HEADER TRANSFERASE 14-DEC-16 5U8Q
TITLE STRUCTURE OF THE ECTODOMAIN OF THE HUMAN TYPE 1 INSULIN-LIKE GROWTH
TITLE 2 FACTOR RECEPTOR IN COMPLEX WITH IGF-I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INSULIN-LIKE GROWTH FACTOR I RECEPTOR,IGF-I RECEPTOR;
COMPND 5 EC: 2.7.10.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: A17DELTA-BETA CONSTRUCT, SEE WHITTEN ET AL., J. MOL.
COMPND 9 BIOL., V394, PP878-92 (2009).;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: INSULIN-LIKE GROWTH FACTOR I;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: IGF-I,MECHANO GROWTH FACTOR,MGF,SOMATOMEDIN-C;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: MATURE IGF-1;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: FV 24-60 HEAVY CHAIN;
COMPND 18 CHAIN: H;
COMPND 19 ENGINEERED: YES;
COMPND 20 OTHER_DETAILS: HEAVY CHAIN VARIABLE DOMAIN (RESIDUES 1-118) OF MAB
COMPND 21 24-60, INCLUDING ADDITIONAL GLY-THR AT THE N TERMINUS AND GLU-ASN-
COMPND 22 LEU-TYR-PHE-GLN AT C TERMINUS.;
COMPND 23 MOL_ID: 4;
COMPND 24 MOLECULE: FV 24-60 LIGHT CHAIN;
COMPND 25 CHAIN: L;
COMPND 26 ENGINEERED: YES;
COMPND 27 OTHER_DETAILS: LIGHT CHAIN VARIABLE DOMAIN (RESIDUES 1-107) OF MAB
COMPND 28 24-60, INCLUDING ADDITIONAL GLY AT THE N TERMINUS.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IGF1R;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: LEC8;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: FIII;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: FIII-IGFR.ECD;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: IGF1, IBP1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 MOL_ID: 3;
SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 20 ORGANISM_TAXID: 10090;
SOURCE 21 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PGPHFT;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PGPHFT-SUMO-SCFV;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 27 ORGANISM_TAXID: 10090;
SOURCE 28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: PGPHFT;
SOURCE 31 EXPRESSION_SYSTEM_PLASMID: PGPHFT-SUMO-SCFV
KEYWDS RECEPTOR TYROSINE KINASE, TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR,
KEYWDS 2 INSULIN-LIKE GROWTH-FACTOR I, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LAWRENCE,Y.XU
REVDAT 3 29-JUL-20 5U8Q 1 COMPND REMARK HETNAM SSBOND
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 14-MAR-18 5U8Q 1 JRNL
REVDAT 1 28-FEB-18 5U8Q 0
JRNL AUTH Y.XU,G.K.KONG,J.G.MENTING,M.B.MARGETTS,C.A.DELAINE,
JRNL AUTH 2 L.M.JENKIN,V.V.KISELYOV,P.DE MEYTS,B.E.FORBES,M.C.LAWRENCE
JRNL TITL HOW LIGAND BINDS TO THE TYPE 1 INSULIN-LIKE GROWTH FACTOR
JRNL TITL 2 RECEPTOR.
JRNL REF NAT COMMUN V. 9 821 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29483580
JRNL DOI 10.1038/S41467-018-03219-7
REMARK 2
REMARK 2 RESOLUTION. 3.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1-2575_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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.326
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 32110
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.260
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.746
REMARK 3 FREE R VALUE TEST SET COUNT : 1524
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 22.1730 - 7.1985 1.00 2995 144 0.2519 0.2993
REMARK 3 2 7.1985 - 5.7464 1.00 2879 136 0.2707 0.3350
REMARK 3 3 5.7464 - 5.0297 1.00 2827 141 0.2156 0.2547
REMARK 3 4 5.0297 - 4.5742 1.00 2804 155 0.2023 0.2358
REMARK 3 5 4.5742 - 4.2488 1.00 2786 146 0.2224 0.2589
REMARK 3 6 4.2488 - 3.9999 0.99 2785 141 0.2527 0.3141
REMARK 3 7 3.9999 - 3.8006 0.99 2751 137 0.2993 0.3401
REMARK 3 8 3.8006 - 3.6359 0.99 2799 118 0.3274 0.3342
REMARK 3 9 3.6359 - 3.4965 0.99 2731 149 0.3348 0.3952
REMARK 3 10 3.4965 - 3.3763 0.99 2736 126 0.3541 0.4154
REMARK 3 11 3.3763 - 3.2710 0.90 2493 131 0.4146 0.4307
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) : 0.543
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.905
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 110.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 177.8
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 : 0.002 8934
REMARK 3 ANGLE : 0.520 12148
REMARK 3 CHIRALITY : 0.044 1337
REMARK 3 PLANARITY : 0.003 1549
REMARK 3 DIHEDRAL : 11.595 5364
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 1 THROUGH 266 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2422 29.7960 -49.9071
REMARK 3 T TENSOR
REMARK 3 T11: 2.5229 T22: 1.9333
REMARK 3 T33: 1.2098 T12: -0.0328
REMARK 3 T13: 0.2074 T23: -0.3994
REMARK 3 L TENSOR
REMARK 3 L11: 7.2606 L22: 1.1278
REMARK 3 L33: 1.8219 L12: 1.2116
REMARK 3 L13: 0.5625 L23: 0.9176
REMARK 3 S TENSOR
REMARK 3 S11: 0.0445 S12: 2.7864 S13: -0.7600
REMARK 3 S21: -0.4098 S22: 0.4533 S23: -0.3603
REMARK 3 S31: 0.3378 S32: 0.6463 S33: -0.4663
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 267 THROUGH 456 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4690 13.2341 1.4006
REMARK 3 T TENSOR
REMARK 3 T11: 2.5183 T22: 0.8510
REMARK 3 T33: 1.2506 T12: 0.0859
REMARK 3 T13: -0.0529 T23: -0.1359
REMARK 3 L TENSOR
REMARK 3 L11: 2.4162 L22: 3.0590
REMARK 3 L33: 2.9909 L12: 1.2821
REMARK 3 L13: -1.3478 L23: -1.4117
REMARK 3 S TENSOR
REMARK 3 S11: -0.1769 S12: -0.3829 S13: -0.1550
REMARK 3 S21: 0.1511 S22: -0.0118 S23: -0.9718
REMARK 3 S31: -0.2033 S32: 0.1161 S33: 0.1402
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 457 THROUGH 575 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5376 -17.8175 6.4361
REMARK 3 T TENSOR
REMARK 3 T11: 3.1563 T22: 0.8962
REMARK 3 T33: 0.6327 T12: 0.3103
REMARK 3 T13: -0.0273 T23: 0.0935
REMARK 3 L TENSOR
REMARK 3 L11: 8.3406 L22: 3.6635
REMARK 3 L33: 6.0028 L12: 0.1421
REMARK 3 L13: -1.2333 L23: -1.0725
REMARK 3 S TENSOR
REMARK 3 S11: -0.0788 S12: -0.3620 S13: 1.0261
REMARK 3 S21: -0.0300 S22: 0.3659 S23: 0.5248
REMARK 3 S31: -0.8633 S32: -0.1547 S33: -0.2346
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 576 THROUGH 900 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1669 -23.3123 -57.9280
REMARK 3 T TENSOR
REMARK 3 T11: 2.8538 T22: 1.5663
REMARK 3 T33: 0.8687 T12: 0.0893
REMARK 3 T13: 0.0942 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.2261 L22: 0.6512
REMARK 3 L33: 2.2604 L12: -0.3632
REMARK 3 L13: -0.0031 L23: 3.0208
REMARK 3 S TENSOR
REMARK 3 S11: 0.3172 S12: -0.0311 S13: 0.1475
REMARK 3 S21: -0.3379 S22: -0.0372 S23: -0.0241
REMARK 3 S31: 0.0554 S32: 0.2890 S33: -0.2995
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1149 24.6526 -44.9978
REMARK 3 T TENSOR
REMARK 3 T11: 2.3705 T22: 1.9866
REMARK 3 T33: 0.5992 T12: -0.0540
REMARK 3 T13: -0.0696 T23: -0.2041
REMARK 3 L TENSOR
REMARK 3 L11: 5.5307 L22: 3.6368
REMARK 3 L33: 9.7914 L12: 0.6185
REMARK 3 L13: -1.0845 L23: -1.6164
REMARK 3 S TENSOR
REMARK 3 S11: -0.1542 S12: 2.4226 S13: 0.1153
REMARK 3 S21: 0.3533 S22: 1.2402 S23: -0.5958
REMARK 3 S31: -0.0652 S32: -0.3302 S33: -0.7493
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 22 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8838 19.9558 -35.6241
REMARK 3 T TENSOR
REMARK 3 T11: 2.2752 T22: 1.2860
REMARK 3 T33: 0.9264 T12: 0.4935
REMARK 3 T13: 0.2642 T23: -0.1151
REMARK 3 L TENSOR
REMARK 3 L11: 8.0633 L22: 4.6026
REMARK 3 L33: 2.7954 L12: 0.5280
REMARK 3 L13: 1.3880 L23: -2.6857
REMARK 3 S TENSOR
REMARK 3 S11: 0.7179 S12: 0.9148 S13: -1.1791
REMARK 3 S21: -1.4741 S22: -0.4348 S23: 0.8086
REMARK 3 S31: 0.9360 S32: -0.4378 S33: -0.1595
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 54 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7378 27.0095 -35.3262
REMARK 3 T TENSOR
REMARK 3 T11: 2.9980 T22: 1.5682
REMARK 3 T33: -0.0647 T12: 0.5210
REMARK 3 T13: -0.2308 T23: -0.1712
REMARK 3 L TENSOR
REMARK 3 L11: 2.5510 L22: 3.2592
REMARK 3 L33: 5.8178 L12: 0.6721
REMARK 3 L13: 1.3888 L23: 4.0178
REMARK 3 S TENSOR
REMARK 3 S11: -0.2037 S12: -0.9814 S13: -0.8864
REMARK 3 S21: 1.2693 S22: -0.1188 S23: 0.2376
REMARK 3 S31: 0.2274 S32: 0.9904 S33: -0.0707
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2524 56.2686 -17.5537
REMARK 3 T TENSOR
REMARK 3 T11: 1.9135 T22: 0.8563
REMARK 3 T33: 0.7914 T12: -0.0781
REMARK 3 T13: -0.1596 T23: 0.1262
REMARK 3 L TENSOR
REMARK 3 L11: 3.6717 L22: 4.9088
REMARK 3 L33: 3.7163 L12: -4.1336
REMARK 3 L13: -0.8465 L23: 1.5556
REMARK 3 S TENSOR
REMARK 3 S11: 1.5032 S12: -0.8674 S13: 0.6975
REMARK 3 S21: -0.9264 S22: -0.3050 S23: 0.3724
REMARK 3 S31: -0.2197 S32: -0.3257 S33: -1.0393
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3624 52.8657 -22.8102
REMARK 3 T TENSOR
REMARK 3 T11: 2.0650 T22: 0.9679
REMARK 3 T33: 0.7574 T12: -0.1597
REMARK 3 T13: 0.0319 T23: -0.1846
REMARK 3 L TENSOR
REMARK 3 L11: 4.3073 L22: 7.5665
REMARK 3 L33: 4.3686 L12: 3.6044
REMARK 3 L13: 0.1549 L23: -1.1821
REMARK 3 S TENSOR
REMARK 3 S11: -1.3066 S12: -0.1802 S13: -0.4419
REMARK 3 S21: -2.0611 S22: -0.6577 S23: 0.3800
REMARK 3 S31: 1.0732 S32: -1.0259 S33: 1.6228
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 26 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1233 46.7007 -15.2555
REMARK 3 T TENSOR
REMARK 3 T11: 1.6294 T22: 0.8647
REMARK 3 T33: 0.5161 T12: -0.4681
REMARK 3 T13: 0.0822 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 4.6994 L22: 7.6742
REMARK 3 L33: 1.1612 L12: -1.4434
REMARK 3 L13: 1.8486 L23: -2.4342
REMARK 3 S TENSOR
REMARK 3 S11: 0.8147 S12: -0.0277 S13: -0.3639
REMARK 3 S21: -1.5201 S22: -0.4592 S23: -0.9171
REMARK 3 S31: -1.6260 S32: 1.2952 S33: -0.4423
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 52 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8618 37.7850 -27.5044
REMARK 3 T TENSOR
REMARK 3 T11: 1.7950 T22: -0.3944
REMARK 3 T33: 1.2726 T12: -0.1854
REMARK 3 T13: 0.4656 T23: -0.5481
REMARK 3 L TENSOR
REMARK 3 L11: 2.1923 L22: 5.1658
REMARK 3 L33: 4.6433 L12: 3.2655
REMARK 3 L13: 1.0646 L23: 2.7439
REMARK 3 S TENSOR
REMARK 3 S11: -0.2780 S12: 0.1157 S13: -0.8475
REMARK 3 S21: -0.2136 S22: -0.5280 S23: 0.3948
REMARK 3 S31: 0.3216 S32: -0.2768 S33: 0.1540
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 58 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1251 37.6775 -12.2212
REMARK 3 T TENSOR
REMARK 3 T11: 1.9664 T22: 1.0713
REMARK 3 T33: 1.0725 T12: -0.3543
REMARK 3 T13: 0.2643 T23: -0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 5.7189 L22: 4.4793
REMARK 3 L33: 5.1569 L12: -5.0545
REMARK 3 L13: -5.4165 L23: 4.8014
REMARK 3 S TENSOR
REMARK 3 S11: 1.4069 S12: -1.1826 S13: -0.4936
REMARK 3 S21: 2.4772 S22: -1.1705 S23: 1.5452
REMARK 3 S31: 1.0675 S32: -0.5601 S33: -0.2916
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 65 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2238 42.6397 -19.8967
REMARK 3 T TENSOR
REMARK 3 T11: 1.8135 T22: 1.0737
REMARK 3 T33: 0.9585 T12: -0.5169
REMARK 3 T13: 0.0228 T23: -0.2303
REMARK 3 L TENSOR
REMARK 3 L11: 4.8013 L22: 9.5350
REMARK 3 L33: 1.7270 L12: -6.4989
REMARK 3 L13: -2.6344 L23: 3.9999
REMARK 3 S TENSOR
REMARK 3 S11: -2.6408 S12: 0.2376 S13: -0.7784
REMARK 3 S21: 0.0033 S22: -0.9192 S23: 1.5499
REMARK 3 S31: 0.1896 S32: -1.3349 S33: 3.4452
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 74 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1334 48.2377 -25.2920
REMARK 3 T TENSOR
REMARK 3 T11: 2.7408 T22: 1.5901
REMARK 3 T33: 0.7766 T12: 0.1165
REMARK 3 T13: -0.2439 T23: -0.2291
REMARK 3 L TENSOR
REMARK 3 L11: 7.3355 L22: 6.3639
REMARK 3 L33: 3.7665 L12: -5.7067
REMARK 3 L13: -4.6134 L23: 4.8862
REMARK 3 S TENSOR
REMARK 3 S11: -0.9919 S12: 2.5027 S13: -1.3902
REMARK 3 S21: -1.6193 S22: -0.8424 S23: -0.4851
REMARK 3 S31: 1.7631 S32: -4.7007 S33: 1.5671
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 84 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3357 48.3619 -8.0278
REMARK 3 T TENSOR
REMARK 3 T11: 2.3733 T22: 1.6384
REMARK 3 T33: 0.7500 T12: -0.1227
REMARK 3 T13: 0.3952 T23: 0.0789
REMARK 3 L TENSOR
REMARK 3 L11: 6.1189 L22: 1.9942
REMARK 3 L33: 3.9388 L12: -4.2213
REMARK 3 L13: 2.9334 L23: 2.3046
REMARK 3 S TENSOR
REMARK 3 S11: 0.8092 S12: -2.2625 S13: -0.5482
REMARK 3 S21: 1.0764 S22: 1.0328 S23: 0.5500
REMARK 3 S31: -1.2219 S32: -0.8777 S33: -0.9789
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 92 THROUGH 97 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3830 52.1430 -12.5903
REMARK 3 T TENSOR
REMARK 3 T11: 2.5734 T22: 0.9408
REMARK 3 T33: 0.6182 T12: 0.2028
REMARK 3 T13: -0.4087 T23: -0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 9.2068 L22: 8.8534
REMARK 3 L33: 2.7131 L12: -0.2652
REMARK 3 L13: -1.1545 L23: 4.7955
REMARK 3 S TENSOR
REMARK 3 S11: 0.2992 S12: -1.5905 S13: 1.8708
REMARK 3 S21: 0.8961 S22: -0.4202 S23: 0.8846
REMARK 3 S31: -0.9588 S32: -1.0692 S33: 0.3519
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 98 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5483 50.1994 -14.6840
REMARK 3 T TENSOR
REMARK 3 T11: 2.1175 T22: 0.9980
REMARK 3 T33: 1.0333 T12: -0.4748
REMARK 3 T13: 0.1117 T23: -0.1121
REMARK 3 L TENSOR
REMARK 3 L11: 2.7559 L22: 1.6890
REMARK 3 L33: 8.9295 L12: 1.5762
REMARK 3 L13: -2.0190 L23: 0.8110
REMARK 3 S TENSOR
REMARK 3 S11: -0.8787 S12: 1.6152 S13: -0.2114
REMARK 3 S21: -1.3639 S22: 0.7353 S23: -0.4737
REMARK 3 S31: 0.5307 S32: 0.2341 S33: 0.1440
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9289 46.8462 4.4989
REMARK 3 T TENSOR
REMARK 3 T11: 2.4985 T22: 1.0525
REMARK 3 T33: 1.0995 T12: -0.0692
REMARK 3 T13: 0.2332 T23: 0.2400
REMARK 3 L TENSOR
REMARK 3 L11: 3.5999 L22: 4.8021
REMARK 3 L33: 7.3758 L12: -0.9142
REMARK 3 L13: 0.5218 L23: 3.6802
REMARK 3 S TENSOR
REMARK 3 S11: 0.7890 S12: -0.8627 S13: 1.5352
REMARK 3 S21: 2.6321 S22: 0.1582 S23: 0.9830
REMARK 3 S31: -0.9587 S32: -0.2458 S33: -0.9090
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 14 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7746 45.9406 -0.6679
REMARK 3 T TENSOR
REMARK 3 T11: 2.0018 T22: 0.9847
REMARK 3 T33: 0.8882 T12: -0.1156
REMARK 3 T13: -0.0197 T23: 0.1342
REMARK 3 L TENSOR
REMARK 3 L11: 5.0776 L22: 3.6083
REMARK 3 L33: 7.3460 L12: -3.4413
REMARK 3 L13: -1.3170 L23: -1.7901
REMARK 3 S TENSOR
REMARK 3 S11: 0.0577 S12: -0.2905 S13: -0.5145
REMARK 3 S21: 1.9494 S22: -0.6686 S23: 0.3983
REMARK 3 S31: 1.4530 S32: 0.8663 S33: 0.5489
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 39 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0720 51.0897 -8.2668
REMARK 3 T TENSOR
REMARK 3 T11: 1.9144 T22: 1.3723
REMARK 3 T33: 0.9332 T12: -0.3654
REMARK 3 T13: -0.1030 T23: 0.0981
REMARK 3 L TENSOR
REMARK 3 L11: 2.4830 L22: 2.5088
REMARK 3 L33: 5.0229 L12: 0.2903
REMARK 3 L13: 0.5650 L23: 3.3312
REMARK 3 S TENSOR
REMARK 3 S11: 0.3321 S12: -0.2832 S13: -0.1620
REMARK 3 S21: 0.3587 S22: -0.2105 S23: -0.1145
REMARK 3 S31: -2.6113 S32: 0.9942 S33: -0.2537
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 68 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.1643 43.5313 1.3355
REMARK 3 T TENSOR
REMARK 3 T11: 1.8894 T22: 0.9210
REMARK 3 T33: 1.7116 T12: 0.2571
REMARK 3 T13: 0.2551 T23: 0.0992
REMARK 3 L TENSOR
REMARK 3 L11: 6.3958 L22: 6.9976
REMARK 3 L33: 5.1645 L12: 6.6180
REMARK 3 L13: -5.7135 L23: -5.9668
REMARK 3 S TENSOR
REMARK 3 S11: -1.1999 S12: -1.5964 S13: -1.6321
REMARK 3 S21: 3.4884 S22: -1.0817 S23: -3.0362
REMARK 3 S31: -0.0218 S32: -0.7378 S33: 2.1050
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 76 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.8422 55.0996 -2.0782
REMARK 3 T TENSOR
REMARK 3 T11: 2.1315 T22: 0.9164
REMARK 3 T33: 0.7732 T12: -0.1853
REMARK 3 T13: 0.0135 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 5.3002 L22: 9.3462
REMARK 3 L33: 3.9408 L12: -2.1796
REMARK 3 L13: 1.7672 L23: 4.2134
REMARK 3 S TENSOR
REMARK 3 S11: -0.2320 S12: -0.3186 S13: -0.4992
REMARK 3 S21: -0.1759 S22: 0.1581 S23: -1.1248
REMARK 3 S31: -0.1750 S32: 1.2022 S33: 0.1646
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8344 46.7011 -2.1176
REMARK 3 T TENSOR
REMARK 3 T11: 2.3582 T22: 0.9883
REMARK 3 T33: 0.7206 T12: -0.4751
REMARK 3 T13: -0.0292 T23: 0.4204
REMARK 3 L TENSOR
REMARK 3 L11: 6.0508 L22: 8.5816
REMARK 3 L33: 1.5368 L12: 3.5345
REMARK 3 L13: -1.3397 L23: 0.2656
REMARK 3 S TENSOR
REMARK 3 S11: -0.0502 S12: -1.0103 S13: -0.4333
REMARK 3 S21: 0.5479 S22: 0.2131 S23: 0.3872
REMARK 3 S31: 0.1081 S32: -0.0888 S33: -0.5123
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 5U8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225483.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32228
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.270
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.19000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 2.07000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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: 5U8R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM SULFATE, 0.1 M
REMARK 280 IMIDAZOLE-MALATE PH 7.0. IGF-1 WAS INCLUDED BY SOAKING DIRECTLY
REMARK 280 INTO THE MOTHER CRYSTAL. FOR FULL DETAILS SEE THE PRIMARY
REMARK 280 CITATION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 44.34500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 98.83000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.34500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 98.83000
REMARK 290 SMTRY3 4 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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 107620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 LYS A 36
REMARK 465 ALA A 37
REMARK 465 GLU A 38
REMARK 465 ASP A 39
REMARK 465 TYR A 40
REMARK 465 GLY A 154
REMARK 465 THR A 155
REMARK 465 MET A 156
REMARK 465 GLU A 157
REMARK 465 GLU A 158
REMARK 465 LYS A 159
REMARK 465 PRO A 160
REMARK 465 MET A 161
REMARK 465 GLY A 190
REMARK 465 LYS A 191
REMARK 465 ARG A 192
REMARK 465 ASP A 645
REMARK 465 GLY A 646
REMARK 465 THR A 647
REMARK 465 ILE A 648
REMARK 465 ASP A 649
REMARK 465 ILE A 650
REMARK 465 GLU A 651
REMARK 465 GLU A 652
REMARK 465 VAL A 653
REMARK 465 THR A 654
REMARK 465 GLU A 655
REMARK 465 ASN A 656
REMARK 465 PRO A 657
REMARK 465 LYS A 658
REMARK 465 THR A 659
REMARK 465 GLU A 660
REMARK 465 VAL A 661
REMARK 465 CYS A 662
REMARK 465 GLY A 663
REMARK 465 GLY A 664
REMARK 465 GLU A 665
REMARK 465 LYS A 666
REMARK 465 GLY A 667
REMARK 465 PRO A 668
REMARK 465 CYS A 669
REMARK 465 CYS A 670
REMARK 465 ALA A 671
REMARK 465 CYS A 672
REMARK 465 PRO A 673
REMARK 465 LYS A 674
REMARK 465 THR A 675
REMARK 465 GLU A 676
REMARK 465 ALA A 677
REMARK 465 GLU A 678
REMARK 465 LYS A 679
REMARK 465 GLN A 680
REMARK 465 ALA A 681
REMARK 465 GLU A 682
REMARK 465 LYS A 683
REMARK 465 GLU A 684
REMARK 465 GLU A 685
REMARK 465 ALA A 686
REMARK 465 GLU A 687
REMARK 465 TYR A 688
REMARK 465 GLU A 726
REMARK 465 ARG A 727
REMARK 465 LYS A 728
REMARK 465 ARG A 729
REMARK 465 ARG A 730
REMARK 465 ASP A 731
REMARK 465 VAL A 732
REMARK 465 MET A 733
REMARK 465 GLN A 734
REMARK 465 VAL A 735
REMARK 465 ALA A 736
REMARK 465 ASN A 737
REMARK 465 ALA A 738
REMARK 465 GLY A 739
REMARK 465 ASN A 740
REMARK 465 ASN A 741
REMARK 465 GLU A 742
REMARK 465 THR A 743
REMARK 465 GLU A 744
REMARK 465 GLU A 901
REMARK 465 ASN A 902
REMARK 465 PHE A 903
REMARK 465 ILE A 904
REMARK 465 HIS A 905
REMARK 465 GLY B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 3
REMARK 465 LYS B 27
REMARK 465 PRO B 28
REMARK 465 THR B 29
REMARK 465 GLY B 30
REMARK 465 TYR B 31
REMARK 465 GLY B 32
REMARK 465 SER B 33
REMARK 465 SER B 34
REMARK 465 SER B 35
REMARK 465 ARG B 36
REMARK 465 ARG B 37
REMARK 465 ALA B 38
REMARK 465 LEU B 64
REMARK 465 LYS B 65
REMARK 465 PRO B 66
REMARK 465 ALA B 67
REMARK 465 LYS B 68
REMARK 465 SER B 69
REMARK 465 ALA B 70
REMARK 465 GLY H -1
REMARK 465 THR H 0
REMARK 465 GLU H 119
REMARK 465 ASN H 120
REMARK 465 LEU H 121
REMARK 465 TYR H 122
REMARK 465 PHE H 123
REMARK 465 GLN H 124
REMARK 465 GLY L 0
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 SER A 187 OG
REMARK 470 THR A 188 OG1 CG2
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 11 -85.36 62.26
REMARK 500 GLU A 53 -133.45 -90.86
REMARK 500 ASN A 94 -5.53 64.75
REMARK 500 ARG A 108 -84.11 -118.64
REMARK 500 CYS A 148 -84.00 -122.88
REMARK 500 ASN A 168 -115.79 59.68
REMARK 500 THR A 195 -156.89 -84.81
REMARK 500 ASN A 198 70.34 60.73
REMARK 500 GLU A 199 118.03 -162.77
REMARK 500 HIS A 223 -105.81 58.56
REMARK 500 GLU A 242 -120.69 59.34
REMARK 500 TRP A 244 -23.95 -140.08
REMARK 500 SER A 286 -73.84 56.07
REMARK 500 GLN A 287 72.72 -67.09
REMARK 500 ARG A 335 -75.00 -76.72
REMARK 500 ASN A 338 -135.20 -98.61
REMARK 500 LYS A 373 -72.59 -74.36
REMARK 500 ASN A 374 0.66 -68.12
REMARK 500 LEU A 379 -103.87 -80.88
REMARK 500 LEU A 398 95.52 -69.30
REMARK 500 ASP A 405 4.02 -62.48
REMARK 500 CYS A 458 -77.48 -77.73
REMARK 500 SER A 471 -155.66 -119.46
REMARK 500 ASN A 473 -1.15 -149.14
REMARK 500 ASN A 504 81.25 -63.69
REMARK 500 ASP A 509 -0.95 -141.88
REMARK 500 ASP A 512 -144.94 58.06
REMARK 500 SER A 516 36.86 -77.19
REMARK 500 SER A 518 -67.67 -144.75
REMARK 500 GLU A 560 77.76 -67.59
REMARK 500 ASP A 562 5.23 -69.18
REMARK 500 ARG A 565 -79.45 -111.12
REMARK 500 ASP A 586 74.63 56.86
REMARK 500 ASN A 754 -58.85 -124.95
REMARK 500 ASN A 762 82.89 57.32
REMARK 500 GLU A 815 -152.53 61.03
REMARK 500 ASN A 816 57.81 -104.64
REMARK 500 ARG A 865 83.72 56.82
REMARK 500 THR A 898 95.26 -61.90
REMARK 500 GLN B 40 39.38 -95.74
REMARK 500 GLU B 46 -49.49 -133.03
REMARK 500 ARG H 85 56.77 39.40
REMARK 500 SER H 98 -155.50 -158.20
REMARK 500 ASP H 101 -167.57 -163.97
REMARK 500 ASN L 31 -118.97 -127.62
REMARK 500 ALA L 51 -32.39 68.99
REMARK 500 SER L 52 -56.77 -128.92
REMARK 500 SER L 91 11.70 -142.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5U8R RELATED DB: PDB
REMARK 900 THE SAME COMPLEX WITHOUT IGF-I
DBREF 5U8Q A 1 905 UNP P08069 IGF1R_HUMAN 31 935
DBREF 5U8Q B 1 70 UNP P05019 IGF1_HUMAN 49 118
DBREF 5U8Q H -1 124 PDB 5U8Q 5U8Q -1 124
DBREF 5U8Q L 0 107 PDB 5U8Q 5U8Q 0 107
SEQADV 5U8Q A UNP P08069 THR 748 DELETION
SEQADV 5U8Q A UNP P08069 THR 749 DELETION
SEQADV 5U8Q A UNP P08069 MET 750 DELETION
SEQADV 5U8Q A UNP P08069 SER 751 DELETION
SEQADV 5U8Q A UNP P08069 SER 752 DELETION
SEQADV 5U8Q A UNP P08069 ARG 753 DELETION
SEQADV 5U8Q A UNP P08069 SER 754 DELETION
SEQADV 5U8Q A UNP P08069 ARG 755 DELETION
SEQADV 5U8Q A UNP P08069 ASN 756 DELETION
SEQADV 5U8Q A UNP P08069 THR 757 DELETION
SEQADV 5U8Q A UNP P08069 THR 758 DELETION
SEQADV 5U8Q A UNP P08069 ALA 759 DELETION
SEQADV 5U8Q A UNP P08069 ALA 760 DELETION
SEQADV 5U8Q A UNP P08069 ASP 761 DELETION
SEQADV 5U8Q A UNP P08069 THR 762 DELETION
SEQADV 5U8Q A UNP P08069 TYR 763 DELETION
SEQADV 5U8Q A UNP P08069 ASN 764 DELETION
SEQADV 5U8Q A UNP P08069 ILE 765 DELETION
SEQADV 5U8Q A UNP P08069 THR 766 DELETION
SEQADV 5U8Q A UNP P08069 ASP 767 DELETION
SEQADV 5U8Q ALA A 738 UNP P08069 PRO 768 CONFLICT
SEQADV 5U8Q GLY A 739 UNP P08069 GLU 769 CONFLICT
SEQADV 5U8Q ASN A 740 UNP P08069 GLU 770 CONFLICT
SEQADV 5U8Q ASN A 741 UNP P08069 LEU 771 CONFLICT
SEQRES 1 A 885 GLU ILE CYS GLY PRO GLY ILE ASP ILE ARG ASN ASP TYR
SEQRES 2 A 885 GLN GLN LEU LYS ARG LEU GLU ASN CYS THR VAL ILE GLU
SEQRES 3 A 885 GLY TYR LEU HIS ILE LEU LEU ILE SER LYS ALA GLU ASP
SEQRES 4 A 885 TYR ARG SER TYR ARG PHE PRO LYS LEU THR VAL ILE THR
SEQRES 5 A 885 GLU TYR LEU LEU LEU PHE ARG VAL ALA GLY LEU GLU SER
SEQRES 6 A 885 LEU GLY ASP LEU PHE PRO ASN LEU THR VAL ILE ARG GLY
SEQRES 7 A 885 TRP LYS LEU PHE TYR ASN TYR ALA LEU VAL ILE PHE GLU
SEQRES 8 A 885 MET THR ASN LEU LYS ASP ILE GLY LEU TYR ASN LEU ARG
SEQRES 9 A 885 ASN ILE THR ARG GLY ALA ILE ARG ILE GLU LYS ASN ALA
SEQRES 10 A 885 ASP LEU CYS TYR LEU SER THR VAL ASP TRP SER LEU ILE
SEQRES 11 A 885 LEU ASP ALA VAL SER ASN ASN TYR ILE VAL GLY ASN LYS
SEQRES 12 A 885 PRO PRO LYS GLU CYS GLY ASP LEU CYS PRO GLY THR MET
SEQRES 13 A 885 GLU GLU LYS PRO MET CYS GLU LYS THR THR ILE ASN ASN
SEQRES 14 A 885 GLU TYR ASN TYR ARG CYS TRP THR THR ASN ARG CYS GLN
SEQRES 15 A 885 LYS MET CYS PRO SER THR CYS GLY LYS ARG ALA CYS THR
SEQRES 16 A 885 GLU ASN ASN GLU CYS CYS HIS PRO GLU CYS LEU GLY SER
SEQRES 17 A 885 CYS SER ALA PRO ASP ASN ASP THR ALA CYS VAL ALA CYS
SEQRES 18 A 885 ARG HIS TYR TYR TYR ALA GLY VAL CYS VAL PRO ALA CYS
SEQRES 19 A 885 PRO PRO ASN THR TYR ARG PHE GLU GLY TRP ARG CYS VAL
SEQRES 20 A 885 ASP ARG ASP PHE CYS ALA ASN ILE LEU SER ALA GLU SER
SEQRES 21 A 885 SER ASP SER GLU GLY PHE VAL ILE HIS ASP GLY GLU CYS
SEQRES 22 A 885 MET GLN GLU CYS PRO SER GLY PHE ILE ARG ASN GLY SER
SEQRES 23 A 885 GLN SER MET TYR CYS ILE PRO CYS GLU GLY PRO CYS PRO
SEQRES 24 A 885 LYS VAL CYS GLU GLU GLU LYS LYS THR LYS THR ILE ASP
SEQRES 25 A 885 SER VAL THR SER ALA GLN MET LEU GLN GLY CYS THR ILE
SEQRES 26 A 885 PHE LYS GLY ASN LEU LEU ILE ASN ILE ARG ARG GLY ASN
SEQRES 27 A 885 ASN ILE ALA SER GLU LEU GLU ASN PHE MET GLY LEU ILE
SEQRES 28 A 885 GLU VAL VAL THR GLY TYR VAL LYS ILE ARG HIS SER HIS
SEQRES 29 A 885 ALA LEU VAL SER LEU SER PHE LEU LYS ASN LEU ARG LEU
SEQRES 30 A 885 ILE LEU GLY GLU GLU GLN LEU GLU GLY ASN TYR SER PHE
SEQRES 31 A 885 TYR VAL LEU ASP ASN GLN ASN LEU GLN GLN LEU TRP ASP
SEQRES 32 A 885 TRP ASP HIS ARG ASN LEU THR ILE LYS ALA GLY LYS MET
SEQRES 33 A 885 TYR PHE ALA PHE ASN PRO LYS LEU CYS VAL SER GLU ILE
SEQRES 34 A 885 TYR ARG MET GLU GLU VAL THR GLY THR LYS GLY ARG GLN
SEQRES 35 A 885 SER LYS GLY ASP ILE ASN THR ARG ASN ASN GLY GLU ARG
SEQRES 36 A 885 ALA SER CYS GLU SER ASP VAL LEU HIS PHE THR SER THR
SEQRES 37 A 885 THR THR SER LYS ASN ARG ILE ILE ILE THR TRP HIS ARG
SEQRES 38 A 885 TYR ARG PRO PRO ASP TYR ARG ASP LEU ILE SER PHE THR
SEQRES 39 A 885 VAL TYR TYR LYS GLU ALA PRO PHE LYS ASN VAL THR GLU
SEQRES 40 A 885 TYR ASP GLY GLN ASP ALA CYS GLY SER ASN SER TRP ASN
SEQRES 41 A 885 MET VAL ASP VAL ASP LEU PRO PRO ASN LYS ASP VAL GLU
SEQRES 42 A 885 PRO GLY ILE LEU LEU HIS GLY LEU LYS PRO TRP THR GLN
SEQRES 43 A 885 TYR ALA VAL TYR VAL LYS ALA VAL THR LEU THR MET VAL
SEQRES 44 A 885 GLU ASN ASP HIS ILE ARG GLY ALA LYS SER GLU ILE LEU
SEQRES 45 A 885 TYR ILE ARG THR ASN ALA SER VAL PRO SER ILE PRO LEU
SEQRES 46 A 885 ASP VAL LEU SER ALA SER ASN SER SER SER GLN LEU ILE
SEQRES 47 A 885 VAL LYS TRP ASN PRO PRO SER LEU PRO ASN GLY ASN LEU
SEQRES 48 A 885 SER TYR TYR ILE VAL ARG TRP GLN ARG GLN PRO GLN ASP
SEQRES 49 A 885 GLY TYR LEU TYR ARG HIS ASN TYR CYS SER LYS ASP LYS
SEQRES 50 A 885 ILE PRO ILE ARG LYS TYR ALA ASP GLY THR ILE ASP ILE
SEQRES 51 A 885 GLU GLU VAL THR GLU ASN PRO LYS THR GLU VAL CYS GLY
SEQRES 52 A 885 GLY GLU LYS GLY PRO CYS CYS ALA CYS PRO LYS THR GLU
SEQRES 53 A 885 ALA GLU LYS GLN ALA GLU LYS GLU GLU ALA GLU TYR ARG
SEQRES 54 A 885 LYS VAL PHE GLU ASN PHE LEU HIS ASN SER ILE PHE VAL
SEQRES 55 A 885 PRO ARG PRO GLU ARG LYS ARG ARG ASP VAL MET GLN VAL
SEQRES 56 A 885 ALA ASN ALA GLY ASN ASN GLU THR GLU TYR PRO PHE PHE
SEQRES 57 A 885 GLU SER ARG VAL ASP ASN LYS GLU ARG THR VAL ILE SER
SEQRES 58 A 885 ASN LEU ARG PRO PHE THR LEU TYR ARG ILE ASP ILE HIS
SEQRES 59 A 885 SER CYS ASN HIS GLU ALA GLU LYS LEU GLY CYS SER ALA
SEQRES 60 A 885 SER ASN PHE VAL PHE ALA ARG THR MET PRO ALA GLU GLY
SEQRES 61 A 885 ALA ASP ASP ILE PRO GLY PRO VAL THR TRP GLU PRO ARG
SEQRES 62 A 885 PRO GLU ASN SER ILE PHE LEU LYS TRP PRO GLU PRO GLU
SEQRES 63 A 885 ASN PRO ASN GLY LEU ILE LEU MET TYR GLU ILE LYS TYR
SEQRES 64 A 885 GLY SER GLN VAL GLU ASP GLN ARG GLU CYS VAL SER ARG
SEQRES 65 A 885 GLN GLU TYR ARG LYS TYR GLY GLY ALA LYS LEU ASN ARG
SEQRES 66 A 885 LEU ASN PRO GLY ASN TYR THR ALA ARG ILE GLN ALA THR
SEQRES 67 A 885 SER LEU SER GLY ASN GLY SER TRP THR ASP PRO VAL PHE
SEQRES 68 A 885 PHE TYR VAL GLN ALA LYS THR GLY TYR GLU ASN PHE ILE
SEQRES 69 A 885 HIS
SEQRES 1 B 70 GLY PRO GLU THR LEU CYS GLY ALA GLU LEU VAL ASP ALA
SEQRES 2 B 70 LEU GLN PHE VAL CYS GLY ASP ARG GLY PHE TYR PHE ASN
SEQRES 3 B 70 LYS PRO THR GLY TYR GLY SER SER SER ARG ARG ALA PRO
SEQRES 4 B 70 GLN THR GLY ILE VAL ASP GLU CYS CYS PHE ARG SER CYS
SEQRES 5 B 70 ASP LEU ARG ARG LEU GLU MET TYR CYS ALA PRO LEU LYS
SEQRES 6 B 70 PRO ALA LYS SER ALA
SEQRES 1 H 126 GLY THR GLN VAL GLN LEU GLN GLN SER GLY PRO ASP VAL
SEQRES 2 H 126 VAL ARG PRO GLY VAL SER VAL LYS ILE SER CYS LYS GLY
SEQRES 3 H 126 SER GLY TYR THR PHE THR ASP TYR ALA ILE HIS TRP VAL
SEQRES 4 H 126 LYS GLN SER HIS ALA LYS SER LEU GLU TRP ILE GLY VAL
SEQRES 5 H 126 ILE SER THR TYR ASN GLY ASN THR LYS TYR ASN GLN LYS
SEQRES 6 H 126 PHE LYS GLY LYS ALA ALA ILE THR VAL ASP LYS SER SER
SEQRES 7 H 126 SER THR ALA TYR LEU GLU LEU ALA ARG LEU THR SER GLU
SEQRES 8 H 126 ASP SER ALA ILE TYR TYR CYS ALA SER TYR GLY ASP LEU
SEQRES 9 H 126 TYR VAL MET ASP TYR TRP GLY GLN GLY THR SER VAL THR
SEQRES 10 H 126 VAL SER SER GLU ASN LEU TYR PHE GLN
SEQRES 1 L 108 GLY ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER
SEQRES 2 L 108 VAL THR PRO GLY ASP SER VAL SER LEU SER CYS ARG ALA
SEQRES 3 L 108 SER GLN THR ILE SER ASN ASN LEU HIS TRP TYR GLN GLN
SEQRES 4 L 108 LYS SER HIS GLU SER PRO ARG LEU LEU ILE LYS TYR ALA
SEQRES 5 L 108 SER GLN SER ILE SER GLY ILE PRO SER ARG PHE SER GLY
SEQRES 6 L 108 SER GLY SER GLY THR ASP PHE THR LEU SER ILE ASN SER
SEQRES 7 L 108 VAL GLU THR GLU ASP PHE GLY MET TYR PHE CYS GLN GLN
SEQRES 8 L 108 SER ASN SER TRP PRO ARG THR PHE GLY ALA GLY THR LYS
SEQRES 9 L 108 LEU GLU LEU LYS
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET MAN D 3 11
HET MAN D 4 11
HET NAG E 1 14
HET NAG E 2 14
HET SO4 A1001 5
HET SO4 A1002 5
HET MLT A1003 9
HET NAG A1004 14
HET NAG A1007 14
HET NAG A1012 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM MLT D-MALATE
HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID
FORMUL 5 NAG 9(C8 H15 N O6)
FORMUL 6 MAN 2(C6 H12 O6)
FORMUL 8 SO4 2(O4 S 2-)
FORMUL 10 MLT C4 H6 O5
HELIX 1 AA1 TYR A 13 GLU A 20 5 8
HELIX 2 AA2 SER A 65 LEU A 69 5 5
HELIX 3 AA3 PRO A 144 CYS A 148 5 5
HELIX 4 AA4 ARG A 249 ALA A 253 1 5
HELIX 5 AA5 THR A 315 GLN A 321 5 7
HELIX 6 AA6 ILE A 340 MET A 348 1 9
HELIX 7 AA7 GLY A 349 ILE A 351 5 3
HELIX 8 AA8 CYS A 425 GLY A 437 1 13
HELIX 9 AA9 ASP A 624 ARG A 629 5 6
HELIX 10 AB1 LYS A 690 PHE A 701 1 12
HELIX 11 AB2 ARG A 852 GLY A 859 1 8
HELIX 12 AB3 GLY B 7 GLY B 19 1 13
HELIX 13 AB4 ILE B 43 CYS B 48 1 6
HELIX 14 AB5 ASP B 53 MET B 59 1 7
HELIX 15 AB6 THR H 28 TYR H 32 5 5
HELIX 16 AB7 GLN H 62 LYS H 65 5 4
HELIX 17 AB8 THR H 87 SER H 91 5 5
HELIX 18 AB9 LYS L 49 GLN L 53 5 5
SHEET 1 AA1 5 ILE A 2 CYS A 3 0
SHEET 2 AA1 5 VAL A 24 ILE A 25 1 O VAL A 24 N CYS A 3
SHEET 3 AA1 5 VAL A 50 ILE A 51 1 O VAL A 50 N ILE A 25
SHEET 4 AA1 5 VAL A 75 ILE A 76 1 O VAL A 75 N ILE A 51
SHEET 5 AA1 5 ASN A 105 ILE A 106 1 O ASN A 105 N ILE A 76
SHEET 1 AA2 6 ILE A 7 ARG A 10 0
SHEET 2 AA2 6 LEU A 29 ILE A 34 1 O HIS A 30 N ILE A 9
SHEET 3 AA2 6 LEU A 55 VAL A 60 1 O LEU A 56 N LEU A 29
SHEET 4 AA2 6 TYR A 85 PHE A 90 1 O VAL A 88 N LEU A 57
SHEET 5 AA2 6 ALA A 110 GLU A 114 1 O ALA A 110 N ALA A 86
SHEET 6 AA2 6 TYR A 138 VAL A 140 1 O TYR A 138 N ILE A 113
SHEET 1 AA3 2 LYS A 164 ILE A 167 0
SHEET 2 AA3 2 GLU A 170 TYR A 173 -1 O GLU A 170 N ILE A 167
SHEET 1 AA4 2 CYS A 205 CYS A 209 0
SHEET 2 AA4 2 CYS A 218 CYS A 221 -1 O ALA A 220 N LEU A 206
SHEET 1 AA5 2 TYR A 224 TYR A 226 0
SHEET 2 AA5 2 VAL A 229 VAL A 231 -1 O VAL A 229 N TYR A 226
SHEET 1 AA6 4 ARG A 245 ASP A 248 0
SHEET 2 AA6 4 THR A 238 PHE A 241 -1 N TYR A 239 O VAL A 247
SHEET 3 AA6 4 GLU A 272 MET A 274 1 O CYS A 273 N ARG A 240
SHEET 4 AA6 4 VAL A 267 HIS A 269 -1 N HIS A 269 O GLU A 272
SHEET 1 AA7 2 ILE A 282 ARG A 283 0
SHEET 2 AA7 2 CYS A 291 ILE A 292 -1 O ILE A 292 N ILE A 282
SHEET 1 AA8 4 CYS A 302 ILE A 311 0
SHEET 2 AA8 4 ILE A 325 ILE A 332 1 O LEU A 331 N ILE A 311
SHEET 3 AA8 4 VAL A 353 VAL A 354 1 O VAL A 353 N PHE A 326
SHEET 4 AA8 4 LEU A 377 ILE A 378 1 O LEU A 377 N VAL A 354
SHEET 1 AA9 5 CYS A 302 ILE A 311 0
SHEET 2 AA9 5 ILE A 325 ILE A 332 1 O LEU A 331 N ILE A 311
SHEET 3 AA9 5 VAL A 358 ARG A 361 1 O LYS A 359 N ILE A 332
SHEET 4 AA9 5 TYR A 388 LEU A 393 1 O SER A 389 N VAL A 358
SHEET 5 AA9 5 LYS A 415 ALA A 419 1 O TYR A 417 N VAL A 392
SHEET 1 AB1 2 ASP A 461 LEU A 463 0
SHEET 2 AB1 2 ALA A 567 SER A 569 1 O LYS A 568 N ASP A 461
SHEET 1 AB2 3 PHE A 465 THR A 470 0
SHEET 2 AB2 3 ILE A 475 TRP A 479 -1 O THR A 478 N THR A 466
SHEET 3 AB2 3 GLY A 535 LEU A 538 -1 O LEU A 538 N ILE A 475
SHEET 1 AB3 4 ASN A 520 VAL A 522 0
SHEET 2 AB3 4 LEU A 490 GLU A 499 -1 N VAL A 495 O VAL A 522
SHEET 3 AB3 4 GLN A 546 LEU A 556 -1 O VAL A 554 N SER A 492
SHEET 4 AB3 4 LEU A 572 ARG A 575 -1 O ILE A 574 N TYR A 547
SHEET 1 AB4 3 LEU A 585 ALA A 590 0
SHEET 2 AB4 3 GLN A 596 ASN A 602 -1 O ASN A 602 N LEU A 585
SHEET 3 AB4 3 ARG A 757 SER A 761 -1 O ILE A 760 N LEU A 597
SHEET 1 AB5 4 PHE A 747 VAL A 752 0
SHEET 2 AB5 4 LEU A 611 ARG A 620 -1 N TYR A 614 O VAL A 752
SHEET 3 AB5 4 LEU A 768 ASN A 777 -1 O ASP A 772 N ARG A 617
SHEET 4 AB5 4 VAL A 791 ARG A 794 -1 O VAL A 791 N ILE A 771
SHEET 1 AB6 3 THR A 809 ARG A 813 0
SHEET 2 AB6 3 SER A 817 LYS A 821 -1 O LYS A 821 N THR A 809
SHEET 3 AB6 3 GLY A 860 LEU A 863 -1 O LEU A 863 N ILE A 818
SHEET 1 AB7 4 GLN A 846 SER A 851 0
SHEET 2 AB7 4 ILE A 832 GLY A 840 -1 N TYR A 835 O VAL A 850
SHEET 3 AB7 4 GLY A 869 SER A 879 -1 O ARG A 874 N LYS A 838
SHEET 4 AB7 4 VAL A 890 VAL A 894 -1 O VAL A 890 N ALA A 873
SHEET 1 AB8 4 GLN H 3 GLN H 6 0
SHEET 2 AB8 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5
SHEET 3 AB8 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18
SHEET 4 AB8 4 ALA H 68 ASP H 73 -1 N ALA H 69 O GLU H 82
SHEET 1 AB9 6 ASP H 10 VAL H 12 0
SHEET 2 AB9 6 THR H 112 VAL H 116 1 O SER H 113 N ASP H 10
SHEET 3 AB9 6 ILE H 93 SER H 98 -1 N TYR H 94 O THR H 112
SHEET 4 AB9 6 ILE H 34 GLN H 39 -1 N HIS H 35 O ALA H 97
SHEET 5 AB9 6 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38
SHEET 6 AB9 6 THR H 58 TYR H 60 -1 O LYS H 59 N VAL H 50
SHEET 1 AC1 4 ASP H 10 VAL H 12 0
SHEET 2 AC1 4 THR H 112 VAL H 116 1 O SER H 113 N ASP H 10
SHEET 3 AC1 4 ILE H 93 SER H 98 -1 N TYR H 94 O THR H 112
SHEET 4 AC1 4 TYR H 107 TRP H 108 -1 O TYR H 107 N SER H 98
SHEET 1 AC2 3 LEU L 4 THR L 5 0
SHEET 2 AC2 3 VAL L 19 ILE L 29 -1 O ARG L 24 N THR L 5
SHEET 3 AC2 3 PHE L 62 ILE L 75 -1 O LEU L 73 N LEU L 21
SHEET 1 AC3 5 THR L 10 VAL L 13 0
SHEET 2 AC3 5 THR L 102 LEU L 106 1 O GLU L 105 N VAL L 13
SHEET 3 AC3 5 MET L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AC3 5 LEU L 33 GLN L 38 -1 N HIS L 34 O GLN L 89
SHEET 5 AC3 5 ARG L 45 ILE L 48 -1 O ARG L 45 N GLN L 37
SHEET 1 AC4 4 THR L 10 VAL L 13 0
SHEET 2 AC4 4 THR L 102 LEU L 106 1 O GLU L 105 N VAL L 13
SHEET 3 AC4 4 MET L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 AC4 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SSBOND 1 CYS A 3 CYS A 22 1555 1555 2.03
SSBOND 2 CYS A 120 CYS A 148 1555 1555 2.03
SSBOND 3 CYS A 152 CYS A 175 1555 1555 2.03
SSBOND 4 CYS A 162 CYS A 181 1555 1555 2.03
SSBOND 5 CYS A 185 CYS A 194 1555 1555 2.03
SSBOND 6 CYS A 189 CYS A 200 1555 1555 2.03
SSBOND 7 CYS A 201 CYS A 209 1555 1555 2.03
SSBOND 8 CYS A 205 CYS A 218 1555 1555 2.03
SSBOND 9 CYS A 221 CYS A 230 1555 1555 2.03
SSBOND 10 CYS A 234 CYS A 246 1555 1555 2.03
SSBOND 11 CYS A 252 CYS A 273 1555 1555 2.03
SSBOND 12 CYS A 277 CYS A 291 1555 1555 2.03
SSBOND 13 CYS A 294 CYS A 298 1555 1555 2.03
SSBOND 14 CYS A 302 CYS A 323 1555 1555 2.03
SSBOND 15 CYS A 425 CYS A 458 1555 1555 2.03
SSBOND 16 CYS A 514 CYS A 514 1555 2555 2.03
SSBOND 17 CYS A 633 CYS A 849 1555 1555 2.03
SSBOND 18 CYS A 776 CYS A 785 1555 1555 2.04
SSBOND 19 CYS B 6 CYS B 48 1555 1555 2.03
SSBOND 20 CYS B 18 CYS B 61 1555 1555 2.03
SSBOND 21 CYS B 47 CYS B 52 1555 1555 2.03
SSBOND 22 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 23 CYS L 23 CYS L 88 1555 1555 2.03
LINK ND2 ASN A 21 C1 NAG A1004 1555 1555 1.44
LINK ND2 ASN A 105 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 504 C1 NAG A1007 1555 1555 1.44
LINK ND2 ASN A 577 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 870 C1 NAG A1012 1555 1555 1.44
LINK ND2 ASN A 883 C1 NAG E 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG D 2 C1 MAN D 3 1555 1555 1.44
LINK O4 MAN D 3 C1 MAN D 4 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
CISPEP 1 GLY A 4 PRO A 5 0 -0.32
CISPEP 2 TRP L 94 PRO L 95 0 -1.43
CRYST1 88.690 197.660 117.650 90.00 90.00 90.00 P 21 21 2 4
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 0.011275 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005059 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008500 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
