HEADER HORMONE 06-NOV-15 5EMS
TITLE CRYSTAL STRUCTURE OF AN IODINATED INSULIN ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: INSULIN;
COMPND 7 CHAIN: B, D, F, H, J, L;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606
KEYWDS INSULIN, HORMONE, NON-STANDARD MODIFICATION, PROTEIN DESIGN, PROTEIN
KEYWDS 2 ENGINEERING
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.LAWRENCE,V.PANDYARAJAN,Z.WAN,M.A.WEISS
REVDAT 8 15-NOV-23 5EMS 1 REMARK
REVDAT 7 27-SEP-23 5EMS 1 LINK
REVDAT 6 25-DEC-19 5EMS 1 REMARK
REVDAT 5 27-SEP-17 5EMS 1 REMARK
REVDAT 4 11-JAN-17 5EMS 1 JRNL
REVDAT 3 21-DEC-16 5EMS 1 JRNL
REVDAT 2 23-NOV-16 5EMS 1 JRNL
REVDAT 1 16-NOV-16 5EMS 0
JRNL AUTH K.EL HAGE,V.PANDYARAJAN,N.B.PHILLIPS,B.J.SMITH,J.G.MENTING,
JRNL AUTH 2 J.WHITTAKER,M.C.LAWRENCE,M.MEUWLY,M.A.WEISS
JRNL TITL EXTENDING HALOGEN-BASED MEDICINAL CHEMISTRY TO PROTEINS:
JRNL TITL 2 IODO-INSULIN AS A CASE STUDY.
JRNL REF J. BIOL. CHEM. V. 291 27023 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27875310
JRNL DOI 10.1074/JBC.M116.761015
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 11926
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1330
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 40.8537 - 4.9525 0.99 1273 139 0.1446 0.1930
REMARK 3 2 4.9525 - 3.9320 1.00 1235 146 0.1291 0.1707
REMARK 3 3 3.9320 - 3.4352 1.00 1239 136 0.1414 0.1974
REMARK 3 4 3.4352 - 3.1213 1.00 1242 135 0.1685 0.2438
REMARK 3 5 3.1213 - 2.8976 1.00 1239 139 0.1903 0.2858
REMARK 3 6 2.8976 - 2.7268 0.99 1204 134 0.1920 0.3181
REMARK 3 7 2.7268 - 2.5903 0.96 1200 135 0.1876 0.3388
REMARK 3 8 2.5903 - 2.4775 0.95 1165 130 0.1895 0.2592
REMARK 3 9 2.4775 - 2.3822 0.92 1151 129 0.2070 0.3007
REMARK 3 10 2.3822 - 2.3000 0.78 978 107 0.2471 0.3239
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.330
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 : 0.008 2411
REMARK 3 ANGLE : 1.089 3234
REMARK 3 CHIRALITY : 0.051 350
REMARK 3 PLANARITY : 0.006 415
REMARK 3 DIHEDRAL : 12.560 796
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -5.0838 3.4147 57.6567
REMARK 3 T TENSOR
REMARK 3 T11: 0.3651 T22: 0.5290
REMARK 3 T33: 0.4008 T12: 0.0297
REMARK 3 T13: -0.1385 T23: -0.0928
REMARK 3 L TENSOR
REMARK 3 L11: 8.0317 L22: 6.1314
REMARK 3 L33: 6.1787 L12: -0.1511
REMARK 3 L13: -0.6837 L23: -2.0083
REMARK 3 S TENSOR
REMARK 3 S11: -0.1747 S12: -0.8547 S13: 0.3836
REMARK 3 S21: 0.6966 S22: -0.1331 S23: -0.7350
REMARK 3 S31: -0.3871 S32: 0.7661 S33: 0.2482
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2730 -2.1911 53.1423
REMARK 3 T TENSOR
REMARK 3 T11: 0.3194 T22: 0.2492
REMARK 3 T33: 0.4047 T12: 0.0047
REMARK 3 T13: -0.0574 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 3.2820 L22: 8.2930
REMARK 3 L33: 5.4659 L12: -4.9638
REMARK 3 L13: -2.8591 L23: 3.0850
REMARK 3 S TENSOR
REMARK 3 S11: -0.3030 S12: -0.2581 S13: -0.0511
REMARK 3 S21: 0.4305 S22: 0.1534 S23: -0.4223
REMARK 3 S31: 0.6229 S32: 0.4455 S33: 0.1882
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3679 -18.3901 47.2766
REMARK 3 T TENSOR
REMARK 3 T11: 0.4380 T22: 0.2346
REMARK 3 T33: 0.3391 T12: -0.0120
REMARK 3 T13: -0.0153 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 3.3868 L22: 9.1000
REMARK 3 L33: 2.3892 L12: 0.1176
REMARK 3 L13: -1.4119 L23: -3.5278
REMARK 3 S TENSOR
REMARK 3 S11: -0.1701 S12: -0.0893 S13: -0.6119
REMARK 3 S21: -0.9603 S22: 0.1082 S23: 0.3337
REMARK 3 S31: 0.3794 S32: -0.0101 S33: 0.1490
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'D'
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4056 -10.1492 48.8043
REMARK 3 T TENSOR
REMARK 3 T11: 0.3736 T22: 0.3246
REMARK 3 T33: 0.3132 T12: 0.0261
REMARK 3 T13: 0.0265 T23: 0.0373
REMARK 3 L TENSOR
REMARK 3 L11: 6.4740 L22: 3.8265
REMARK 3 L33: 3.2617 L12: -1.9576
REMARK 3 L13: -1.0749 L23: 1.1176
REMARK 3 S TENSOR
REMARK 3 S11: -0.2487 S12: -0.3243 S13: -0.4004
REMARK 3 S21: 0.5327 S22: -0.0488 S23: -0.1316
REMARK 3 S31: 0.5698 S32: 0.4319 S33: 0.3868
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'E'
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3290 17.1381 33.8272
REMARK 3 T TENSOR
REMARK 3 T11: 0.3298 T22: 0.2877
REMARK 3 T33: 0.4458 T12: -0.0239
REMARK 3 T13: -0.0080 T23: 0.1341
REMARK 3 L TENSOR
REMARK 3 L11: 6.3775 L22: 5.2947
REMARK 3 L33: 2.9729 L12: 0.3549
REMARK 3 L13: -0.6149 L23: -0.5092
REMARK 3 S TENSOR
REMARK 3 S11: 0.0902 S12: 0.2396 S13: 0.7545
REMARK 3 S21: -0.0058 S22: -0.2766 S23: -0.1994
REMARK 3 S31: -0.7664 S32: -0.1443 S33: 0.0277
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'F'
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1072 9.9951 37.4427
REMARK 3 T TENSOR
REMARK 3 T11: 0.2694 T22: 0.2969
REMARK 3 T33: 0.4353 T12: 0.0321
REMARK 3 T13: -0.0161 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 4.5425 L22: 3.6792
REMARK 3 L33: 2.7578 L12: -0.1396
REMARK 3 L13: -2.0587 L23: 0.3237
REMARK 3 S TENSOR
REMARK 3 S11: -0.2164 S12: -0.0760 S13: 0.5505
REMARK 3 S21: 0.1262 S22: -0.0738 S23: -0.0891
REMARK 3 S31: -0.1789 S32: 0.2344 S33: 0.2236
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'G'
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2811 -2.2798 37.0966
REMARK 3 T TENSOR
REMARK 3 T11: 0.2686 T22: 0.4436
REMARK 3 T33: 0.6113 T12: 0.0454
REMARK 3 T13: -0.0162 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 3.6456 L22: 4.8562
REMARK 3 L33: 5.0269 L12: 3.0183
REMARK 3 L13: 2.2141 L23: 1.8545
REMARK 3 S TENSOR
REMARK 3 S11: 0.2258 S12: 0.5741 S13: -0.0998
REMARK 3 S21: 0.2925 S22: 0.2474 S23: -0.7083
REMARK 3 S31: 0.4520 S32: 0.5320 S33: -0.5188
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'H'
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4480 2.4548 35.0215
REMARK 3 T TENSOR
REMARK 3 T11: 0.2442 T22: 0.2859
REMARK 3 T33: 0.4912 T12: 0.0338
REMARK 3 T13: 0.0298 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 3.5902 L22: 7.8222
REMARK 3 L33: 8.4022 L12: 2.9681
REMARK 3 L13: 1.7442 L23: 5.6558
REMARK 3 S TENSOR
REMARK 3 S11: 0.1227 S12: 0.1299 S13: 0.3937
REMARK 3 S21: -0.2879 S22: 0.0828 S23: -0.3862
REMARK 3 S31: -0.3733 S32: 0.4428 S33: -0.2222
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'I'
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4233 -0.7777 48.7411
REMARK 3 T TENSOR
REMARK 3 T11: 0.2535 T22: 0.3634
REMARK 3 T33: 0.3732 T12: 0.0382
REMARK 3 T13: 0.1047 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 5.7104 L22: 5.2477
REMARK 3 L33: 8.1488 L12: -1.2313
REMARK 3 L13: 3.9886 L23: 2.5961
REMARK 3 S TENSOR
REMARK 3 S11: -0.0057 S12: -0.4505 S13: -0.1379
REMARK 3 S21: 0.4419 S22: -0.0996 S23: 0.6706
REMARK 3 S31: 0.2183 S32: -0.8478 S33: 0.0321
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'J'
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0460 -0.0420 40.8898
REMARK 3 T TENSOR
REMARK 3 T11: 0.1950 T22: 0.3249
REMARK 3 T33: 0.2894 T12: -0.0226
REMARK 3 T13: 0.0269 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 7.4536 L22: 5.1526
REMARK 3 L33: 4.9282 L12: 3.3069
REMARK 3 L13: 3.6717 L23: 2.7493
REMARK 3 S TENSOR
REMARK 3 S11: -0.1460 S12: 0.2685 S13: 0.1120
REMARK 3 S21: 0.1999 S22: -0.1635 S23: 0.7107
REMARK 3 S31: -0.1251 S32: -0.1445 S33: 0.3354
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'K'
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4608 -2.0144 23.6534
REMARK 3 T TENSOR
REMARK 3 T11: 0.3226 T22: 0.4251
REMARK 3 T33: 0.3249 T12: 0.0909
REMARK 3 T13: -0.0599 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 2.5839 L22: 8.0427
REMARK 3 L33: 7.2817 L12: -0.4117
REMARK 3 L13: -1.7701 L23: -0.6861
REMARK 3 S TENSOR
REMARK 3 S11: 0.3417 S12: 0.9251 S13: 0.2371
REMARK 3 S21: -0.9083 S22: -0.3267 S23: 0.3319
REMARK 3 S31: -0.1072 S32: -0.6576 S33: 0.0002
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'L'
REMARK 3 ORIGIN FOR THE GROUP (A): -23.5905 -3.1530 32.7744
REMARK 3 T TENSOR
REMARK 3 T11: 0.2649 T22: 0.3530
REMARK 3 T33: 0.3473 T12: -0.0187
REMARK 3 T13: -0.0157 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 4.1133 L22: 3.7286
REMARK 3 L33: 5.3838 L12: -3.4195
REMARK 3 L13: 0.3429 L23: 0.3173
REMARK 3 S TENSOR
REMARK 3 S11: 0.1767 S12: 0.7699 S13: -0.0742
REMARK 3 S21: -0.0495 S22: -0.2837 S23: 0.6088
REMARK 3 S31: -0.0702 S32: -0.2528 S33: 0.1027
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 5EMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 233
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13255
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 4.760
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
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: 1ZNJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, 0.08% ZINC
REMARK 280 ACETATE, 2% PHENOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.81500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -235.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L
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 NLE B 29
REMARK 465 THR B 30
REMARK 465 PHE D 1
REMARK 465 VAL D 2
REMARK 465 NLE D 29
REMARK 465 THR D 30
REMARK 465 NLE F 29
REMARK 465 THR F 30
REMARK 465 NLE H 29
REMARK 465 THR H 30
REMARK 465 PHE J 1
REMARK 465 NLE J 29
REMARK 465 THR J 30
REMARK 465 NLE L 29
REMARK 465 THR L 30
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 N PHE L 1 O HOH L 101 2.14
REMARK 500 NH1 ARG D 22 O HOH D 201 2.16
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 ZN B 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 10 NE2
REMARK 620 2 HIS F 10 NE2 110.8
REMARK 620 3 HIS J 10 NE2 115.5 104.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 10 NE2
REMARK 620 2 HIS H 10 NE2 101.3
REMARK 620 3 HIS L 10 NE2 106.9 112.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH E 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IPH K 101
DBREF 5EMS A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 5EMS B 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 5EMS C 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 5EMS D 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 5EMS E 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 5EMS F 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 5EMS G 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 5EMS H 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 5EMS I 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 5EMS J 1 30 UNP P01308 INS_HUMAN 25 54
DBREF 5EMS K 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 5EMS L 1 30 UNP P01308 INS_HUMAN 25 54
SEQADV 5EMS NLE B 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQADV 5EMS NLE D 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQADV 5EMS NLE F 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQADV 5EMS NLE H 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQADV 5EMS NLE J 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQADV 5EMS NLE L 29 UNP P01308 LYS 53 ENGINEERED MUTATION
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE IYR
SEQRES 3 B 30 THR PRO NLE THR
SEQRES 1 C 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 C 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 D 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 D 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE IYR
SEQRES 3 D 30 THR PRO NLE THR
SEQRES 1 E 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 E 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 F 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 F 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE IYR
SEQRES 3 F 30 THR PRO NLE THR
SEQRES 1 G 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 G 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 H 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 H 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE IYR
SEQRES 3 H 30 THR PRO NLE THR
SEQRES 1 I 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 I 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 J 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 J 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE IYR
SEQRES 3 J 30 THR PRO NLE THR
SEQRES 1 K 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 K 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 L 30 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 L 30 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE PHE IYR
SEQRES 3 L 30 THR PRO NLE THR
MODRES 5EMS IYR B 26 TYR MODIFIED RESIDUE
MODRES 5EMS IYR D 26 TYR MODIFIED RESIDUE
MODRES 5EMS IYR F 26 TYR MODIFIED RESIDUE
MODRES 5EMS IYR H 26 TYR MODIFIED RESIDUE
MODRES 5EMS IYR J 26 TYR MODIFIED RESIDUE
MODRES 5EMS IYR L 26 TYR MODIFIED RESIDUE
HET IYR B 26 13
HET IYR D 26 13
HET IYR F 26 13
HET IYR H 26 13
HET IYR J 26 13
HET IYR L 26 13
HET IPH A 101 7
HET ZN B 101 1
HET IPH C 101 7
HET ZN D 101 1
HET CL D 102 1
HET IPH E 101 7
HET CL F 101 1
HET IPH G 101 7
HET IPH I 101 7
HET IPH K 101 7
HETNAM IYR 3-IODO-TYROSINE
HETNAM IPH PHENOL
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 2 IYR 6(C9 H10 I N O3)
FORMUL 13 IPH 6(C6 H6 O)
FORMUL 14 ZN 2(ZN 2+)
FORMUL 17 CL 2(CL 1-)
FORMUL 23 HOH *75(H2 O)
HELIX 1 AA1 GLY A 1 THR A 8 1 8
HELIX 2 AA2 SER A 12 ASN A 18 1 7
HELIX 3 AA3 VAL B 2 GLY B 20 1 19
HELIX 4 AA4 ILE C 2 CYS C 7 1 6
HELIX 5 AA5 SER C 12 ASN C 18 1 7
HELIX 6 AA6 GLN D 4 GLY D 20 1 17
HELIX 7 AA7 ILE E 2 CYS E 7 1 6
HELIX 8 AA8 SER E 12 ASN E 18 1 7
HELIX 9 AA9 VAL F 2 GLY F 20 1 19
HELIX 10 AB1 ILE G 2 CYS G 7 1 6
HELIX 11 AB2 SER G 12 GLU G 17 1 6
HELIX 12 AB3 ASN G 18 CYS G 20 5 3
HELIX 13 AB4 VAL H 2 GLY H 20 1 19
HELIX 14 AB5 GLU H 21 GLY H 23 5 3
HELIX 15 AB6 ILE I 2 CYS I 7 1 6
HELIX 16 AB7 SER I 12 ASN I 18 1 7
HELIX 17 AB8 ASN J 3 GLY J 20 1 18
HELIX 18 AB9 GLU J 21 GLY J 23 5 3
HELIX 19 AC1 ILE K 2 CYS K 7 1 6
HELIX 20 AC2 SER K 12 GLU K 17 1 6
HELIX 21 AC3 ASN K 18 CYS K 20 5 3
HELIX 22 AC4 VAL L 2 GLY L 20 1 19
SHEET 1 AA1 2 PHE B 24 IYR B 26 0
SHEET 2 AA1 2 PHE D 24 IYR D 26 -1 O IYR D 26 N PHE B 24
SHEET 1 AA2 2 PHE F 24 IYR F 26 0
SHEET 2 AA2 2 PHE H 24 IYR H 26 -1 O PHE H 24 N IYR F 26
SHEET 1 AA3 2 PHE J 24 IYR J 26 0
SHEET 2 AA3 2 PHE L 24 IYR L 26 -1 O PHE L 24 N IYR J 26
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.04
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.03
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.04
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.04
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.04
SSBOND 7 CYS E 6 CYS E 11 1555 1555 2.02
SSBOND 8 CYS E 7 CYS F 7 1555 1555 2.03
SSBOND 9 CYS E 20 CYS F 19 1555 1555 2.03
SSBOND 10 CYS G 6 CYS G 11 1555 1555 2.02
SSBOND 11 CYS G 7 CYS H 7 1555 1555 2.03
SSBOND 12 CYS G 20 CYS H 19 1555 1555 2.03
SSBOND 13 CYS I 6 CYS I 11 1555 1555 2.03
SSBOND 14 CYS I 7 CYS J 7 1555 1555 2.04
SSBOND 15 CYS I 20 CYS J 19 1555 1555 2.03
SSBOND 16 CYS K 6 CYS K 11 1555 1555 2.02
SSBOND 17 CYS K 7 CYS L 7 1555 1555 2.03
SSBOND 18 CYS K 20 CYS L 19 1555 1555 2.05
LINK C PHE B 25 N IYR B 26 1555 1555 1.33
LINK C IYR B 26 N THR B 27 1555 1555 1.33
LINK C PHE D 25 N IYR D 26 1555 1555 1.33
LINK C IYR D 26 N THR D 27 1555 1555 1.33
LINK C PHE F 25 N IYR F 26 1555 1555 1.33
LINK C IYR F 26 N THR F 27 1555 1555 1.33
LINK C PHE H 25 N IYR H 26 1555 1555 1.33
LINK C IYR H 26 N THR H 27 1555 1555 1.33
LINK C PHE J 25 N IYR J 26 1555 1555 1.33
LINK C IYR J 26 N THR J 27 1555 1555 1.33
LINK C PHE L 25 N IYR L 26 1555 1555 1.33
LINK C IYR L 26 N THR L 27 1555 1555 1.33
LINK NE2 HIS B 10 ZN ZN B 101 1555 1555 2.10
LINK ZN ZN B 101 NE2 HIS F 10 1555 1555 1.99
LINK ZN ZN B 101 NE2 HIS J 10 1555 1555 2.09
LINK NE2 HIS D 10 ZN ZN D 101 1555 1555 1.97
LINK ZN ZN D 101 NE2 HIS H 10 1555 1555 2.08
LINK ZN ZN D 101 NE2 HIS L 10 1555 1555 2.00
SITE 1 AC1 4 CYS A 6 SER A 9 ILE A 10 CYS A 11
SITE 1 AC2 4 HIS B 10 HIS F 10 CL F 101 HIS J 10
SITE 1 AC3 4 CYS C 6 ILE C 10 CYS C 11 LEU C 16
SITE 1 AC4 4 HIS D 10 CL D 102 HIS H 10 HIS L 10
SITE 1 AC5 4 HIS D 10 ZN D 101 HIS H 10 HIS L 10
SITE 1 AC6 5 CYS E 6 SER E 9 ILE E 10 CYS E 11
SITE 2 AC6 5 LEU F 11
SITE 1 AC7 4 HIS B 10 ZN B 101 HIS F 10 HIS J 10
SITE 1 AC8 4 HIS D 5 CYS G 6 CYS G 11 LEU H 11
SITE 1 AC9 5 HIS B 5 CYS I 6 ILE I 10 CYS I 11
SITE 2 AC9 5 LEU J 11
SITE 1 AD1 6 HIS H 5 CYS K 6 SER K 9 ILE K 10
SITE 2 AD1 6 CYS K 11 LEU L 11
CRYST1 46.430 61.630 58.580 90.00 111.38 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021538 0.000000 0.008431 0.00000
SCALE2 0.000000 0.016226 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
