HEADER CYTOKINE 09-SEP-14 4RA8
TITLE STRUCTURE ANALYSIS OF THE MIP1A P8A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-C MOTIF CHEMOKINE 3;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: UNP RESIDUES 23-91;
COMPND 5 SYNONYM: G0/G1 SWITCH REGULATORY PROTEIN 19-1, MACROPHAGE
COMPND 6 INFLAMMATORY PROTEIN 1-ALPHA, MIP-1-ALPHA, PAT 464.1, SIS-BETA,
COMPND 7 SMALL-INDUCIBLE CYTOKINE A3, TONSILLAR LYMPHOCYTE LD78 ALPHA PROTEIN,
COMPND 8 MIP-1-ALPHA(4-69), LD78-ALPHA(4-69);
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CCL3, G0S19-1, MIP1A, SCYA3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.G.LIANG,M.REN,Q.GUO,W.J.TANG
REVDAT 4 20-SEP-23 4RA8 1 SEQADV
REVDAT 3 22-NOV-17 4RA8 1 REMARK
REVDAT 2 13-MAY-15 4RA8 1 JRNL
REVDAT 1 24-SEP-14 4RA8 0
SPRSDE 24-SEP-14 4RA8 3TN1
JRNL AUTH W.G.LIANG,M.REN,F.ZHAO,W.J.TANG
JRNL TITL STRUCTURES OF HUMAN CCL18, CCL3, AND CCL4 REVEAL MOLECULAR
JRNL TITL 2 DETERMINANTS FOR QUATERNARY STRUCTURES AND SENSITIVITY TO
JRNL TITL 3 INSULIN-DEGRADING ENZYME.
JRNL REF J.MOL.BIOL. V. 427 1345 2015
JRNL REFN ISSN 0022-2836
JRNL PMID 25636406
JRNL DOI 10.1016/J.JMB.2015.01.012
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 21934
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.050
REMARK 3 FREE R VALUE TEST SET COUNT : 790
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 46.9471 - 4.7303 0.80 5616 183 0.1905 0.2278
REMARK 3 2 4.7303 - 3.7550 0.66 4599 145 0.1688 0.2340
REMARK 3 3 3.7550 - 3.2805 0.55 3870 118 0.2129 0.2364
REMARK 3 4 3.2805 - 2.9806 0.53 3680 115 0.2454 0.2805
REMARK 3 5 2.9806 - 2.7670 0.53 3681 115 0.2507 0.3320
REMARK 3 6 2.7670 - 2.6000 0.53 3677 114 0.2259 0.2730
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.640
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 2706
REMARK 3 ANGLE : 0.744 3658
REMARK 3 CHIRALITY : 0.030 410
REMARK 3 PLANARITY : 0.003 472
REMARK 3 DIHEDRAL : 15.220 970
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 23
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 2:6 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.1675 64.0855 -6.0642
REMARK 3 T TENSOR
REMARK 3 T11: 1.0469 T22: 0.7165
REMARK 3 T33: 1.2386 T12: -0.0638
REMARK 3 T13: -0.2149 T23: 0.1935
REMARK 3 L TENSOR
REMARK 3 L11: 6.7605 L22: 2.0017
REMARK 3 L33: 2.0007 L12: -4.1486
REMARK 3 L13: -7.7691 L23: 1.9973
REMARK 3 S TENSOR
REMARK 3 S11: -0.8310 S12: 0.6074 S13: 3.2709
REMARK 3 S21: -1.0060 S22: -0.0621 S23: 0.7181
REMARK 3 S31: -2.0836 S32: 1.5620 S33: 0.9726
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 7:30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.9867 82.1396 -2.1241
REMARK 3 T TENSOR
REMARK 3 T11: 0.2686 T22: 0.4987
REMARK 3 T33: 0.1922 T12: -0.1746
REMARK 3 T13: 0.0072 T23: 0.0619
REMARK 3 L TENSOR
REMARK 3 L11: 4.7013 L22: 0.5852
REMARK 3 L33: 2.4130 L12: 0.9330
REMARK 3 L13: 2.6631 L23: -0.0061
REMARK 3 S TENSOR
REMARK 3 S11: -0.1086 S12: 0.0655 S13: 0.2556
REMARK 3 S21: -0.1000 S22: -0.0130 S23: 0.0205
REMARK 3 S31: -0.1318 S32: -0.2140 S33: 0.1080
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 31:69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.5919 79.5950 -0.9248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2381 T22: 0.4835
REMARK 3 T33: 0.2676 T12: -0.1779
REMARK 3 T13: -0.0054 T23: 0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 1.2675 L22: 1.2371
REMARK 3 L33: 1.9260 L12: 0.1310
REMARK 3 L13: 0.8519 L23: -0.6735
REMARK 3 S TENSOR
REMARK 3 S11: 0.0689 S12: -0.1011 S13: 0.0473
REMARK 3 S21: -0.0411 S22: -0.0220 S23: 0.0966
REMARK 3 S31: -0.1773 S32: -0.2710 S33: -0.0171
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 1:5 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.7768 48.9041 -12.1519
REMARK 3 T TENSOR
REMARK 3 T11: 0.9104 T22: 0.7171
REMARK 3 T33: 0.6239 T12: -0.1514
REMARK 3 T13: -0.0174 T23: -0.2026
REMARK 3 L TENSOR
REMARK 3 L11: 1.5796 L22: 6.3605
REMARK 3 L33: 0.0780 L12: 3.1710
REMARK 3 L13: 0.3515 L23: 0.7054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0233 S12: -0.5544 S13: 0.2520
REMARK 3 S21: 0.1873 S22: 0.1966 S23: 0.1929
REMARK 3 S31: -0.4443 S32: -0.4360 S33: -0.1846
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 6:21 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.9742 62.8025 3.9509
REMARK 3 T TENSOR
REMARK 3 T11: 0.3338 T22: 0.4794
REMARK 3 T33: 0.2672 T12: -0.2102
REMARK 3 T13: -0.0369 T23: 0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 1.5342 L22: 1.1677
REMARK 3 L33: 0.7196 L12: 0.8573
REMARK 3 L13: 0.5639 L23: -0.0208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0038 S12: 0.2415 S13: -0.0061
REMARK 3 S21: 0.0646 S22: -0.0765 S23: -0.1851
REMARK 3 S31: 0.0689 S32: 0.1087 S33: 0.0548
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 22:30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.0056 60.4874 0.8069
REMARK 3 T TENSOR
REMARK 3 T11: 0.3485 T22: 0.6366
REMARK 3 T33: 0.1094 T12: -0.3872
REMARK 3 T13: -0.0682 T23: -0.0591
REMARK 3 L TENSOR
REMARK 3 L11: 5.3861 L22: 9.5183
REMARK 3 L33: 5.1879 L12: -2.3637
REMARK 3 L13: -0.3513 L23: 1.0876
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: 0.1279 S13: -0.2933
REMARK 3 S21: -0.0525 S22: -0.0752 S23: 0.2052
REMARK 3 S31: 0.3000 S32: -0.0073 S33: 0.0510
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN B AND RESID 31:56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.5778 60.6488 3.3841
REMARK 3 T TENSOR
REMARK 3 T11: 0.3536 T22: 0.4370
REMARK 3 T33: 0.2117 T12: -0.1954
REMARK 3 T13: 0.0014 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 3.0520 L22: 2.3911
REMARK 3 L33: 0.4590 L12: -1.8856
REMARK 3 L13: 1.0799 L23: -0.8894
REMARK 3 S TENSOR
REMARK 3 S11: 0.1481 S12: 0.2967 S13: 0.0248
REMARK 3 S21: -0.2197 S22: -0.2644 S23: -0.0781
REMARK 3 S31: 0.2808 S32: 0.0484 S33: 0.1525
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 57:69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.9424 57.5108 7.6252
REMARK 3 T TENSOR
REMARK 3 T11: 0.3019 T22: 0.5323
REMARK 3 T33: 0.3118 T12: -0.3270
REMARK 3 T13: 0.0236 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.3019 L22: 3.9777
REMARK 3 L33: 0.9938 L12: 1.0627
REMARK 3 L13: -0.5266 L23: 0.1743
REMARK 3 S TENSOR
REMARK 3 S11: 0.0539 S12: 0.0128 S13: -0.3600
REMARK 3 S21: 0.0293 S22: -0.0959 S23: 0.3880
REMARK 3 S31: 0.3057 S32: -0.2857 S33: 0.0355
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN C AND RESID 4:8 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.4648 68.8873 -3.1400
REMARK 3 T TENSOR
REMARK 3 T11: 0.6012 T22: 0.6493
REMARK 3 T33: 0.8003 T12: 0.2425
REMARK 3 T13: -0.0595 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.7639 L22: 2.0001
REMARK 3 L33: 3.1980 L12: -3.5583
REMARK 3 L13: 1.5643 L23: -7.2813
REMARK 3 S TENSOR
REMARK 3 S11: 0.0998 S12: 0.5264 S13: 0.7921
REMARK 3 S21: -0.2559 S22: -0.0499 S23: 0.0881
REMARK 3 S31: -1.0312 S32: -0.2245 S33: 0.0099
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN C AND RESID 9:13 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.5789 56.4453 -0.5817
REMARK 3 T TENSOR
REMARK 3 T11: 0.3648 T22: 0.4915
REMARK 3 T33: 0.2567 T12: -0.1012
REMARK 3 T13: 0.0286 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 4.4260 L22: 8.8834
REMARK 3 L33: 2.7646 L12: -4.6782
REMARK 3 L13: 2.1002 L23: -3.3248
REMARK 3 S TENSOR
REMARK 3 S11: -0.1867 S12: -0.0714 S13: -0.1974
REMARK 3 S21: 0.1046 S22: 0.1190 S23: -0.0948
REMARK 3 S31: 0.1266 S32: 0.1171 S33: 0.0987
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN C AND RESID 14:18 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.2356 48.3938 -8.9702
REMARK 3 T TENSOR
REMARK 3 T11: 0.6593 T22: 0.6254
REMARK 3 T33: 0.3968 T12: -0.0566
REMARK 3 T13: 0.1514 T23: -0.0805
REMARK 3 L TENSOR
REMARK 3 L11: 4.3359 L22: 2.0055
REMARK 3 L33: 7.3218 L12: 0.1626
REMARK 3 L13: 0.9018 L23: 1.4407
REMARK 3 S TENSOR
REMARK 3 S11: -0.0678 S12: 0.7188 S13: -0.7553
REMARK 3 S21: -0.9284 S22: 0.3907 S23: -1.2116
REMARK 3 S31: 0.9016 S32: 0.7731 S33: -0.3693
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN C AND RESID 19:24 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.1510 53.7018 -20.7950
REMARK 3 T TENSOR
REMARK 3 T11: 0.9699 T22: 0.8120
REMARK 3 T33: 0.4672 T12: -0.4050
REMARK 3 T13: 0.2666 T23: -0.2185
REMARK 3 L TENSOR
REMARK 3 L11: 7.1145 L22: 6.1882
REMARK 3 L33: 3.0123 L12: 0.2630
REMARK 3 L13: -3.3730 L23: 2.8324
REMARK 3 S TENSOR
REMARK 3 S11: -0.1425 S12: 0.5713 S13: -0.0635
REMARK 3 S21: -0.8547 S22: 0.1394 S23: -0.2401
REMARK 3 S31: 0.2340 S32: 0.1090 S33: -0.0307
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN C AND RESID 25:30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3977 62.5658 -12.2454
REMARK 3 T TENSOR
REMARK 3 T11: 0.3304 T22: 0.6504
REMARK 3 T33: 0.3390 T12: -0.1964
REMARK 3 T13: 0.0482 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 7.8760 L22: 8.6879
REMARK 3 L33: 8.9587 L12: 2.3512
REMARK 3 L13: -6.0231 L23: 1.8341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0567 S12: -0.0265 S13: -0.0757
REMARK 3 S21: -0.2483 S22: 0.2367 S23: -0.3185
REMARK 3 S31: -0.1086 S32: 0.3103 S33: -0.2428
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN C AND RESID 31:56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7566 57.0034 -8.0307
REMARK 3 T TENSOR
REMARK 3 T11: 0.3222 T22: 0.5780
REMARK 3 T33: 0.3269 T12: -0.2034
REMARK 3 T13: 0.0107 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 1.5267 L22: 2.8735
REMARK 3 L33: 5.2318 L12: 0.2072
REMARK 3 L13: -0.0625 L23: 0.2602
REMARK 3 S TENSOR
REMARK 3 S11: -0.0784 S12: -0.0501 S13: -0.0261
REMARK 3 S21: -0.2787 S22: 0.1695 S23: 0.0982
REMARK 3 S31: 0.4325 S32: -0.2746 S33: -0.1015
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: ( CHAIN C AND RESID 57:69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0934 60.2927 -15.0675
REMARK 3 T TENSOR
REMARK 3 T11: 0.3893 T22: 0.6170
REMARK 3 T33: 0.4664 T12: -0.1922
REMARK 3 T13: 0.1815 T23: -0.1772
REMARK 3 L TENSOR
REMARK 3 L11: 4.3873 L22: 7.1564
REMARK 3 L33: 6.0135 L12: 2.3912
REMARK 3 L13: -1.5385 L23: -2.3635
REMARK 3 S TENSOR
REMARK 3 S11: -0.2834 S12: -0.0844 S13: -0.4709
REMARK 3 S21: -0.3287 S22: -0.2034 S23: -1.0284
REMARK 3 S31: 0.3362 S32: 0.4548 S33: 0.3723
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: ( CHAIN D AND RESID 5:8 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.3698 35.2816 -16.5021
REMARK 3 T TENSOR
REMARK 3 T11: 1.2180 T22: 0.7360
REMARK 3 T33: 0.5798 T12: -0.1917
REMARK 3 T13: -0.0685 T23: -0.1089
REMARK 3 L TENSOR
REMARK 3 L11: 0.7752 L22: 1.7020
REMARK 3 L33: 3.4502 L12: 1.1512
REMARK 3 L13: 1.6395 L23: 2.4245
REMARK 3 S TENSOR
REMARK 3 S11: -0.3787 S12: 0.4166 S13: -0.2968
REMARK 3 S21: -0.3784 S22: -0.0175 S23: 0.5443
REMARK 3 S31: 0.2847 S32: -0.5128 S33: 0.3268
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: ( CHAIN D AND RESID 9:30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.6148 41.6819 3.4336
REMARK 3 T TENSOR
REMARK 3 T11: 0.6201 T22: 0.4993
REMARK 3 T33: 0.3594 T12: -0.2798
REMARK 3 T13: -0.0046 T23: 0.0838
REMARK 3 L TENSOR
REMARK 3 L11: 4.1116 L22: 0.2911
REMARK 3 L33: 3.0981 L12: -0.1035
REMARK 3 L13: -2.5020 L23: 0.2306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: -0.3563 S13: -0.2720
REMARK 3 S21: 0.2349 S22: -0.2077 S23: -0.1922
REMARK 3 S31: 0.2230 S32: 0.1319 S33: 0.1372
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: ( CHAIN D AND RESID 31:56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -55.5241 39.5706 0.7318
REMARK 3 T TENSOR
REMARK 3 T11: 0.6939 T22: 0.5023
REMARK 3 T33: 0.4221 T12: -0.2868
REMARK 3 T13: -0.0253 T23: 0.0683
REMARK 3 L TENSOR
REMARK 3 L11: 3.4634 L22: 1.5385
REMARK 3 L33: 1.7884 L12: -0.9742
REMARK 3 L13: -1.0085 L23: 1.0482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0553 S12: -0.2103 S13: 0.1437
REMARK 3 S21: 0.4297 S22: -0.2444 S23: -0.2753
REMARK 3 S31: 0.4356 S32: -0.1424 S33: 0.1613
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: ( CHAIN D AND RESID 57:69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -63.4120 34.9664 9.3206
REMARK 3 T TENSOR
REMARK 3 T11: 0.9565 T22: 0.4014
REMARK 3 T33: -0.2431 T12: -0.7114
REMARK 3 T13: 0.7433 T23: 0.3772
REMARK 3 L TENSOR
REMARK 3 L11: 5.3724 L22: 5.1031
REMARK 3 L33: 1.9443 L12: 3.1287
REMARK 3 L13: -1.0349 L23: 0.1773
REMARK 3 S TENSOR
REMARK 3 S11: 0.0506 S12: -0.4392 S13: -0.3197
REMARK 3 S21: 0.2648 S22: -0.1759 S23: -0.0870
REMARK 3 S31: 0.2764 S32: 0.1274 S33: 0.1150
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: ( CHAIN E AND RESID 2:6 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.4713 51.8842 -2.3913
REMARK 3 T TENSOR
REMARK 3 T11: 0.9827 T22: 0.7299
REMARK 3 T33: 0.3365 T12: -0.0087
REMARK 3 T13: -0.0862 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 7.3234 L22: 2.0017
REMARK 3 L33: 4.1284 L12: 3.4779
REMARK 3 L13: -1.1110 L23: 5.2243
REMARK 3 S TENSOR
REMARK 3 S11: 0.0406 S12: 0.9021 S13: 0.3669
REMARK 3 S21: -1.0229 S22: -0.1306 S23: 0.4526
REMARK 3 S31: -0.0824 S32: -0.3342 S33: 0.0749
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: ( CHAIN E AND RESID 7:30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.9885 40.7852 -21.3820
REMARK 3 T TENSOR
REMARK 3 T11: 0.7687 T22: 0.5587
REMARK 3 T33: 0.4917 T12: -0.3438
REMARK 3 T13: 0.1196 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 0.8166 L22: 1.2372
REMARK 3 L33: 5.0920 L12: -0.0245
REMARK 3 L13: -0.5106 L23: -1.6505
REMARK 3 S TENSOR
REMARK 3 S11: -0.1957 S12: 0.4143 S13: -0.3271
REMARK 3 S21: -0.7786 S22: 0.5084 S23: -0.2505
REMARK 3 S31: -0.3390 S32: 0.1067 S33: -0.2214
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: ( CHAIN E AND RESID 31:56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.8753 40.7579 -18.7009
REMARK 3 T TENSOR
REMARK 3 T11: 0.6248 T22: 0.4570
REMARK 3 T33: 0.5368 T12: -0.2960
REMARK 3 T13: 0.1695 T23: -0.0952
REMARK 3 L TENSOR
REMARK 3 L11: 1.7672 L22: 2.7215
REMARK 3 L33: 4.3005 L12: 0.5398
REMARK 3 L13: 1.8042 L23: -0.3272
REMARK 3 S TENSOR
REMARK 3 S11: -0.0577 S12: 0.0753 S13: -0.6817
REMARK 3 S21: -0.6255 S22: 0.3449 S23: -0.4327
REMARK 3 S31: 0.0086 S32: 0.0653 S33: -0.2600
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: ( CHAIN E AND RESID 57:69 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.0441 47.6166 -27.8725
REMARK 3 T TENSOR
REMARK 3 T11: 1.0290 T22: 0.8617
REMARK 3 T33: 0.4232 T12: -0.4942
REMARK 3 T13: 0.0803 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 1.3324 L22: 5.8393
REMARK 3 L33: 2.1366 L12: 1.4933
REMARK 3 L13: 0.6762 L23: -1.9327
REMARK 3 S TENSOR
REMARK 3 S11: -0.2840 S12: 0.4007 S13: 0.0824
REMARK 3 S21: -0.5428 S22: -0.0334 S23: -0.4163
REMARK 3 S31: 0.1391 S32: 0.2015 S33: 0.1377
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 4RA8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21934
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2X69
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 5.5, 2 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.69867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.84933
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 51.69867
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 25.84933
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 51.69867
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 25.84933
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 51.69867
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 25.84933
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -90.07700
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 156.01794
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 ALA A 1
REMARK 465 ALA C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 ALA D 1
REMARK 465 SER D 2
REMARK 465 LEU D 3
REMARK 465 ALA D 4
REMARK 465 ALA E 1
DBREF 4RA8 A 1 69 UNP P10147 CCL3_HUMAN 23 91
DBREF 4RA8 B 1 69 UNP P10147 CCL3_HUMAN 23 91
DBREF 4RA8 C 1 69 UNP P10147 CCL3_HUMAN 23 91
DBREF 4RA8 D 1 69 UNP P10147 CCL3_HUMAN 23 91
DBREF 4RA8 E 1 69 UNP P10147 CCL3_HUMAN 23 91
SEQADV 4RA8 ALA A 8 UNP P10147 PRO 30 ENGINEERED MUTATION
SEQADV 4RA8 ALA B 8 UNP P10147 PRO 30 ENGINEERED MUTATION
SEQADV 4RA8 ALA C 8 UNP P10147 PRO 30 ENGINEERED MUTATION
SEQADV 4RA8 ALA D 8 UNP P10147 PRO 30 ENGINEERED MUTATION
SEQADV 4RA8 ALA E 8 UNP P10147 PRO 30 ENGINEERED MUTATION
SEQRES 1 A 69 ALA SER LEU ALA ALA ASP THR ALA THR ALA CYS CYS PHE
SEQRES 2 A 69 SER TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA
SEQRES 3 A 69 ASP TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY
SEQRES 4 A 69 VAL ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA
SEQRES 5 A 69 ASP PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP
SEQRES 6 A 69 LEU GLU LEU SER
SEQRES 1 B 69 ALA SER LEU ALA ALA ASP THR ALA THR ALA CYS CYS PHE
SEQRES 2 B 69 SER TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA
SEQRES 3 B 69 ASP TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY
SEQRES 4 B 69 VAL ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA
SEQRES 5 B 69 ASP PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP
SEQRES 6 B 69 LEU GLU LEU SER
SEQRES 1 C 69 ALA SER LEU ALA ALA ASP THR ALA THR ALA CYS CYS PHE
SEQRES 2 C 69 SER TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA
SEQRES 3 C 69 ASP TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY
SEQRES 4 C 69 VAL ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA
SEQRES 5 C 69 ASP PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP
SEQRES 6 C 69 LEU GLU LEU SER
SEQRES 1 D 69 ALA SER LEU ALA ALA ASP THR ALA THR ALA CYS CYS PHE
SEQRES 2 D 69 SER TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA
SEQRES 3 D 69 ASP TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY
SEQRES 4 D 69 VAL ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA
SEQRES 5 D 69 ASP PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP
SEQRES 6 D 69 LEU GLU LEU SER
SEQRES 1 E 69 ALA SER LEU ALA ALA ASP THR ALA THR ALA CYS CYS PHE
SEQRES 2 E 69 SER TYR THR SER ARG GLN ILE PRO GLN ASN PHE ILE ALA
SEQRES 3 E 69 ASP TYR PHE GLU THR SER SER GLN CYS SER LYS PRO GLY
SEQRES 4 E 69 VAL ILE PHE LEU THR LYS ARG SER ARG GLN VAL CYS ALA
SEQRES 5 E 69 ASP PRO SER GLU GLU TRP VAL GLN LYS TYR VAL SER ASP
SEQRES 6 E 69 LEU GLU LEU SER
FORMUL 6 HOH *54(H2 O)
HELIX 1 1 PRO A 21 ASN A 23 5 3
HELIX 2 2 GLU A 56 LEU A 68 1 13
HELIX 3 3 PRO B 21 ASN B 23 5 3
HELIX 4 4 GLU B 56 LEU B 68 1 13
HELIX 5 5 PRO C 21 ASN C 23 5 3
HELIX 6 6 GLU C 56 SER C 69 1 14
HELIX 7 7 PRO D 21 ASN D 23 5 3
HELIX 8 8 GLU D 56 LEU D 68 1 13
HELIX 9 9 PRO E 21 ASN E 23 5 3
HELIX 10 10 GLU E 56 SER E 69 1 14
SHEET 1 A 3 ILE A 25 GLU A 30 0
SHEET 2 A 3 VAL A 40 THR A 44 -1 O LEU A 43 N ALA A 26
SHEET 3 A 3 GLN A 49 ALA A 52 -1 O VAL A 50 N PHE A 42
SHEET 1 B 2 THR B 9 CYS B 11 0
SHEET 2 B 2 THR C 9 CYS C 11 -1 O CYS C 11 N THR B 9
SHEET 1 C 3 ILE B 25 GLU B 30 0
SHEET 2 C 3 VAL B 40 THR B 44 -1 O ILE B 41 N PHE B 29
SHEET 3 C 3 GLN B 49 ALA B 52 -1 O VAL B 50 N PHE B 42
SHEET 1 D 3 ILE C 25 GLU C 30 0
SHEET 2 D 3 VAL C 40 THR C 44 -1 O LEU C 43 N ALA C 26
SHEET 3 D 3 GLN C 49 ALA C 52 -1 O VAL C 50 N PHE C 42
SHEET 1 E 2 THR D 9 CYS D 11 0
SHEET 2 E 2 THR E 9 CYS E 11 -1 O THR E 9 N CYS D 11
SHEET 1 F 3 ILE D 25 GLU D 30 0
SHEET 2 F 3 VAL D 40 THR D 44 -1 O LEU D 43 N ALA D 26
SHEET 3 F 3 GLN D 49 ALA D 52 -1 O ALA D 52 N VAL D 40
SHEET 1 G 3 ILE E 25 GLU E 30 0
SHEET 2 G 3 VAL E 40 THR E 44 -1 O ILE E 41 N PHE E 29
SHEET 3 G 3 GLN E 49 ALA E 52 -1 O VAL E 50 N PHE E 42
SSBOND 1 CYS A 11 CYS A 35 1555 1555 2.04
SSBOND 2 CYS A 12 CYS A 51 1555 1555 2.06
SSBOND 3 CYS B 11 CYS B 35 1555 1555 2.05
SSBOND 4 CYS B 12 CYS B 51 1555 1555 2.06
SSBOND 5 CYS C 11 CYS C 35 1555 1555 2.04
SSBOND 6 CYS C 12 CYS C 51 1555 1555 2.05
SSBOND 7 CYS D 11 CYS D 35 1555 1555 2.04
SSBOND 8 CYS D 12 CYS D 51 1555 1555 2.04
SSBOND 9 CYS E 11 CYS E 35 1555 1555 2.04
SSBOND 10 CYS E 12 CYS E 51 1555 1555 2.05
CRYST1 180.154 180.154 77.548 90.00 90.00 120.00 P 62 2 2 60
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 0.005551 0.003205 0.000000 0.00000
SCALE2 0.000000 0.006410 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012895 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
