HEADER OXIDOREDUCTASE/ISOMERASE 13-MAR-13 3W8J
TITLE CRYSTAL STRUCTURE OF P5 A0 IN A COMPLEX WITH PRX4 C-TERM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE A6;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: P5 A0, UNP RESIDUES 20-140;
COMPND 5 SYNONYM: ENDOPLASMIC RETICULUM PROTEIN 5, ER PROTEIN 5, ERP5, PROTEIN
COMPND 6 DISULFIDE ISOMERASE P5, THIOREDOXIN DOMAIN-CONTAINING PROTEIN 7;
COMPND 7 EC: 5.3.4.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: C-TERMINAL PEPTIDE FROM PEROXIREDOXIN-4;
COMPND 12 CHAIN: C, D;
COMPND 13 FRAGMENT: UNP RESIDUES 244-263;
COMPND 14 SYNONYM: ANTIOXIDANT ENZYME AOE372, PEROXIREDOXIN IV, PRX-IV,
COMPND 15 THIOREDOXIN PEROXIDASE AO372, THIOREDOXIN-DEPENDENT PEROXIDE
COMPND 16 REDUCTASE A0372;
COMPND 17 EC: 1.11.1.15;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PDIA6, ERP5, P5, TXNDC7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090
KEYWDS PDI FAMILY MEMBER, THIOREDOXIN FOLD, PROTEIN DISULFIDE ISOMERASE,
KEYWDS 2 OXIDOREDUCTASE-ISOMERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.INABA,M.SUZUKI,R.KOJIMA
REVDAT 1 04-SEP-13 3W8J 0
JRNL AUTH Y.SATO,R.KOJIMA,M.OKUMURA,M.HAGIWARA,S.MASUI,K.MAEGAWA,
JRNL AUTH 2 M.SAIKI,T.HORIBE,M.SUZUKI,K.INABA
JRNL TITL SYNERGISTIC COOPERATION OF PDI FAMILY MEMBERS IN
JRNL TITL 2 PEROXIREDOXIN 4-DRIVEN OXIDATIVE PROTEIN FOLDING
JRNL REF SCI REP V. 3 2456 2013
JRNL REFN ESSN 2045-2322
JRNL PMID 23949117
JRNL DOI 10.1038/SREP02456
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.7
REMARK 3 NUMBER OF REFLECTIONS : 14047
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 709
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.6767 - 3.5907 0.99 3384 157 0.1609 0.2110
REMARK 3 2 3.5907 - 2.8502 1.00 3204 189 0.1866 0.2597
REMARK 3 3 2.8502 - 2.4900 0.93 2948 160 0.2133 0.2687
REMARK 3 4 2.4900 - 2.2623 0.71 2236 125 0.2242 0.3060
REMARK 3 5 2.2623 - 2.1002 0.49 1566 78 0.2085 0.2643
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) : 26.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.58
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 : 0.007 2028
REMARK 3 ANGLE : 1.036 2739
REMARK 3 CHIRALITY : 0.067 296
REMARK 3 PLANARITY : 0.004 355
REMARK 3 DIHEDRAL : 14.108 731
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 22:36)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.820 43.730 9.836
REMARK 3 T TENSOR
REMARK 3 T11: 0.6611 T22: 0.3773
REMARK 3 T33: 0.3703 T12: -0.0720
REMARK 3 T13: -0.1702 T23: 0.0709
REMARK 3 L TENSOR
REMARK 3 L11: 0.0464 L22: 0.3137
REMARK 3 L33: 0.0660 L12: 0.1156
REMARK 3 L13: 0.0519 L23: 0.1472
REMARK 3 S TENSOR
REMARK 3 S11: 0.1729 S12: 0.2175 S13: -0.4203
REMARK 3 S21: -0.4784 S22: 0.2707 S23: 0.0815
REMARK 3 S31: 0.8466 S32: -0.5342 S33: 0.0100
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 37:47)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.827 49.813 18.272
REMARK 3 T TENSOR
REMARK 3 T11: -0.1088 T22: 1.3879
REMARK 3 T33: 0.3916 T12: -0.0132
REMARK 3 T13: -0.0178 T23: 0.2335
REMARK 3 L TENSOR
REMARK 3 L11: 0.1721 L22: 0.1607
REMARK 3 L33: 0.2876 L12: 0.1619
REMARK 3 L13: 0.2242 L23: 0.2140
REMARK 3 S TENSOR
REMARK 3 S11: -0.1037 S12: 0.1195 S13: -0.1014
REMARK 3 S21: 0.0218 S22: -0.0732 S23: 0.2194
REMARK 3 S31: 0.0372 S32: -0.4249 S33: -0.4708
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 48:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.578 52.224 -0.866
REMARK 3 T TENSOR
REMARK 3 T11: 0.3385 T22: 0.3335
REMARK 3 T33: 0.2609 T12: 0.0102
REMARK 3 T13: -0.0567 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.0211 L22: 0.7743
REMARK 3 L33: 0.1924 L12: 0.0640
REMARK 3 L13: -0.0148 L23: -0.2150
REMARK 3 S TENSOR
REMARK 3 S11: 0.1998 S12: -0.0259 S13: -0.1849
REMARK 3 S21: -0.6590 S22: 0.3336 S23: 0.4411
REMARK 3 S31: 0.0576 S32: -0.4303 S33: 0.0178
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 58:73)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.367 50.418 7.250
REMARK 3 T TENSOR
REMARK 3 T11: 0.3524 T22: 0.2416
REMARK 3 T33: 0.2421 T12: 0.0971
REMARK 3 T13: -0.0067 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.1291 L22: 0.0778
REMARK 3 L33: 0.0339 L12: 0.0354
REMARK 3 L13: 0.0702 L23: 0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0737 S12: 0.0519 S13: 0.1030
REMARK 3 S21: -0.1889 S22: 0.1482 S23: -0.1648
REMARK 3 S31: -0.3569 S32: 0.0463 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resseq 74:94)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6575 49.3837 8.0666
REMARK 3 T TENSOR
REMARK 3 T11: 0.1942 T22: 0.6356
REMARK 3 T33: 0.1421 T12: -0.1237
REMARK 3 T13: -0.1277 T23: 0.0779
REMARK 3 L TENSOR
REMARK 3 L11: 0.7349 L22: 0.5085
REMARK 3 L33: 0.4495 L12: 0.4392
REMARK 3 L13: 0.4082 L23: 0.0235
REMARK 3 S TENSOR
REMARK 3 S11: 0.1122 S12: 0.2489 S13: -0.2772
REMARK 3 S21: -0.1313 S22: 0.1099 S23: -0.2078
REMARK 3 S31: 0.2567 S32: -0.4971 S33: 0.2789
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resseq 95:106)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0014 57.8492 5.4482
REMARK 3 T TENSOR
REMARK 3 T11: 0.3383 T22: 0.5663
REMARK 3 T33: 0.2877 T12: 0.1991
REMARK 3 T13: -0.0055 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.0852 L22: 0.9581
REMARK 3 L33: 0.0958 L12: 0.2848
REMARK 3 L13: 0.0737 L23: 0.2614
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: -0.4452 S13: 0.0305
REMARK 3 S21: -0.0203 S22: 0.3014 S23: 0.3786
REMARK 3 S31: -0.3011 S32: -0.4950 S33: -0.0334
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resseq 107:121)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.652 60.793 11.565
REMARK 3 T TENSOR
REMARK 3 T11: 0.2617 T22: 0.6953
REMARK 3 T33: 0.3783 T12: 0.2284
REMARK 3 T13: -0.0890 T23: 0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 0.1944 L22: 1.9358
REMARK 3 L33: 0.3748 L12: 0.3496
REMARK 3 L13: -0.0117 L23: 0.6782
REMARK 3 S TENSOR
REMARK 3 S11: -0.3305 S12: -0.5675 S13: 0.4556
REMARK 3 S21: -0.2166 S22: 0.1797 S23: 0.0728
REMARK 3 S31: -0.5791 S32: -0.6134 S33: -0.0336
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resseq 122:140)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8543 60.1663 22.1400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2967 T22: 0.2975
REMARK 3 T33: 0.3130 T12: 0.0742
REMARK 3 T13: -0.0526 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 0.0789 L22: 0.1233
REMARK 3 L33: 0.2550 L12: -0.0031
REMARK 3 L13: -0.0417 L23: 0.0773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0162 S12: -0.1454 S13: 0.1912
REMARK 3 S21: -0.2349 S22: 0.0360 S23: 0.0471
REMARK 3 S31: -0.4663 S32: 0.0210 S33: 0.0010
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'B' and (resseq 21:36)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3317 43.7710 42.5431
REMARK 3 T TENSOR
REMARK 3 T11: 0.3023 T22: 0.2138
REMARK 3 T33: 0.2772 T12: -0.1432
REMARK 3 T13: 0.0794 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.8497 L22: 0.4003
REMARK 3 L33: 1.4882 L12: -0.5382
REMARK 3 L13: -0.9300 L23: 0.7469
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: -0.3852 S13: -0.1395
REMARK 3 S21: 0.1991 S22: 0.1901 S23: 0.3414
REMARK 3 S31: 0.4836 S32: -0.1084 S33: 0.1593
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'B' and (resseq 37:47)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.413 43.017 31.579
REMARK 3 T TENSOR
REMARK 3 T11: 0.3088 T22: 0.2004
REMARK 3 T33: 0.2286 T12: 0.0198
REMARK 3 T13: 0.0128 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 0.0831 L22: 0.0103
REMARK 3 L33: 0.0434 L12: 0.0045
REMARK 3 L13: 0.0587 L23: -0.0106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: 0.1659 S13: 0.0875
REMARK 3 S21: -0.1961 S22: -0.0811 S23: -0.1706
REMARK 3 S31: 0.2241 S32: -0.3040 S33: -0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'B' and (resseq 48:78)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4969 52.9283 42.6862
REMARK 3 T TENSOR
REMARK 3 T11: 0.3022 T22: 0.2478
REMARK 3 T33: 0.2493 T12: 0.0280
REMARK 3 T13: 0.0551 T23: -0.0643
REMARK 3 L TENSOR
REMARK 3 L11: 0.3284 L22: 0.3227
REMARK 3 L33: 0.0844 L12: 0.0853
REMARK 3 L13: -0.0095 L23: -0.0352
REMARK 3 S TENSOR
REMARK 3 S11: 0.1396 S12: -0.0923 S13: 0.0464
REMARK 3 S21: 0.1317 S22: -0.2261 S23: 0.1216
REMARK 3 S31: 0.1005 S32: -0.2008 S33: -0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resseq 79:88)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.850 42.960 48.577
REMARK 3 T TENSOR
REMARK 3 T11: 0.4748 T22: 0.2226
REMARK 3 T33: 0.1940 T12: -0.0266
REMARK 3 T13: 0.0437 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.1486 L22: 0.0274
REMARK 3 L33: 0.0563 L12: -0.0171
REMARK 3 L13: 0.0981 L23: 0.0085
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.3184 S13: 0.0266
REMARK 3 S21: 0.5028 S22: 0.1153 S23: 0.3400
REMARK 3 S31: 0.4094 S32: -0.3174 S33: 0.0102
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resseq 89:113)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5425 48.1928 40.2881
REMARK 3 T TENSOR
REMARK 3 T11: 0.2228 T22: 0.2381
REMARK 3 T33: 0.2533 T12: 0.0154
REMARK 3 T13: 0.0263 T23: -0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 0.1463 L22: 0.1667
REMARK 3 L33: 0.1257 L12: 0.1597
REMARK 3 L13: 0.0769 L23: 0.1249
REMARK 3 S TENSOR
REMARK 3 S11: 0.1177 S12: 0.0000 S13: -0.0584
REMARK 3 S21: 0.1264 S22: 0.0692 S23: -0.3401
REMARK 3 S31: 0.0262 S32: 0.2166 S33: 0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'B' and (resseq 114:121)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.011 61.746 40.285
REMARK 3 T TENSOR
REMARK 3 T11: 0.3485 T22: 0.0230
REMARK 3 T33: 0.2008 T12: 0.0822
REMARK 3 T13: 0.1324 T23: -0.1149
REMARK 3 L TENSOR
REMARK 3 L11: -0.0018 L22: 0.2926
REMARK 3 L33: 0.3538 L12: -0.0019
REMARK 3 L13: -0.0313 L23: -0.0973
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: 0.2291 S13: -0.0230
REMARK 3 S21: -0.2220 S22: -0.3248 S23: -0.3802
REMARK 3 S31: 0.0863 S32: 0.2440 S33: -0.0154
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'B' and (resseq 122:140)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2326 56.7000 26.0782
REMARK 3 T TENSOR
REMARK 3 T11: 0.2862 T22: 0.1342
REMARK 3 T33: 0.1780 T12: 0.0662
REMARK 3 T13: 0.0021 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.1254 L22: 0.1945
REMARK 3 L33: 0.3162 L12: 0.0295
REMARK 3 L13: 0.1284 L23: 0.2117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: -0.0814 S13: 0.1671
REMARK 3 S21: -0.2097 S22: 0.1492 S23: 0.0293
REMARK 3 S31: -0.4167 S32: 0.3398 S33: -0.0018
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'C' and (resseq 0:5)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1290 59.4222 -4.9052
REMARK 3 T TENSOR
REMARK 3 T11: 0.4779 T22: 0.4163
REMARK 3 T33: 0.3227 T12: 0.0677
REMARK 3 T13: -0.0600 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.0642 L22: 0.0042
REMARK 3 L33: 0.0117 L12: -0.0029
REMARK 3 L13: 0.0233 L23: 0.0051
REMARK 3 S TENSOR
REMARK 3 S11: -0.1017 S12: -0.0632 S13: 0.2027
REMARK 3 S21: 0.1699 S22: -0.2826 S23: -0.1982
REMARK 3 S31: -0.2087 S32: 0.1730 S33: -0.0001
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'D' and (resseq 0:5)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5807 55.4364 53.2685
REMARK 3 T TENSOR
REMARK 3 T11: 0.4270 T22: 0.3698
REMARK 3 T33: 0.3602 T12: 0.0039
REMARK 3 T13: 0.0165 T23: -0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 0.0314 L22: 0.0104
REMARK 3 L33: 0.0098 L12: 0.0197
REMARK 3 L13: 0.0000 L23: -0.0007
REMARK 3 S TENSOR
REMARK 3 S11: -0.2341 S12: -0.1330 S13: 0.0270
REMARK 3 S21: -0.0417 S22: -0.1571 S23: -0.1696
REMARK 3 S31: 0.1033 S32: 0.0168 S33: -0.0010
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 3W8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-13.
REMARK 100 THE RCSB ID CODE IS RCSB096020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 41.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 6.700
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 2000 MME, 0.1M POTASSIUM
REMARK 280 THIOCYANATE, 0.1M TRIS-HCL (PH 7.3), VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 19.52250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.67650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.68750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.67650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.52250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.68750
REMARK 290 SMTRY3 4 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: 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: 7030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 LEU A 12
REMARK 465 VAL A 13
REMARK 465 PRO A 14
REMARK 465 ARG A 15
REMARK 465 GLY A 16
REMARK 465 SER A 17
REMARK 465 HIS A 18
REMARK 465 MET A 19
REMARK 465 MET B -1
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 SER B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 GLY B 11
REMARK 465 LEU B 12
REMARK 465 VAL B 13
REMARK 465 PRO B 14
REMARK 465 ARG B 15
REMARK 465 GLY B 16
REMARK 465 SER B 17
REMARK 465 HIS B 18
REMARK 465 HIS C -2
REMARK 465 GLY C -1
REMARK 465 TRP C 6
REMARK 465 LYS C 7
REMARK 465 PRO C 8
REMARK 465 GLY C 9
REMARK 465 SER C 10
REMARK 465 GLU C 11
REMARK 465 THR C 12
REMARK 465 ILE C 13
REMARK 465 ILE C 14
REMARK 465 PRO C 15
REMARK 465 ASP C 16
REMARK 465 PRO C 17
REMARK 465 HIS D -2
REMARK 465 GLY D -1
REMARK 465 TRP D 6
REMARK 465 LYS D 7
REMARK 465 PRO D 8
REMARK 465 GLY D 9
REMARK 465 SER D 10
REMARK 465 GLU D 11
REMARK 465 THR D 12
REMARK 465 ILE D 13
REMARK 465 ILE D 14
REMARK 465 PRO D 15
REMARK 465 ASP D 16
REMARK 465 PRO D 17
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 MET B 19 CB CG SD CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 34 0.44 -158.43
REMARK 500 GLN A 41 37.62 -86.06
REMARK 500 ASP A 82 92.11 -68.88
REMARK 500 VAL B 39 -64.13 -102.90
REMARK 500 HIS B 86 67.17 -103.31
REMARK 500 ARG B 118 39.69 -91.40
REMARK 500
REMARK 500 REMARK: NULL
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 K B 206 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 27 O
REMARK 620 2 SER B 22 O 136.9
REMARK 620 3 ASP B 25 O 104.2 87.0
REMARK 620 4 ASP B 25 OD1 75.7 69.3 69.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 201 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 49 OE2
REMARK 620 2 ALA A 58 O 101.6
REMARK 620 3 TYR A 21 OH 89.7 148.3
REMARK 620 4 THR A 62 OG1 167.4 67.6 96.6
REMARK 620 5 GLU A 49 OE1 42.6 138.9 47.3 143.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 205 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 58 O
REMARK 620 2 THR B 62 OG1 75.8
REMARK 620 3 GLU B 49 OE2 102.8 161.8
REMARK 620 4 TYR B 21 OH 141.2 85.1 85.2
REMARK 620 5 GLU B 49 OE1 135.1 130.8 39.6 46.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 202 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 22 O
REMARK 620 2 VAL A 27 O 115.5
REMARK 620 3 ASP A 25 O 85.6 99.8
REMARK 620 4 ASP A 25 OD1 60.5 66.9 61.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VWW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF P5 A0
REMARK 900 RELATED ID: 3VWU RELATED DB: PDB
REMARK 900 RELATED ID: 3VWV RELATED DB: PDB
DBREF 3W8J A 20 140 UNP Q15084 PDIA6_HUMAN 20 140
DBREF 3W8J B 20 140 UNP Q15084 PDIA6_HUMAN 20 140
DBREF 3W8J C -2 17 UNP O08807 PRDX4_MOUSE 244 263
DBREF 3W8J D -2 17 UNP O08807 PRDX4_MOUSE 244 263
SEQADV 3W8J MET A -1 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J GLY A 0 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER A 1 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER A 2 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 3 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 4 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 5 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 6 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 7 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 8 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER A 9 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER A 10 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J GLY A 11 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J LEU A 12 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J VAL A 13 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J PRO A 14 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J ARG A 15 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J GLY A 16 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER A 17 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS A 18 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J MET A 19 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J ALA A 58 UNP Q15084 CYS 58 ENGINEERED MUTATION
SEQADV 3W8J MET B -1 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J GLY B 0 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER B 1 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER B 2 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 3 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 4 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 5 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 6 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 7 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 8 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER B 9 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER B 10 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J GLY B 11 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J LEU B 12 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J VAL B 13 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J PRO B 14 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J ARG B 15 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J GLY B 16 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J SER B 17 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J HIS B 18 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J MET B 19 UNP Q15084 EXPRESSION TAG
SEQADV 3W8J ALA B 58 UNP Q15084 CYS 58 ENGINEERED MUTATION
SEQRES 1 A 142 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 142 LEU VAL PRO ARG GLY SER HIS MET LEU TYR SER SER SER
SEQRES 3 A 142 ASP ASP VAL ILE GLU LEU THR PRO SER ASN PHE ASN ARG
SEQRES 4 A 142 GLU VAL ILE GLN SER ASP SER LEU TRP LEU VAL GLU PHE
SEQRES 5 A 142 TYR ALA PRO TRP CYS GLY HIS ALA GLN ARG LEU THR PRO
SEQRES 6 A 142 GLU TRP LYS LYS ALA ALA THR ALA LEU LYS ASP VAL VAL
SEQRES 7 A 142 LYS VAL GLY ALA VAL ASP ALA ASP LYS HIS HIS SER LEU
SEQRES 8 A 142 GLY GLY GLN TYR GLY VAL GLN GLY PHE PRO THR ILE LYS
SEQRES 9 A 142 ILE PHE GLY SER ASN LYS ASN ARG PRO GLU ASP TYR GLN
SEQRES 10 A 142 GLY GLY ARG THR GLY GLU ALA ILE VAL ASP ALA ALA LEU
SEQRES 11 A 142 SER ALA LEU ARG GLN LEU VAL LYS ASP ARG LEU GLY
SEQRES 1 B 142 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 142 LEU VAL PRO ARG GLY SER HIS MET LEU TYR SER SER SER
SEQRES 3 B 142 ASP ASP VAL ILE GLU LEU THR PRO SER ASN PHE ASN ARG
SEQRES 4 B 142 GLU VAL ILE GLN SER ASP SER LEU TRP LEU VAL GLU PHE
SEQRES 5 B 142 TYR ALA PRO TRP CYS GLY HIS ALA GLN ARG LEU THR PRO
SEQRES 6 B 142 GLU TRP LYS LYS ALA ALA THR ALA LEU LYS ASP VAL VAL
SEQRES 7 B 142 LYS VAL GLY ALA VAL ASP ALA ASP LYS HIS HIS SER LEU
SEQRES 8 B 142 GLY GLY GLN TYR GLY VAL GLN GLY PHE PRO THR ILE LYS
SEQRES 9 B 142 ILE PHE GLY SER ASN LYS ASN ARG PRO GLU ASP TYR GLN
SEQRES 10 B 142 GLY GLY ARG THR GLY GLU ALA ILE VAL ASP ALA ALA LEU
SEQRES 11 B 142 SER ALA LEU ARG GLN LEU VAL LYS ASP ARG LEU GLY
SEQRES 1 C 20 HIS GLY GLU VAL CYS PRO ALA GLY TRP LYS PRO GLY SER
SEQRES 2 C 20 GLU THR ILE ILE PRO ASP PRO
SEQRES 1 D 20 HIS GLY GLU VAL CYS PRO ALA GLY TRP LYS PRO GLY SER
SEQRES 2 D 20 GLU THR ILE ILE PRO ASP PRO
HET K A 201 1
HET K A 202 1
HET GOL B 201 6
HET GOL B 202 6
HET GOL B 203 6
HET GOL B 204 6
HET K B 205 1
HET K B 206 1
HETNAM K POTASSIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 K 4(K 1+)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 13 HOH *62(H2 O)
HELIX 1 1 ASN A 34 VAL A 39 1 6
HELIX 2 2 CYS A 55 LEU A 72 1 18
HELIX 3 3 HIS A 86 TYR A 93 1 8
HELIX 4 4 THR A 119 GLY A 140 1 22
HELIX 5 5 ASN B 34 VAL B 39 1 6
HELIX 6 6 CYS B 55 LEU B 72 1 18
HELIX 7 7 HIS B 86 TYR B 93 1 8
HELIX 8 8 THR B 119 GLY B 140 1 22
SHEET 1 A 5 ILE A 28 GLU A 29 0
SHEET 2 A 5 LYS A 77 ASP A 82 1 O VAL A 78 N ILE A 28
SHEET 3 A 5 TRP A 46 TYR A 51 1 N LEU A 47 O GLY A 79
SHEET 4 A 5 THR A 100 PHE A 104 -1 O PHE A 104 N TRP A 46
SHEET 5 A 5 GLU A 112 ASP A 113 -1 O GLU A 112 N ILE A 103
SHEET 1 B 2 GLY A 97 PHE A 98 0
SHEET 2 B 2 CYS C 2 PRO C 3 -1 O CYS C 2 N PHE A 98
SHEET 1 C 5 ILE B 28 LEU B 30 0
SHEET 2 C 5 LYS B 77 ASP B 82 1 O ALA B 80 N LEU B 30
SHEET 3 C 5 TRP B 46 TYR B 51 1 N LEU B 47 O GLY B 79
SHEET 4 C 5 THR B 100 PHE B 104 -1 O THR B 100 N PHE B 50
SHEET 5 C 5 GLU B 112 TYR B 114 -1 O GLU B 112 N ILE B 103
SHEET 1 D 2 GLY B 97 PHE B 98 0
SHEET 2 D 2 CYS D 2 PRO D 3 -1 O CYS D 2 N PHE B 98
SSBOND 1 CYS A 55 CYS C 2 1555 1555 2.07
SSBOND 2 CYS B 55 CYS D 2 1555 1555 2.06
LINK O VAL B 27 K K B 206 1555 1555 2.57
LINK O SER B 22 K K B 206 1555 1555 2.58
LINK OE2 GLU A 49 K K A 201 1555 1555 2.68
LINK O ALA B 58 K K B 205 1555 1555 2.70
LINK O ALA A 58 K K A 201 1555 1555 2.73
LINK O SER A 22 K K A 202 1555 1555 2.74
LINK OH TYR A 21 K K A 201 1555 1555 2.74
LINK OG1 THR B 62 K K B 205 1555 1555 2.76
LINK OG1 THR A 62 K K A 201 1555 1555 2.79
LINK O VAL A 27 K K A 202 1555 1555 2.80
LINK OE2 GLU B 49 K K B 205 1555 1555 2.82
LINK O ASP A 25 K K A 202 1555 1555 2.88
LINK O ASP B 25 K K B 206 1555 1555 2.89
LINK OD1 ASP B 25 K K B 206 1555 1555 3.05
LINK OH TYR B 21 K K B 205 1555 1555 3.12
LINK OE1 GLU A 49 K K A 201 1555 1555 3.23
LINK OD1 ASP A 25 K K A 202 1555 1555 3.35
LINK OE1 GLU B 49 K K B 205 1555 1555 3.48
CISPEP 1 PHE A 98 PRO A 99 0 -2.46
CISPEP 2 PHE B 98 PRO B 99 0 -6.30
SITE 1 AC1 4 TYR A 21 GLU A 49 ALA A 58 THR A 62
SITE 1 AC2 3 SER A 22 ASP A 25 VAL A 27
SITE 1 AC3 5 ILE B 40 ASN B 109 GLU B 121 ALA B 122
SITE 2 AC3 5 ASP B 125
SITE 1 AC4 3 GLN A 41 ASP B 137 HOH B 330
SITE 1 AC5 5 ALA B 83 VAL B 95 PHE B 98 GLY D 5
SITE 2 AC5 5 HOH D 102
SITE 1 AC6 2 GLN B 96 HOH D 102
SITE 1 AC7 5 LEU B 20 TYR B 21 GLU B 49 ALA B 58
SITE 2 AC7 5 THR B 62
SITE 1 AC8 4 SER B 22 SER B 23 ASP B 25 VAL B 27
CRYST1 39.045 53.375 133.353 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025611 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007499 0.00000
(ATOM LINES ARE NOT SHOWN.)
END