HEADER TRANSFERASE 15-FEB-17 5UTK
TITLE CRYSTAL STRUCTURE OF THE MEMBRANE PROXIMAL THREE FIBRONECTIN TYPE III
TITLE 2 (FNIII) DOMAINS OF TIE2 (TIE2[FNIIIA-C])
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOPOIETIN-1 RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 399-698;
COMPND 5 SYNONYM: ENDOTHELIAL TYROSINE KINASE,TUNICA INTERNA ENDOTHELIAL CELL
COMPND 6 KINASE,TYROSINE KINASE WITH IG AND EGF HOMOLOGY DOMAINS-2,TYROSINE-
COMPND 7 PROTEIN KINASE RECEPTOR TEK,TYROSINE-PROTEIN KINASE RECEPTOR TIE-2,
COMPND 8 HTIE2,P140 TEK;
COMPND 9 EC: 2.7.10.1;
COMPND 10 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: TEK, TIE2, VMCM, VMCM1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS RECEPTOR TYROSINE KINASE, EXTRACELLULAR REGION, DIMERIZATION,
KEYWDS 2 FIBRONECTIN TYPE III DOMAIN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.O.MOORE,M.A.LEMMON,K.M.FERGUSON
REVDAT 5 04-DEC-19 5UTK 1 REMARK
REVDAT 4 20-SEP-17 5UTK 1 REMARK
REVDAT 3 03-MAY-17 5UTK 1 JRNL
REVDAT 2 26-APR-17 5UTK 1 JRNL
REVDAT 1 12-APR-17 5UTK 0
JRNL AUTH J.O.MOORE,M.A.LEMMON,K.M.FERGUSON
JRNL TITL DIMERIZATION OF TIE2 MEDIATED BY ITS MEMBRANE-PROXIMAL FNIII
JRNL TITL 2 DOMAINS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 4382 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28396397
JRNL DOI 10.1073/PNAS.1617800114
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 30165
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1539
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 49.3375 - 5.5577 0.97 2725 156 0.2117 0.1968
REMARK 3 2 5.5577 - 4.4122 0.99 2683 162 0.1781 0.2097
REMARK 3 3 4.4122 - 3.8547 0.99 2665 150 0.2030 0.2355
REMARK 3 4 3.8547 - 3.5024 0.98 2640 137 0.2188 0.2391
REMARK 3 5 3.5024 - 3.2514 0.99 2639 133 0.2323 0.2370
REMARK 3 6 3.2514 - 3.0597 0.99 2703 124 0.2469 0.2855
REMARK 3 7 3.0597 - 2.9065 0.99 2655 149 0.2626 0.3062
REMARK 3 8 2.9065 - 2.7800 0.99 2631 143 0.2778 0.3368
REMARK 3 9 2.7800 - 2.6730 0.99 2685 145 0.2908 0.3066
REMARK 3 10 2.6730 - 2.5807 0.94 2504 131 0.2951 0.3821
REMARK 3 11 2.5807 - 2.5001 0.78 2096 109 0.3158 0.3337
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.70
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) : 30.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.76
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 : 0.005 4523
REMARK 3 ANGLE : 0.901 6202
REMARK 3 CHIRALITY : 0.056 720
REMARK 3 PLANARITY : 0.004 809
REMARK 3 DIHEDRAL : 13.672 1630
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5UTK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226363.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04, 0.97944, 0.97927, 0.94928
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30201
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.56200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THREE-DIMENSIONAL PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-40% GLYCEROL, 2.5-15% PEG 3K, 100
REMARK 280 MM SODIUM ACETATE, 100 MM SODIUM PHOSPHATE, PH 4.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 87.47500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.01300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 87.47500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 26.01300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLY A 438
REMARK 465 SER A 439
REMARK 465 GLY A 440
REMARK 465 SER A 441
REMARK 465 GLU A 524
REMARK 465 GLY A 525
REMARK 465 LYS A 679
REMARK 465 GLN A 736
REMARK 465 ALA A 737
REMARK 465 PRO A 738
REMARK 465 ALA A 739
REMARK 465 ASP A 740
REMARK 465 LEU A 741
REMARK 465 GLY B 438
REMARK 465 SER B 439
REMARK 465 GLY B 440
REMARK 465 SER B 441
REMARK 465 ARG B 522
REMARK 465 GLY B 523
REMARK 465 GLU B 524
REMARK 465 GLY B 525
REMARK 465 VAL B 583
REMARK 465 GLN B 584
REMARK 465 LYS B 585
REMARK 465 SER B 586
REMARK 465 ASP B 587
REMARK 465 GLN B 588
REMARK 465 GLN B 589
REMARK 465 SER B 735
REMARK 465 GLN B 736
REMARK 465 ALA B 737
REMARK 465 PRO B 738
REMARK 465 ALA B 739
REMARK 465 ASP B 740
REMARK 465 LEU B 741
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 LYS A 442 CG CD CE NZ
REMARK 470 LYS A 446 CG CD CE NZ
REMARK 470 PHE A 471 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 522 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 571 CG CD OE1 OE2
REMARK 470 ASP A 573 CG OD1 OD2
REMARK 470 LYS A 585 CG CD CE NZ
REMARK 470 GLN A 589 CG CD OE1 NE2
REMARK 470 LYS A 620 CG CD CE NZ
REMARK 470 GLN A 622 CG CD OE1 NE2
REMARK 470 GLU A 627 CG CD OE1 OE2
REMARK 470 LYS A 646 CG CD CE NZ
REMARK 470 LYS A 675 CG CD CE NZ
REMARK 470 GLN A 677 CG CD OE1 NE2
REMARK 470 ASN A 680 CG OD1 ND2
REMARK 470 GLU A 681 CG CD OE1 OE2
REMARK 470 LYS A 690 CG CD CE NZ
REMARK 470 GLN A 696 CG CD OE1 NE2
REMARK 470 GLN A 698 CG CD OE1 NE2
REMARK 470 HIS A 727 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 728 CG CD OE1 OE2
REMARK 470 GLU A 734 CG CD OE1 OE2
REMARK 470 LYS B 442 CG CD CE NZ
REMARK 470 LEU B 448 CG CD1 CD2
REMARK 470 GLU B 468 CG CD OE1 OE2
REMARK 470 PHE B 471 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 477 CG CD CE NZ
REMARK 470 LYS B 554 CG CD CE NZ
REMARK 470 ASP B 573 CG OD1 OD2
REMARK 470 SER B 582 OG
REMARK 470 LYS B 592 CG CD CE NZ
REMARK 470 LYS B 620 CG CD CE NZ
REMARK 470 LYS B 646 CG CD CE NZ
REMARK 470 LYS B 679 CG CD CE NZ
REMARK 470 ASN B 680 CG OD1 ND2
REMARK 470 LYS B 690 CG CD CE NZ
REMARK 470 GLU B 705 CG CD OE1 OE2
REMARK 470 HIS B 727 CG ND1 CD2 CE1 NE2
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 OE1 GLU A 508 O HOH A 801 1.75
REMARK 500 O HOH B 807 O HOH B 838 1.88
REMARK 500 O HOH A 823 O HOH A 838 1.89
REMARK 500 O HOH A 822 O HOH B 822 1.90
REMARK 500 O HOH A 806 O HOH B 833 1.92
REMARK 500 OE2 GLU B 579 NH2 ARG B 614 2.06
REMARK 500 O HOH A 837 O HOH A 839 2.16
REMARK 500 N HIS B 529 O HOH B 801 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 836 O HOH B 817 1545 2.00
REMARK 500
REMARK 500 REMARK: NULL
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 PRO A 475 -164.18 -79.32
REMARK 500 ASN A 499 -92.08 -111.71
REMARK 500 GLU A 500 -22.00 -156.00
REMARK 500 SER A 586 -100.04 -87.83
REMARK 500 LEU A 602 76.14 -100.40
REMARK 500 LEU A 605 -154.94 -114.27
REMARK 500 THR A 619 -114.16 -121.66
REMARK 500 SER A 648 -163.96 -121.65
REMARK 500 ASN A 649 45.73 39.40
REMARK 500 THR A 651 -161.93 -124.35
REMARK 500 ASN B 459 19.68 -143.80
REMARK 500 ASN B 499 -126.16 -106.63
REMARK 500 SER B 555 -161.21 -161.11
REMARK 500 GLU B 571 30.22 -94.29
REMARK 500 THR B 619 -104.51 -109.66
REMARK 500 THR B 651 -161.91 -124.31
REMARK 500 PRO B 733 172.43 -53.78
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5UTK A 442 741 UNP Q02763 TIE2_HUMAN 399 698
DBREF 5UTK B 442 741 UNP Q02763 TIE2_HUMAN 399 698
SEQADV 5UTK GLY A 438 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK SER A 439 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK GLY A 440 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK SER A 441 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK MSE A 612 UNP Q02763 VAL 569 ENGINEERED MUTATION
SEQADV 5UTK MSE A 656 UNP Q02763 VAL 613 ENGINEERED MUTATION
SEQADV 5UTK GLY B 438 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK SER B 439 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK GLY B 440 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK SER B 441 UNP Q02763 EXPRESSION TAG
SEQADV 5UTK MSE B 612 UNP Q02763 VAL 569 ENGINEERED MUTATION
SEQADV 5UTK MSE B 656 UNP Q02763 VAL 613 ENGINEERED MUTATION
SEQRES 1 A 304 GLY SER GLY SER LYS VAL LEU PRO LYS PRO LEU ASN ALA
SEQRES 2 A 304 PRO ASN VAL ILE ASP THR GLY HIS ASN PHE ALA VAL ILE
SEQRES 3 A 304 ASN ILE SER SER GLU PRO TYR PHE GLY ASP GLY PRO ILE
SEQRES 4 A 304 LYS SER LYS LYS LEU LEU TYR LYS PRO VAL ASN HIS TYR
SEQRES 5 A 304 GLU ALA TRP GLN HIS ILE GLN VAL THR ASN GLU ILE VAL
SEQRES 6 A 304 THR LEU ASN TYR LEU GLU PRO ARG THR GLU TYR GLU LEU
SEQRES 7 A 304 CYS VAL GLN LEU VAL ARG ARG GLY GLU GLY GLY GLU GLY
SEQRES 8 A 304 HIS PRO GLY PRO VAL ARG ARG PHE THR THR ALA SER ILE
SEQRES 9 A 304 GLY LEU PRO PRO PRO ARG GLY LEU ASN LEU LEU PRO LYS
SEQRES 10 A 304 SER GLN THR THR LEU ASN LEU THR TRP GLN PRO ILE PHE
SEQRES 11 A 304 PRO SER SER GLU ASP ASP PHE TYR VAL GLU VAL GLU ARG
SEQRES 12 A 304 ARG SER VAL GLN LYS SER ASP GLN GLN ASN ILE LYS VAL
SEQRES 13 A 304 PRO GLY ASN LEU THR SER VAL LEU LEU ASN ASN LEU HIS
SEQRES 14 A 304 PRO ARG GLU GLN TYR MSE VAL ARG ALA ARG VAL ASN THR
SEQRES 15 A 304 LYS ALA GLN GLY GLU TRP SER GLU ASP LEU THR ALA TRP
SEQRES 16 A 304 THR LEU SER ASP ILE LEU PRO PRO GLN PRO GLU ASN ILE
SEQRES 17 A 304 LYS ILE SER ASN ILE THR HIS SER SER ALA MSE ILE SER
SEQRES 18 A 304 TRP THR ILE LEU ASP GLY TYR SER ILE SER SER ILE THR
SEQRES 19 A 304 ILE ARG TYR LYS VAL GLN GLY LYS ASN GLU ASP GLN HIS
SEQRES 20 A 304 VAL ASP VAL LYS ILE LYS ASN ALA THR ILE THR GLN TYR
SEQRES 21 A 304 GLN LEU LYS GLY LEU GLU PRO GLU THR ALA TYR GLN VAL
SEQRES 22 A 304 ASP ILE PHE ALA GLU ASN ASN ILE GLY SER SER ASN PRO
SEQRES 23 A 304 ALA PHE SER HIS GLU LEU VAL THR LEU PRO GLU SER GLN
SEQRES 24 A 304 ALA PRO ALA ASP LEU
SEQRES 1 B 304 GLY SER GLY SER LYS VAL LEU PRO LYS PRO LEU ASN ALA
SEQRES 2 B 304 PRO ASN VAL ILE ASP THR GLY HIS ASN PHE ALA VAL ILE
SEQRES 3 B 304 ASN ILE SER SER GLU PRO TYR PHE GLY ASP GLY PRO ILE
SEQRES 4 B 304 LYS SER LYS LYS LEU LEU TYR LYS PRO VAL ASN HIS TYR
SEQRES 5 B 304 GLU ALA TRP GLN HIS ILE GLN VAL THR ASN GLU ILE VAL
SEQRES 6 B 304 THR LEU ASN TYR LEU GLU PRO ARG THR GLU TYR GLU LEU
SEQRES 7 B 304 CYS VAL GLN LEU VAL ARG ARG GLY GLU GLY GLY GLU GLY
SEQRES 8 B 304 HIS PRO GLY PRO VAL ARG ARG PHE THR THR ALA SER ILE
SEQRES 9 B 304 GLY LEU PRO PRO PRO ARG GLY LEU ASN LEU LEU PRO LYS
SEQRES 10 B 304 SER GLN THR THR LEU ASN LEU THR TRP GLN PRO ILE PHE
SEQRES 11 B 304 PRO SER SER GLU ASP ASP PHE TYR VAL GLU VAL GLU ARG
SEQRES 12 B 304 ARG SER VAL GLN LYS SER ASP GLN GLN ASN ILE LYS VAL
SEQRES 13 B 304 PRO GLY ASN LEU THR SER VAL LEU LEU ASN ASN LEU HIS
SEQRES 14 B 304 PRO ARG GLU GLN TYR MSE VAL ARG ALA ARG VAL ASN THR
SEQRES 15 B 304 LYS ALA GLN GLY GLU TRP SER GLU ASP LEU THR ALA TRP
SEQRES 16 B 304 THR LEU SER ASP ILE LEU PRO PRO GLN PRO GLU ASN ILE
SEQRES 17 B 304 LYS ILE SER ASN ILE THR HIS SER SER ALA MSE ILE SER
SEQRES 18 B 304 TRP THR ILE LEU ASP GLY TYR SER ILE SER SER ILE THR
SEQRES 19 B 304 ILE ARG TYR LYS VAL GLN GLY LYS ASN GLU ASP GLN HIS
SEQRES 20 B 304 VAL ASP VAL LYS ILE LYS ASN ALA THR ILE THR GLN TYR
SEQRES 21 B 304 GLN LEU LYS GLY LEU GLU PRO GLU THR ALA TYR GLN VAL
SEQRES 22 B 304 ASP ILE PHE ALA GLU ASN ASN ILE GLY SER SER ASN PRO
SEQRES 23 B 304 ALA PHE SER HIS GLU LEU VAL THR LEU PRO GLU SER GLN
SEQRES 24 B 304 ALA PRO ALA ASP LEU
HET MSE A 612 8
HET MSE A 656 8
HET MSE B 612 8
HET MSE B 656 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 HOH *77(H2 O)
SHEET 1 AA1 2 LYS A 446 PRO A 447 0
SHEET 2 AA1 2 TYR A 470 PHE A 471 -1 O PHE A 471 N LYS A 446
SHEET 1 AA2 3 ASN A 452 THR A 456 0
SHEET 2 AA2 3 ALA A 461 ASN A 464 -1 O ASN A 464 N ASN A 452
SHEET 3 AA2 3 ILE A 501 LEU A 504 -1 O VAL A 502 N ILE A 463
SHEET 1 AA3 4 GLN A 493 VAL A 497 0
SHEET 2 AA3 4 ILE A 476 PRO A 485 -1 N LEU A 481 O ILE A 495
SHEET 3 AA3 4 GLU A 512 ARG A 521 -1 O CYS A 516 N LEU A 482
SHEET 4 AA3 4 ARG A 534 THR A 537 -1 O PHE A 536 N TYR A 513
SHEET 1 AA4 3 ASN A 550 PRO A 553 0
SHEET 2 AA4 3 LEU A 559 THR A 562 -1 O THR A 562 N ASN A 550
SHEET 3 AA4 3 SER A 599 LEU A 602 -1 O LEU A 602 N LEU A 559
SHEET 1 AA5 4 GLN A 589 PRO A 594 0
SHEET 2 AA5 4 TYR A 575 ARG A 581 -1 N VAL A 576 O VAL A 593
SHEET 3 AA5 4 GLN A 610 ASN A 618 -1 O MSE A 612 N ARG A 581
SHEET 4 AA5 4 LEU A 629 TRP A 632 -1 O LEU A 629 N VAL A 613
SHEET 1 AA6 3 GLU A 643 SER A 648 0
SHEET 2 AA6 3 ALA A 655 THR A 660 -1 O THR A 660 N GLU A 643
SHEET 3 AA6 3 GLN A 696 LEU A 699 -1 O TYR A 697 N ILE A 657
SHEET 1 AA7 4 VAL A 685 ILE A 689 0
SHEET 2 AA7 4 SER A 669 VAL A 676 -1 N ILE A 670 O ILE A 689
SHEET 3 AA7 4 ALA A 707 GLU A 715 -1 O ASP A 711 N ARG A 673
SHEET 4 AA7 4 ALA A 724 VAL A 730 -1 O LEU A 729 N TYR A 708
SHEET 1 AA8 2 LYS B 446 PRO B 447 0
SHEET 2 AA8 2 TYR B 470 PHE B 471 -1 O PHE B 471 N LYS B 446
SHEET 1 AA9 3 ASN B 452 THR B 456 0
SHEET 2 AA9 3 ALA B 461 ASN B 464 -1 O ASN B 464 N ASN B 452
SHEET 3 AA9 3 ILE B 501 LEU B 504 -1 O LEU B 504 N ALA B 461
SHEET 1 AB1 4 GLN B 493 GLN B 496 0
SHEET 2 AB1 4 SER B 478 PRO B 485 -1 N TYR B 483 O GLN B 493
SHEET 3 AB1 4 GLU B 512 VAL B 520 -1 O CYS B 516 N LEU B 482
SHEET 4 AB1 4 ARG B 534 THR B 537 -1 O PHE B 536 N TYR B 513
SHEET 1 AB2 3 ASN B 550 PRO B 553 0
SHEET 2 AB2 3 LEU B 559 THR B 562 -1 O ASN B 560 N LEU B 552
SHEET 3 AB2 3 SER B 599 LEU B 602 -1 O LEU B 602 N LEU B 559
SHEET 1 AB3 4 ILE B 591 PRO B 594 0
SHEET 2 AB3 4 TYR B 575 ARG B 580 -1 N VAL B 576 O VAL B 593
SHEET 3 AB3 4 GLN B 610 ASN B 618 -1 O ARG B 614 N GLU B 579
SHEET 4 AB3 4 LEU B 629 TRP B 632 -1 O LEU B 629 N VAL B 613
SHEET 1 AB4 3 GLU B 643 SER B 648 0
SHEET 2 AB4 3 ALA B 655 THR B 660 -1 O THR B 660 N GLU B 643
SHEET 3 AB4 3 GLN B 696 LEU B 699 -1 O LEU B 699 N ALA B 655
SHEET 1 AB5 4 VAL B 685 ILE B 689 0
SHEET 2 AB5 4 SER B 669 VAL B 676 -1 N ILE B 670 O ILE B 689
SHEET 3 AB5 4 ALA B 707 GLU B 715 -1 O GLN B 709 N LYS B 675
SHEET 4 AB5 4 ALA B 724 PHE B 725 -1 O ALA B 724 N ILE B 712
SHEET 1 AB6 4 VAL B 685 ILE B 689 0
SHEET 2 AB6 4 SER B 669 VAL B 676 -1 N ILE B 670 O ILE B 689
SHEET 3 AB6 4 ALA B 707 GLU B 715 -1 O GLN B 709 N LYS B 675
SHEET 4 AB6 4 LEU B 729 VAL B 730 -1 O LEU B 729 N TYR B 708
LINK C TYR A 611 N MSE A 612 1555 1555 1.33
LINK C MSE A 612 N VAL A 613 1555 1555 1.33
LINK C ALA A 655 N MSE A 656 1555 1555 1.34
LINK C MSE A 656 N ILE A 657 1555 1555 1.33
LINK C TYR B 611 N MSE B 612 1555 1555 1.33
LINK C MSE B 612 N VAL B 613 1555 1555 1.33
LINK C ALA B 655 N MSE B 656 1555 1555 1.33
LINK C MSE B 656 N ILE B 657 1555 1555 1.33
CISPEP 1 GLU A 468 PRO A 469 0 3.74
CISPEP 2 GLY A 474 PRO A 475 0 -1.76
CISPEP 3 GLU B 468 PRO B 469 0 3.75
CISPEP 4 GLY B 474 PRO B 475 0 -1.21
CRYST1 174.950 52.026 111.427 90.00 117.49 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005716 0.000000 0.002975 0.00000
SCALE2 0.000000 0.019221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010117 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
