 L33: 4.4587 L12: 0.7156
REMARK 3 L13: 1.7354 L23: -0.3999
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: 0.0662 S13: -0.2886
REMARK 3 S21: -0.0719 S22: 0.1150 S23: -0.3044
REMARK 3 S31: 0.1267 S32: 0.4652 S33: -0.0529
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 4J0D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109375
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.05900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.5, 20%
REMARK 280 PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K
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
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 MET B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
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 240 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 240 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 ND1 HIS A 451 CD CD A 502 1.67
REMARK 500 O HOH B 925 O HOH B 934 1.67
REMARK 500 O HOH B 893 O HOH B 1014 1.74
REMARK 500 O HOH B 936 O HOH B 947 1.76
REMARK 500 O HOH B 811 O HOH B 993 1.79
REMARK 500 O HOH B 701 O HOH B 976 1.81
REMARK 500 O HOH B 701 O HOH B 975 1.85
REMARK 500 O HOH B 775 O HOH B 836 1.87
REMARK 500 O HOH B 829 O HOH B 993 1.89
REMARK 500 NZ LYS A 273 O HOH A 940 1.90
REMARK 500 O HOH B 840 O HOH B 893 1.90
REMARK 500 O HOH B 702 O HOH B 781 1.91
REMARK 500 NZ LYS A 409 O HOH A 905 1.92
REMARK 500 O HOH B 760 O HOH B 993 1.94
REMARK 500 O HOH A 900 O HOH A 965 1.94
REMARK 500 O HOH A 844 O HOH A 946 1.95
REMARK 500 O HOH A 813 O HOH A 944 1.95
REMARK 500 NH2 ARG B 149 O HOH B 916 1.96
REMARK 500 O1 PG4 B 504 O HOH B 824 1.97
REMARK 500 OD1 ASP A 294 NH2 ARG A 297 1.98
REMARK 500 O HOH A 882 O HOH A 904 1.98
REMARK 500 O HOH A 779 O HOH A 888 1.99
REMARK 500 OD1 ASP B 294 NH2 ARG B 297 1.99
REMARK 500 O HOH B 933 O HOH B 964 1.99
REMARK 500 O HOH A 861 O HOH A 864 2.01
REMARK 500 O HOH B 745 O HOH B 878 2.02
REMARK 500 ND2 ASN A 94 O HOH A 870 2.03
REMARK 500 O HOH B 843 O HOH B 899 2.03
REMARK 500 O HOH A 759 O HOH A 760 2.03
REMARK 500 O HOH A 971 O HOH A 972 2.03
REMARK 500 O HOH B 813 O HOH B 855 2.05
REMARK 500 O HOH B 928 O HOH B 930 2.05
REMARK 500 NE2 GLN A 16 O HOH A 875 2.05
REMARK 500 O HOH B 962 O HOH B 999 2.06
REMARK 500 OE1 GLN A 350 OG1 THR A 354 2.06
REMARK 500 O HOH B 982 O HOH B 983 2.06
REMARK 500 O HOH A 759 O HOH A 782 2.07
REMARK 500 NZ LYS B 273 O HOH B 973 2.07
REMARK 500 O HOH B 835 O HOH B 908 2.08
REMARK 500 O HOH B 702 O HOH B 735 2.08
REMARK 500 O HOH B 780 O HOH B 796 2.09
REMARK 500 O HOH B 695 O HOH B 835 2.09
REMARK 500 CE1 HIS A 451 CD CD A 502 2.09
REMARK 500 O HOH B 996 O HOH B 997 2.09
REMARK 500 O HOH B 849 O HOH B 992 2.09
REMARK 500 O1 PEG B 512 O HOH B 952 2.10
REMARK 500 O HOH A 931 O HOH A 971 2.11
REMARK 500 O HOH B 935 O HOH B 943 2.12
REMARK 500 O HOH A 682 O HOH A 817 2.14
REMARK 500 O HOH A 949 O HOH A 950 2.14
REMARK 500
REMARK 500 THIS ENTRY HAS 62 CLOSE CONTACTS
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 B 956 O HOH B 974 1455 1.89
REMARK 500 O HOH B 816 O HOH B 817 1565 1.97
REMARK 500 O HOH B 872 O HOH B 907 1545 2.17
REMARK 500 O HOH A 959 O HOH B 767 1556 2.19
REMARK 500 OE1 GLU A 244 O HOH A 918 1455 2.19
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 ALA A 20 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 LEU A 385 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG B 104 NE - CZ - NH2 ANGL. DEV. = -3.1 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 VAL A 19 119.43 -164.60
REMARK 500 SER A 163 -126.38 71.15
REMARK 500 CYS A 204 58.30 39.47
REMARK 500 ARG A 228 -155.54 -148.21
REMARK 500 ALA A 233 -148.61 -76.67
REMARK 500 THR A 340 146.48 77.74
REMARK 500 SER B 57 -167.40 -114.16
REMARK 500 SER B 163 -128.69 69.57
REMARK 500 CYS B 204 59.29 36.85
REMARK 500 ARG B 228 -155.14 -145.61
REMARK 500 THR B 236 -172.74 -65.45
REMARK 500 THR B 340 149.33 78.34
REMARK 500 PHE B 348 -53.66 -121.20
REMARK 500 PHE B 371 17.41 -145.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 929 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A 934 DISTANCE = 5.27 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 502 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 451 ND1
REMARK 620 2 ASP B 419 OD1 88.6
REMARK 620 3 ASP B 419 OD2 68.6 52.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 501 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 281 ND1
REMARK 620 2 HOH B 972 O 106.1
REMARK 620 3 HOH B 984 O 85.4 102.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 501 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 281 ND1
REMARK 620 2 HOH B 970 O 85.5
REMARK 620 3 HOH B 969 O 100.5 82.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 502 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 419 OD1
REMARK 620 2 ASP A 419 OD2 55.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 512
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4J0C RELATED DB: PDB
REMARK 900 RELATED ID: 4J0G RELATED DB: PDB
REMARK 900 RELATED ID: 4J0H RELATED DB: PDB
REMARK 900 RELATED ID: 4J0I RELATED DB: PDB
REMARK 900 RELATED ID: 4J0J RELATED DB: PDB
REMARK 900 RELATED ID: 4J0K RELATED DB: PDB
REMARK 900 RELATED ID: 4JUI RELATED DB: PDB
DBREF 4J0D A 1 469 UNP B3Y018 B3Y018_LACPN 1 469
DBREF 4J0D B 1 469 UNP B3Y018 B3Y018_LACPN 1 469
SEQADV 4J0D MET A -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS A -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS A -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS A -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS A -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS A -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS A -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D SER A -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D SER A -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLY A -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D VAL A -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D ASP A -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D LEU A -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLY A -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D THR A -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLU A -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D ASN A -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D LEU A -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D TYR A -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D PHE A -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLN A -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D SER A 0 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D MET B -21 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS B -20 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS B -19 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS B -18 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS B -17 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS B -16 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D HIS B -15 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D SER B -14 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D SER B -13 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLY B -12 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D VAL B -11 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D ASP B -10 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D LEU B -9 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLY B -8 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D THR B -7 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLU B -6 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D ASN B -5 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D LEU B -4 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D TYR B -3 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D PHE B -2 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D GLN B -1 UNP B3Y018 EXPRESSION TAG
SEQADV 4J0D SER B 0 UNP B3Y018 EXPRESSION TAG
SEQRES 1 A 491 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 491 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ASN ARG
SEQRES 3 A 491 LEU ILE PHE ASP ALA ASP TRP LEU VAL PRO GLU GLN VAL
SEQRES 4 A 491 GLN VAL ALA GLY GLN ALA ILE GLN TYR TYR ALA ALA ARG
SEQRES 5 A 491 ASN ILE GLN TYR VAL GLN HIS PRO VAL ALA ALA ILE GLN
SEQRES 6 A 491 VAL LEU ASN VAL PHE VAL PRO ALA ALA TYR LEU HIS GLY
SEQRES 7 A 491 SER SER VAL ASN GLY TYR GLN ARG ALA THR ALA PRO ILE
SEQRES 8 A 491 LEU MET PRO ASN THR VAL GLY GLY TYR LEU PRO GLY PRO
SEQRES 9 A 491 ALA ASP ASP PRO GLN ARG VAL THR TRP PRO THR ASN ALA
SEQRES 10 A 491 GLY THR ILE GLN GLN ALA LEU LYS ARG GLY TYR VAL VAL
SEQRES 11 A 491 VAL ALA ALA GLY ILE ARG GLY ARG THR THR VAL ASP LYS
SEQRES 12 A 491 SER GLY GLN ARG VAL GLY GLN ALA PRO ALA PHE ILE VAL
SEQRES 13 A 491 ASP MET LYS ALA ALA ILE ARG TYR VAL LYS TYR ASN GLN
SEQRES 14 A 491 GLY ARG LEU PRO GLY ASP ALA ASN ARG ILE ILE THR ASN
SEQRES 15 A 491 GLY THR SER ALA GLY GLY ALA THR SER ALA LEU ALA GLY
SEQRES 16 A 491 ALA SER GLY ASN SER ALA TYR PHE GLU PRO ALA LEU THR
SEQRES 17 A 491 ALA LEU GLY ALA ALA PRO ALA THR ASP ASP ILE PHE ALA
SEQRES 18 A 491 VAL SER ALA TYR CYS PRO ILE HIS ASN LEU GLU HIS ALA
SEQRES 19 A 491 ASP MET ALA TYR GLU TRP GLN PHE ASN GLY ILE ASN ASP
SEQRES 20 A 491 TRP HIS ARG TYR GLN PRO VAL ALA GLY THR THR LYS ASN
SEQRES 21 A 491 GLY ARG PRO LYS PHE GLU PRO VAL SER GLY GLN LEU THR
SEQRES 22 A 491 VAL GLU GLU GLN ALA LEU SER LEU ALA LEU LYS ALA GLN
SEQRES 23 A 491 PHE SER THR TYR LEU ASN GLN LEU LYS LEU THR ALA SER
SEQRES 24 A 491 ASP GLY THR HIS LEU THR LEU ASN GLU ALA GLY MET GLY
SEQRES 25 A 491 SER PHE ARG ASP VAL VAL ARG GLN LEU LEU ILE SER SER
SEQRES 26 A 491 ALA GLN THR ALA PHE ASP GLN GLY THR ASP ILE HIS LYS
SEQRES 27 A 491 TYR ALA GLY PHE VAL VAL THR GLY ASN GLN VAL THR ASP
SEQRES 28 A 491 LEU ASP LEU SER ALA TYR LEU LYS SER LEU THR ARG MET
SEQRES 29 A 491 LYS ALA VAL PRO ALA PHE ASP GLN LEU ASP LEU THR SER
SEQRES 30 A 491 PRO GLU ASN ASN LEU PHE GLY ASP ALA THR ALA LYS ALA
SEQRES 31 A 491 LYS HIS PHE THR ALA LEU ALA GLN THR ARG SER THR VAL
SEQRES 32 A 491 THR ALA GLN LEU ALA ASP ALA GLU LEU ILE GLN ALA ILE
SEQRES 33 A 491 ASN PRO LEU SER TYR LEU THR THR THR SER SER GLN VAL
SEQRES 34 A 491 ALA LYS HIS TRP ARG ILE ARG HIS GLY ALA ALA ASP ARG
SEQRES 35 A 491 ASP THR SER PHE ALA ILE PRO ILE ILE LEU ALA ILE MET
SEQRES 36 A 491 LEU GLU ASN HIS GLY TYR GLY ILE ASP PHE ALA LEU PRO
SEQRES 37 A 491 TRP ASP ILE PRO HIS SER GLY ASP TYR ASP LEU GLY ASP
SEQRES 38 A 491 LEU PHE SER TRP ILE ASP GLY LEU CYS GLN
SEQRES 1 B 491 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 491 GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ASN ARG
SEQRES 3 B 491 LEU ILE PHE ASP ALA ASP TRP LEU VAL PRO GLU GLN VAL
SEQRES 4 B 491 GLN VAL ALA GLY GLN ALA ILE GLN TYR TYR ALA ALA ARG
SEQRES 5 B 491 ASN ILE GLN TYR VAL GLN HIS PRO VAL ALA ALA ILE GLN
SEQRES 6 B 491 VAL LEU ASN VAL PHE VAL PRO ALA ALA TYR LEU HIS GLY
SEQRES 7 B 491 SER SER VAL ASN GLY TYR GLN ARG ALA THR ALA PRO ILE
SEQRES 8 B 491 LEU MET PRO ASN THR VAL GLY GLY TYR LEU PRO GLY PRO
SEQRES 9 B 491 ALA ASP ASP PRO GLN ARG VAL THR TRP PRO THR ASN ALA
SEQRES 10 B 491 GLY THR ILE GLN GLN ALA LEU LYS ARG GLY TYR VAL VAL
SEQRES 11 B 491 VAL ALA ALA GLY ILE ARG GLY ARG THR THR VAL ASP LYS
SEQRES 12 B 491 SER GLY GLN ARG VAL GLY GLN ALA PRO ALA PHE ILE VAL
SEQRES 13 B 491 ASP MET LYS ALA ALA ILE ARG TYR VAL LYS TYR ASN GLN
SEQRES 14 B 491 GLY ARG LEU PRO GLY ASP ALA ASN ARG ILE ILE THR ASN
SEQRES 15 B 491 GLY THR SER ALA GLY GLY ALA THR SER ALA LEU ALA GLY
SEQRES 16 B 491 ALA SER GLY ASN SER ALA TYR PHE GLU PRO ALA LEU THR
SEQRES 17 B 491 ALA LEU GLY ALA ALA PRO ALA THR ASP ASP ILE PHE ALA
SEQRES 18 B 491 VAL SER ALA TYR CYS PRO ILE HIS ASN LEU GLU HIS ALA
SEQRES 19 B 491 ASP MET ALA TYR GLU TRP GLN PHE ASN GLY ILE ASN ASP
SEQRES 20 B 491 TRP HIS ARG TYR GLN PRO VAL ALA GLY THR THR LYS ASN
SEQRES 21 B 491 GLY ARG PRO LYS PHE GLU PRO VAL SER GLY GLN LEU THR
SEQRES 22 B 491 VAL GLU GLU GLN ALA LEU SER LEU ALA LEU LYS ALA GLN
SEQRES 23 B 491 PHE SER THR TYR LEU ASN GLN LEU LYS LEU THR ALA SER
SEQRES 24 B 491 ASP GLY THR HIS LEU THR LEU ASN GLU ALA GLY MET GLY
SEQRES 25 B 491 SER PHE ARG ASP VAL VAL ARG GLN LEU LEU ILE SER SER
SEQRES 26 B 491 ALA GLN THR ALA PHE ASP GLN GLY THR ASP ILE HIS LYS
SEQRES 27 B 491 TYR ALA GLY PHE VAL VAL THR GLY ASN GLN VAL THR ASP
SEQRES 28 B 491 LEU ASP LEU SER ALA TYR LEU LYS SER LEU THR ARG MET
SEQRES 29 B 491 LYS ALA VAL PRO ALA PHE ASP GLN LEU ASP LEU THR SER
SEQRES 30 B 491 PRO GLU ASN ASN LEU PHE GLY ASP ALA THR ALA LYS ALA
SEQRES 31 B 491 LYS HIS PHE THR ALA LEU ALA GLN THR ARG SER THR VAL
SEQRES 32 B 491 THR ALA GLN LEU ALA ASP ALA GLU LEU ILE GLN ALA ILE
SEQRES 33 B 491 ASN PRO LEU SER TYR LEU THR THR THR SER SER GLN VAL
SEQRES 34 B 491 ALA LYS HIS TRP ARG ILE ARG HIS GLY ALA ALA ASP ARG
SEQRES 35 B 491 ASP THR SER PHE ALA ILE PRO ILE ILE LEU ALA ILE MET
SEQRES 36 B 491 LEU GLU ASN HIS GLY TYR GLY ILE ASP PHE ALA LEU PRO
SEQRES 37 B 491 TRP ASP ILE PRO HIS SER GLY ASP TYR ASP LEU GLY ASP
SEQRES 38 B 491 LEU PHE SER TRP ILE ASP GLY LEU CYS GLN
HET CD A 501 1
HET CD A 502 1
HET PEG A 503 7
HET PGE A 504 10
HET PEG A 505 7
HET PEG A 506 7
HET CD B 501 1
HET CD B 502 1
HET PG4 B 503 13
HET PG4 B 504 13
HET PEG B 505 7
HET PEG B 506 7
HET PEG B 507 7
HET PEG B 508 7
HET PEG B 509 7
HET PEG B 510 7
HET PEG B 511 7
HET PEG B 512 7
HETNAM CD CADMIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 CD 4(CD 2+)
FORMUL 5 PEG 11(C4 H10 O3)
FORMUL 6 PGE C6 H14 O4
FORMUL 11 PG4 2(C8 H18 O5)
FORMUL 21 HOH *787(H2 O)
HELIX 1 1 ASP A 8 LEU A 12 5 5
HELIX 2 2 ALA A 52 HIS A 55 5 4
HELIX 3 3 ASN A 94 ARG A 104 1 11
HELIX 4 4 PRO A 130 ASN A 146 1 17
HELIX 5 5 ASP A 153 ASN A 155 5 3
HELIX 6 6 SER A 163 SER A 175 1 13
HELIX 7 7 SER A 178 TYR A 180 5 3
HELIX 8 8 PHE A 181 GLY A 189 1 9
HELIX 9 9 ASN A 208 ASN A 221 1 14
HELIX 10 10 THR A 251 LEU A 272 1 22
HELIX 11 11 GLY A 290 GLN A 310 1 21
HELIX 12 12 ASP A 313 TYR A 317 5 5
HELIX 13 13 ASP A 331 THR A 340 1 10
HELIX 14 14 SER A 355 PHE A 361 1 7
HELIX 15 15 THR A 372 ARG A 378 1 7
HELIX 16 16 ASP A 387 ILE A 394 1 8
HELIX 17 17 ASN A 395 LEU A 400 5 6
HELIX 18 18 PHE A 424 HIS A 437 1 14
HELIX 19 19 ASP A 456 GLN A 469 1 14
HELIX 20 20 ASP B 8 LEU B 12 5 5
HELIX 21 21 ALA B 52 HIS B 55 5 4
HELIX 22 22 ASN B 94 GLY B 105 1 12
HELIX 23 23 PRO B 130 ASN B 146 1 17
HELIX 24 24 ASP B 153 ASN B 155 5 3
HELIX 25 25 SER B 163 SER B 175 1 13
HELIX 26 26 SER B 178 TYR B 180 5 3
HELIX 27 27 PHE B 181 GLY B 189 1 9
HELIX 28 28 ASN B 208 ASN B 221 1 14
HELIX 29 29 THR B 251 LEU B 272 1 22
HELIX 30 30 GLY B 290 GLN B 310 1 21
HELIX 31 31 ASP B 313 TYR B 317 5 5
HELIX 32 32 ASP B 331 THR B 340 1 10
HELIX 33 33 SER B 355 PHE B 361 1 7
HELIX 34 34 THR B 372 ARG B 378 1 7
HELIX 35 35 ASP B 387 ILE B 394 1 8
HELIX 36 36 ASN B 395 LEU B 400 5 6
HELIX 37 37 PHE B 424 HIS B 437 1 14
HELIX 38 38 ASP B 456 GLN B 469 1 14
SHEET 1 A 9 VAL A 13 GLN A 18 0
SHEET 2 A 9 ALA A 23 GLN A 33 -1 O ILE A 24 N VAL A 17
SHEET 3 A 9 VAL A 44 PRO A 50 -1 O VAL A 47 N ALA A 29
SHEET 4 A 9 VAL A 107 ALA A 111 -1 O VAL A 108 N PHE A 48
SHEET 5 A 9 ILE A 69 PRO A 72 1 N LEU A 70 O VAL A 107
SHEET 6 A 9 ILE A 157 THR A 162 1 O ILE A 158 N MET A 71
SHEET 7 A 9 ALA A 199 TYR A 203 1 O TYR A 203 N GLY A 161
SHEET 8 A 9 HIS A 410 ARG A 414 1 O ARG A 412 N VAL A 200
SHEET 9 A 9 GLY A 440 ALA A 444 1 O ASP A 442 N ILE A 413
SHEET 1 B 2 ASP A 225 PRO A 231 0
SHEET 2 B 2 PHE A 243 GLN A 249 -1 O VAL A 246 N ARG A 228
SHEET 1 C 2 PHE A 320 THR A 323 0
SHEET 2 C 2 GLN A 326 LEU A 330 -1 O GLN A 326 N THR A 323
SHEET 1 D 9 VAL B 13 VAL B 19 0
SHEET 2 D 9 GLN B 22 GLN B 33 -1 O TYR B 26 N GLU B 15
SHEET 3 D 9 VAL B 44 PRO B 50 -1 O VAL B 47 N ALA B 29
SHEET 4 D 9 VAL B 107 ALA B 111 -1 O VAL B 108 N PHE B 48
SHEET 5 D 9 ILE B 69 PRO B 72 1 N LEU B 70 O VAL B 107
SHEET 6 D 9 ILE B 157 THR B 162 1 O ILE B 158 N MET B 71
SHEET 7 D 9 ALA B 199 TYR B 203 1 O TYR B 203 N GLY B 161
SHEET 8 D 9 HIS B 410 ARG B 414 1 O ARG B 412 N VAL B 200
SHEET 9 D 9 GLY B 440 ALA B 444 1 O ASP B 442 N ILE B 413
SHEET 1 E 2 ASP B 225 THR B 235 0
SHEET 2 E 2 PRO B 241 GLN B 249 -1 O VAL B 246 N ARG B 228
SHEET 1 F 2 PHE B 320 THR B 323 0
SHEET 2 F 2 GLN B 326 LEU B 330 -1 O GLN B 326 N THR B 323
LINK ND1 HIS B 451 CD CD B 502 1555 1555 2.07
LINK ND1 HIS B 281 CD CD B 501 1555 1555 2.23
LINK ND1 HIS A 281 CD CD A 501 1555 1555 2.25
LINK OD1 ASP A 419 CD CD A 502 1555 1555 2.29
LINK OD2 ASP A 419 CD CD A 502 1555 1555 2.37
LINK OD1 ASP B 419 CD CD B 502 1555 1555 2.39
LINK OD2 ASP B 419 CD CD B 502 1555 1555 2.48
LINK CD CD B 501 O HOH B 972 1555 1555 2.04
LINK CD CD A 501 O HOH B 970 1555 1555 2.29
LINK CD CD B 501 O HOH B 984 1555 1555 2.34
LINK CD CD A 501 O HOH B 969 1555 1555 2.49
CISPEP 1 VAL A 19 ALA A 20 0 -25.70
CISPEP 2 TRP A 91 PRO A 92 0 -4.11
CISPEP 3 ALA A 129 PRO A 130 0 6.91
CISPEP 4 VAL A 345 PRO A 346 0 -10.84
CISPEP 5 TRP B 91 PRO B 92 0 -3.34
CISPEP 6 ALA B 129 PRO B 130 0 5.65
CISPEP 7 VAL B 345 PRO B 346 0 -10.81
SITE 1 AC1 5 LYS A 273 HIS A 281 HOH A 940 HOH B 969
SITE 2 AC1 5 HOH B 970
SITE 1 AC2 4 CYS A 204 ASP A 419 ASP A 421 HIS A 451
SITE 1 AC3 6 ARG A 412 ARG A 414 ASP A 442 ASP A 456
SITE 2 AC3 6 ASP A 459 HOH A 743
SITE 1 AC4 9 TRP A 218 GLN A 219 LYS A 262 ALA A 287
SITE 2 AC4 9 GLY A 288 ARG A 293 LEU A 332 SER A 333
SITE 3 AC4 9 LEU A 336
SITE 1 AC5 8 SER A 58 ASN A 60 GLY A 61 GLN A 63
SITE 2 AC5 8 TYR B 229 LEU B 339 ARG B 420 HOH B 734
SITE 1 AC6 3 GLN A 100 GLY A 458 GLU B 244
SITE 1 AC7 3 HIS B 281 HOH B 972 HOH B 984
SITE 1 AC8 5 CYS B 204 HIS B 415 ASP B 419 ASP B 421
SITE 2 AC8 5 HIS B 451
SITE 1 AC9 13 TRP B 218 GLN B 219 ASN B 221 LYS B 262
SITE 2 AC9 13 ALA B 287 GLY B 288 MET B 289 ARG B 293
SITE 3 AC9 13 LEU B 332 SER B 333 LEU B 336 LYS B 337
SITE 4 AC9 13 HOH B 746
SITE 1 BC1 9 ALA B 65 THR B 66 GLY B 123 GLN B 124
SITE 2 BC1 9 ASN B 155 HOH B 608 HOH B 801 HOH B 824
SITE 3 BC1 9 HOH B 974
SITE 1 BC2 6 TRP B 11 ALA B 28 ALA B 29 ARG B 30
SITE 2 BC2 6 GLY B 324 HOH B 847
SITE 1 BC3 6 SER B 0 ASN B 3 PRO B 38 ASP B 329
SITE 2 BC3 6 LEU B 330 HOH B 691
SITE 1 BC4 3 PRO B 14 GLU B 15 GLN B 25
SITE 1 BC5 5 LYS B 409 GLY B 438 TYR B 439 HOH B 823
SITE 2 BC5 5 HOH B 883
SITE 1 BC6 4 ARG B 64 GLY B 148 ARG B 149 LEU B 150
SITE 1 BC7 3 VAL B 17 VAL B 19 GLN B 99
SITE 1 BC8 7 ARG B 412 ARG B 414 PRO B 446 ASP B 456
SITE 2 BC8 7 ASP B 459 HOH B 671 HOH B 903
SITE 1 BC9 4 SER B 291 ASP B 294 VAL B 295 HOH B 952
CRYST1 46.940 62.918 84.070 70.58 85.70 78.96 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 0.021304 -0.004156 -0.000265 0.00000
SCALE2 0.000000 0.016193 -0.005566 0.00000
SCALE3 0.000000 0.000000 0.012613 0.00000
TER 3639 GLN A 469
TER 7275 GLN B 469
MASTER 729 0 18 38 26 0 33 6 8067 2 128 76
END |