HEADER HORMONE/HORMONE RECEPTOR 22-JAN-15 4XSS
TITLE INSULIN-LIKE GROWTH FACTOR I IN COMPLEX WITH SITE 1 OF A HYBRID
TITLE 2 INSULIN RECEPTOR / TYPE 1 INSULIN-LIKE GROWTH FACTOR RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR I;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: UNP RESIDUES 49-118;
COMPND 5 SYNONYM: IGF-I,MECHANO GROWTH FACTOR,MGF,SOMATOMEDIN-C;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: INSULIN RECEPTOR;
COMPND 9 CHAIN: E;
COMPND 10 FRAGMENT: L1-CR, UNP RESIDUES 28-377;
COMPND 11 SYNONYM: IR;
COMPND 12 EC: 2.7.10.1;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: INSULIN-LIKE GROWTH FACTOR RECEPTOR ALPHA-CT PEPTIDE;
COMPND 16 CHAIN: F;
COMPND 17 FRAGMENT: ALPHA-CT PEPTIDE, UNP RESIDUES 691-706;
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: IGF1, IBP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: INSR;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: LEC 8 MUTANT CHO CELL;
SOURCE 16 MOL_ID: 3;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS CELL SURFACE RECEPTOR/IMMUNE SYSTEM, INSULIN RECEPTOR, CT PEPTIDE,
KEYWDS 2 INSULIN-LIKE GROWTH FACTOR RECEPTOR, HORMONE RECEPTOR-HORMONE-IMMUNE
KEYWDS 3 SYSTEM COMPLEX, HORMONE-HORMONE RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.LAWRENCE,G.K.-W.KONG,J.G.MENTING,M.C.LAWRENCE
REVDAT 6 27-SEP-23 4XSS 1 HETSYN LINK
REVDAT 5 29-JUL-20 4XSS 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 08-JAN-20 4XSS 1 REMARK
REVDAT 3 13-SEP-17 4XSS 1 SOURCE JRNL REMARK
REVDAT 2 22-JUL-15 4XSS 1 JRNL
REVDAT 1 10-JUN-15 4XSS 0
JRNL AUTH J.G.MENTING,C.F.LAWRENCE,G.K.KONG,M.B.MARGETTS,C.W.WARD,
JRNL AUTH 2 M.C.LAWRENCE
JRNL TITL STRUCTURAL CONGRUENCY OF LIGAND BINDING TO THE INSULIN AND
JRNL TITL 2 INSULIN/TYPE 1 INSULIN-LIKE GROWTH FACTOR HYBRID RECEPTORS.
JRNL REF STRUCTURE V. 23 1271 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 26027733
JRNL DOI 10.1016/J.STR.2015.04.016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.G.MENTING
REMARK 1 TITL PROTECTIVE HINGE IN INSULIN OPENS TO ENABLE ITS RECEPTOR
REMARK 1 TITL 2 ENGAGEMENT
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 111 E3395 2014
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.1412897111
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.G.MENTING
REMARK 1 TITL HOW INSULIN ENGAGES ITS PRIMARY BINDING SITE ON THE INSULIN
REMARK 1 TITL 2 RECEPTOR
REMARK 1 REF NATURE V. 493 241 2013
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/NATURE11781
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22377
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1147
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 11
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2931
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2777
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2767
REMARK 3 BIN R VALUE (WORKING SET) : 0.2775
REMARK 3 BIN FREE R VALUE : 0.2808
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 164
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2933
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 148
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 92.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 129.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 19.10080
REMARK 3 B22 (A**2) : 19.10080
REMARK 3 B33 (A**2) : -38.20170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.721
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.332
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.247
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.346
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.254
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3177 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4332 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1126 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 77 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 455 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3177 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 438 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3419 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.25
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.22
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.88
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 142.0555 143.3666 45.7306
REMARK 3 T TENSOR
REMARK 3 T11: -0.6476 T22: -0.7883
REMARK 3 T33: 0.6704 T12: 0.3889
REMARK 3 T13: 0.8037 T23: -0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 2.2478 L22: 8.7352
REMARK 3 L33: 9.6839 L12: -3.0250
REMARK 3 L13: 1.0867 L23: 1.8913
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: 0.5746 S13: -2.1363
REMARK 3 S21: 0.0123 S22: -0.3574 S23: -0.2974
REMARK 3 S31: 1.2200 S32: 0.1681 S33: 0.3603
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 128.9346 167.2206 45.9027
REMARK 3 T TENSOR
REMARK 3 T11: -0.6828 T22: -0.6762
REMARK 3 T33: -0.1839 T12: 0.1434
REMARK 3 T13: 0.3632 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 2.8517 L22: 2.8659
REMARK 3 L33: 1.1623 L12: -0.4041
REMARK 3 L13: 0.1295 L23: -0.0972
REMARK 3 S TENSOR
REMARK 3 S11: -0.1630 S12: 0.4817 S13: -0.4639
REMARK 3 S21: -0.5943 S22: -0.1575 S23: -0.4756
REMARK 3 S31: 0.3562 S32: 0.2240 S33: 0.3205
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 139.6418 148.7233 49.9330
REMARK 3 T TENSOR
REMARK 3 T11: -0.3123 T22: -0.3434
REMARK 3 T33: 1.0836 T12: 0.4428
REMARK 3 T13: 0.6473 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: -2.5632 L22: 8.8765
REMARK 3 L33: 0.8881 L12: 0.1672
REMARK 3 L13: 4.3463 L23: -6.0600
REMARK 3 S TENSOR
REMARK 3 S11: 0.0726 S12: 0.4225 S13: -1.5662
REMARK 3 S21: 0.3789 S22: -0.4624 S23: -0.6519
REMARK 3 S31: 0.7470 S32: -0.4015 S33: 0.3898
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4XSS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 (SI111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22377
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 2.11000
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: 3LOH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75 M AMMONIUM SULFATE, 0.1 M CAPS
REMARK 280 -NAOH (PH 10.5), 0.2 M LISO4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 109.58000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.26604
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 40.40667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 109.58000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 63.26604
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 40.40667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 109.58000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 63.26604
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 40.40667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 109.58000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 63.26604
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 40.40667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 109.58000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 63.26604
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 40.40667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 109.58000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 63.26604
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 40.40667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 126.53208
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 80.81333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 126.53208
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 80.81333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 126.53208
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 80.81333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 126.53208
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 80.81333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 126.53208
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 80.81333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 126.53208
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 80.81333
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 45600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 107910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, F, 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 BIOMT1 2 -0.500000 -0.866025 0.000000 328.74000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 189.79813
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 379.59625
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 121.22000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 379.59625
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 121.22000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 328.74000
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 189.79813
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 121.22000
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 GLY B 1
REMARK 465 PRO B 2
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 PRO B 39
REMARK 465 GLN B 40
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 LYS E 310
REMARK 465 SER E 311
REMARK 465 SER E 312
REMARK 465 SER E 313
REMARK 465 LEU E 314
REMARK 465 VAL E 315
REMARK 465 PRO E 316
REMARK 465 ARG E 317
REMARK 465 VAL F 691
REMARK 465 PHE F 692
REMARK 465 PRO F 705
REMARK 465 GLU F 706
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 E 15 -57.90 66.71
REMARK 500 ASP E 59 -101.89 -101.87
REMARK 500 ASN E 90 5.55 88.10
REMARK 500 GLU E 153 57.87 -112.21
REMARK 500 ASP E 157 112.13 -28.35
REMARK 500 LYS E 197 -131.46 51.75
REMARK 500 ASN E 230 -88.92 -109.04
REMARK 500 ASP E 234 67.28 32.89
REMARK 500 PRO E 244 31.62 -97.87
REMARK 500 TRP E 251 -18.01 -151.43
REMARK 500 LYS E 267 -84.79 -92.69
REMARK 500 SER E 269 77.95 60.99
REMARK 500 ARG E 271 -169.86 -71.85
REMARK 500 GLN E 272 15.45 53.90
REMARK 500 ASN E 298 19.82 -151.02
REMARK 500 LEU E 299 15.74 52.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W11 RELATED DB: PDB
REMARK 900 RELATED ID: 3W12 RELATED DB: PDB
REMARK 900 RELATED ID: 3W13 RELATED DB: PDB
REMARK 900 RELATED ID: 3W14 RELATED DB: PDB
REMARK 900 RELATED ID: 4OGA RELATED DB: PDB
REMARK 900 RELATED ID: 4XST RELATED DB: PDB
DBREF 4XSS B 1 70 UNP P05019 IGF1_HUMAN 49 118
DBREF 4XSS E 1 310 UNP P06213 INSR_HUMAN 28 337
DBREF 4XSS F 691 706 PDB 4XSS 4XSS 691 706
SEQADV 4XSS HIS E 144 UNP P06213 TYR 171 CONFLICT
SEQADV 4XSS SER E 311 UNP P06213 EXPRESSION TAG
SEQADV 4XSS SER E 312 UNP P06213 EXPRESSION TAG
SEQADV 4XSS SER E 313 UNP P06213 EXPRESSION TAG
SEQADV 4XSS LEU E 314 UNP P06213 EXPRESSION TAG
SEQADV 4XSS VAL E 315 UNP P06213 EXPRESSION TAG
SEQADV 4XSS PRO E 316 UNP P06213 EXPRESSION TAG
SEQADV 4XSS ARG E 317 UNP P06213 EXPRESSION TAG
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 E 317 HIS LEU TYR PRO GLY GLU VAL CYS PRO GLY MET ASP ILE
SEQRES 2 E 317 ARG ASN ASN LEU THR ARG LEU HIS GLU LEU GLU ASN CYS
SEQRES 3 E 317 SER VAL ILE GLU GLY HIS LEU GLN ILE LEU LEU MET PHE
SEQRES 4 E 317 LYS THR ARG PRO GLU ASP PHE ARG ASP LEU SER PHE PRO
SEQRES 5 E 317 LYS LEU ILE MET ILE THR ASP TYR LEU LEU LEU PHE ARG
SEQRES 6 E 317 VAL TYR GLY LEU GLU SER LEU LYS ASP LEU PHE PRO ASN
SEQRES 7 E 317 LEU THR VAL ILE ARG GLY SER ARG LEU PHE PHE ASN TYR
SEQRES 8 E 317 ALA LEU VAL ILE PHE GLU MET VAL HIS LEU LYS GLU LEU
SEQRES 9 E 317 GLY LEU TYR ASN LEU MET ASN ILE THR ARG GLY SER VAL
SEQRES 10 E 317 ARG ILE GLU LYS ASN ASN GLU LEU CYS TYR LEU ALA THR
SEQRES 11 E 317 ILE ASP TRP SER ARG ILE LEU ASP SER VAL GLU ASP ASN
SEQRES 12 E 317 HIS ILE VAL LEU ASN LYS ASP ASP ASN GLU GLU CYS GLY
SEQRES 13 E 317 ASP ILE CYS PRO GLY THR ALA LYS GLY LYS THR ASN CYS
SEQRES 14 E 317 PRO ALA THR VAL ILE ASN GLY GLN PHE VAL GLU ARG CYS
SEQRES 15 E 317 TRP THR HIS SER HIS CYS GLN LYS VAL CYS PRO THR ILE
SEQRES 16 E 317 CYS LYS SER HIS GLY CYS THR ALA GLU GLY LEU CYS CYS
SEQRES 17 E 317 HIS SER GLU CYS LEU GLY ASN CYS SER GLN PRO ASP ASP
SEQRES 18 E 317 PRO THR LYS CYS VAL ALA CYS ARG ASN PHE TYR LEU ASP
SEQRES 19 E 317 GLY ARG CYS VAL GLU THR CYS PRO PRO PRO TYR TYR HIS
SEQRES 20 E 317 PHE GLN ASP TRP ARG CYS VAL ASN PHE SER PHE CYS GLN
SEQRES 21 E 317 ASP LEU HIS HIS LYS CYS LYS ASN SER ARG ARG GLN GLY
SEQRES 22 E 317 CYS HIS GLN TYR VAL ILE HIS ASN ASN LYS CYS ILE PRO
SEQRES 23 E 317 GLU CYS PRO SER GLY TYR THR MET ASN SER SER ASN LEU
SEQRES 24 E 317 LEU CYS THR PRO CYS LEU GLY PRO CYS PRO LYS SER SER
SEQRES 25 E 317 SER LEU VAL PRO ARG
SEQRES 1 F 16 VAL PHE GLU ASN PHE LEU HIS ASN SER ILE PHE VAL PRO
SEQRES 2 F 16 ARG PRO GLU
HET NAG A 1 14
HET NAG A 2 14
HET BMA A 3 11
HET FUC A 4 10
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET SO4 E 401 5
HET NAG E 402 14
HET NAG E 407 14
HET NAG E 408 14
HET NAG E 412 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 4 NAG 8(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 FUC 2(C6 H12 O5)
FORMUL 6 SO4 O4 S 2-
HELIX 1 AA1 CYS B 6 GLY B 19 1 14
HELIX 2 AA2 ASP B 20 GLY B 22 5 3
HELIX 3 AA3 GLY B 42 CYS B 48 1 7
HELIX 4 AA4 ASP B 53 GLU B 58 1 6
HELIX 5 AA5 MET B 59 CYS B 61 5 3
HELIX 6 AA6 LEU E 17 GLU E 24 5 8
HELIX 7 AA7 ARG E 42 ARG E 47 5 6
HELIX 8 AA8 ASP E 132 ILE E 136 5 5
HELIX 9 AA9 ASP E 150 ASN E 152 5 3
HELIX 10 AB1 PRO E 193 GLY E 200 5 8
HELIX 11 AB2 PHE E 256 HIS E 264 1 9
HELIX 12 AB3 ASN F 694 PHE F 701 1 8
SHEET 1 AA1 5 GLU E 6 ARG E 14 0
SHEET 2 AA1 5 CYS E 26 MET E 38 1 O GLU E 30 N CYS E 8
SHEET 3 AA1 5 MET E 56 ILE E 57 1 O MET E 56 N ILE E 29
SHEET 4 AA1 5 VAL E 81 ILE E 82 1 O VAL E 81 N ILE E 57
SHEET 5 AA1 5 ASN E 111 ILE E 112 1 O ASN E 111 N ILE E 82
SHEET 1 AA2 6 GLU E 6 ARG E 14 0
SHEET 2 AA2 6 CYS E 26 MET E 38 1 O GLU E 30 N CYS E 8
SHEET 3 AA2 6 LEU E 61 VAL E 66 1 O LEU E 62 N LEU E 33
SHEET 4 AA2 6 TYR E 91 PHE E 96 1 O VAL E 94 N LEU E 63
SHEET 5 AA2 6 SER E 116 ASN E 122 1 O ARG E 118 N LEU E 93
SHEET 6 AA2 6 HIS E 144 ASN E 148 1 O HIS E 144 N VAL E 117
SHEET 1 AA3 2 ALA E 171 ILE E 174 0
SHEET 2 AA3 2 GLN E 177 GLU E 180 -1 O GLN E 177 N ILE E 174
SHEET 1 AA4 2 CYS E 182 THR E 184 0
SHEET 2 AA4 2 HIS E 187 CYS E 188 -1 O HIS E 187 N TRP E 183
SHEET 1 AA5 2 PHE E 231 TYR E 232 0
SHEET 2 AA5 2 CYS E 237 VAL E 238 -1 O VAL E 238 N PHE E 231
SHEET 1 AA6 4 ARG E 252 ASN E 255 0
SHEET 2 AA6 4 TYR E 245 PHE E 248 -1 N TYR E 246 O VAL E 254
SHEET 3 AA6 4 LYS E 283 ILE E 285 1 O CYS E 284 N HIS E 247
SHEET 4 AA6 4 VAL E 278 HIS E 280 -1 N VAL E 278 O ILE E 285
SHEET 1 AA7 2 TYR E 292 MET E 294 0
SHEET 2 AA7 2 CYS E 301 PRO E 303 -1 O THR E 302 N THR E 293
SSBOND 1 CYS B 6 CYS B 48 1555 1555 2.04
SSBOND 2 CYS B 18 CYS B 61 1555 1555 2.05
SSBOND 3 CYS B 47 CYS B 52 1555 1555 2.06
SSBOND 4 CYS E 8 CYS E 26 1555 1555 2.04
SSBOND 5 CYS E 126 CYS E 155 1555 1555 2.04
SSBOND 6 CYS E 159 CYS E 182 1555 1555 2.05
SSBOND 7 CYS E 169 CYS E 188 1555 1555 2.05
SSBOND 8 CYS E 192 CYS E 201 1555 1555 2.04
SSBOND 9 CYS E 196 CYS E 207 1555 1555 2.04
SSBOND 10 CYS E 208 CYS E 216 1555 1555 2.03
SSBOND 11 CYS E 212 CYS E 225 1555 1555 2.01
SSBOND 12 CYS E 228 CYS E 237 1555 1555 2.02
SSBOND 13 CYS E 241 CYS E 253 1555 1555 2.04
SSBOND 14 CYS E 259 CYS E 284 1555 1555 2.04
SSBOND 15 CYS E 266 CYS E 274 1555 1555 2.05
SSBOND 16 CYS E 288 CYS E 301 1555 1555 2.05
SSBOND 17 CYS E 304 CYS E 308 1555 1555 2.05
LINK ND2 ASN E 16 C1 NAG E 402 1555 1555 1.43
LINK ND2 ASN E 25 C1 NAG A 1 1555 1555 1.44
LINK ND2 ASN E 111 C1 NAG E 407 1555 1555 1.44
LINK ND2 ASN E 215 C1 NAG E 408 1555 1555 1.43
LINK ND2 ASN E 255 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN E 295 C1 NAG E 412 1555 1555 1.44
LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.43
LINK O6 NAG A 1 C1 FUC A 4 1555 1555 1.41
LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.43
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.41
CISPEP 1 PRO E 243 PRO E 244 0 10.39
CRYST1 219.160 219.160 121.220 90.00 90.00 120.00 H 3 2 18
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 0.004563 0.002634 0.000000 0.00000
SCALE2 0.000000 0.005269 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008249 0.00000
(ATOM LINES ARE NOT SHOWN.)
END