HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-OCT-15 5E92
TITLE TGF-BETA RECEPTOR TYPE 2 KINASE DOMAIN (E431A,R433A,E485A,K488A,R493A,
TITLE 2 R495A) IN COMPLEX WITH AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TGF-BETA RECEPTOR TYPE-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 237-549;
COMPND 5 SYNONYM: TGFR-2,TGF-BETA TYPE II RECEPTOR,TRANSFORMING GROWTH FACTOR-
COMPND 6 BETA RECEPTOR TYPE II,TBETAR-II;
COMPND 7 EC: 2.7.11.30;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TGFBR2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: FALL ARMYWORM;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1
KEYWDS KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.SHERIFF
REVDAT 3 27-SEP-23 5E92 1 LINK
REVDAT 2 18-APR-18 5E92 1 JRNL REMARK
REVDAT 1 11-MAY-16 5E92 0
JRNL AUTH A.J.TEBBEN,M.RUZANOV,M.GAO,D.XIE,S.E.KIEFER,C.YAN,
JRNL AUTH 2 J.A.NEWITT,L.ZHANG,K.KIM,H.LU,L.M.KOPCHO,S.SHERIFF
JRNL TITL CRYSTAL STRUCTURES OF APO AND INHIBITOR-BOUND TGF BETA R2
JRNL TITL 2 KINASE DOMAIN: INSIGHTS INTO TGF BETA R ISOFORM SELECTIVITY.
JRNL REF ACTA CRYSTALLOGR D STRUCT V. 72 658 2016
JRNL REF 2 BIOL
JRNL REFN ISSN 2059-7983
JRNL PMID 27139629
JRNL DOI 10.1107/S2059798316003624
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.6
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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 22741
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1095
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.18
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.19
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2929
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2325
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2776
REMARK 3 BIN R VALUE (WORKING SET) : 0.2307
REMARK 3 BIN FREE R VALUE : 0.2675
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.22
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 153
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 : 2261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.31630
REMARK 3 B22 (A**2) : 3.73910
REMARK 3 B33 (A**2) : 12.57710
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) : 0.284
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.182
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.156
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.179
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.155
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 : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2372 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3247 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 790 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 51 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 362 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2372 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 317 ; 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 : 2698 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.56
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E92 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22789
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 41.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.38300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 3TZM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 8.5, 150 MM MGCL2,
REMARK 280 24%(W/V) PEG4000, 20%(V/V) GLCYEROL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 31.38000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.93500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.74000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.93500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.38000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.74000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 234
REMARK 465 HIS A 235
REMARK 465 MET A 236
REMARK 465 HIS A 237
REMARK 465 ASN A 238
REMARK 465 THR A 239
REMARK 465 GLN A 265
REMARK 465 ASN A 266
REMARK 465 THR A 267
REMARK 465 SER A 268
REMARK 465 GLU A 269
REMARK 465 GLN A 270
REMARK 465 LEU A 544
REMARK 465 ASP A 545
REMARK 465 ARG A 546
REMARK 465 LEU A 547
REMARK 465 SER A 548
REMARK 465 GLY A 549
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 GLU A 240 CG CD OE1 OE2
REMARK 470 GLU A 245 CG CD OE1 OE2
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 PHE A 271 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 316 CG CD OE1 OE2
REMARK 470 LEU A 317 CG CD1 CD2
REMARK 470 ARG A 339 CD NE CZ NH1 NH2
REMARK 470 GLU A 345 CD OE1 OE2
REMARK 470 ARG A 348 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2
REMARK 470 SER A 409 OG
REMARK 470 VAL A 410 CG1 CG2
REMARK 470 ASP A 411 CG OD1 OD2
REMARK 470 ASP A 412 CG OD1 OD2
REMARK 470 ASN A 415 CG OD1 ND2
REMARK 470 SER A 416 OG
REMARK 470 LEU A 436 CG CD1 CD2
REMARK 470 GLU A 437 CG CD OE1 OE2
REMARK 470 VAL A 439 CG1 CG2
REMARK 470 GLU A 440 CG CD OE1 OE2
REMARK 470 LYS A 468 CG CD CE NZ
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 SER A 476 OG
REMARK 470 LYS A 477 CD CE NZ
REMARK 470 GLU A 480 CD OE1 OE2
REMARK 470 GLN A 508 CG CD OE1 NE2
REMARK 470 MET A 512 SD CE
REMARK 470 GLU A 542 CG CD OE1 OE2
REMARK 470 HIS A 543 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER A 416 C - N - CA ANGL. DEV. = 15.7 DEGREES
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 ASP A 247 -62.46 -105.26
REMARK 500 LYS A 300 117.67 -35.12
REMARK 500 LEU A 308 -67.98 -99.33
REMARK 500 ARG A 378 -4.53 71.14
REMARK 500 ASP A 379 47.45 -143.92
REMARK 500 ASP A 397 87.04 63.07
REMARK 500 ASN A 415 98.65 -162.31
REMARK 500 SER A 416 -83.86 38.37
REMARK 500 LEU A 436 37.45 -73.69
REMARK 500 GLU A 437 -68.59 -123.85
REMARK 500 LEU A 492 -74.76 -97.90
REMARK 500 LEU A 541 49.92 -73.53
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 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 384 OD1
REMARK 620 2 ASP A 397 OD2 95.1
REMARK 620 3 ANP A 601 O2G 106.1 89.9
REMARK 620 4 ANP A 601 O2A 100.4 88.6 153.4
REMARK 620 5 HOH A 739 O 87.6 175.0 93.3 86.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 397 OD1
REMARK 620 2 ASP A 397 OD2 63.2
REMARK 620 3 ANP A 601 O1G 157.2 94.4
REMARK 620 4 ANP A 601 O2B 87.9 87.8 95.9
REMARK 620 5 HOH A 721 O 81.5 144.3 120.2 96.4
REMARK 620 6 HOH A 740 O 86.6 93.1 90.6 173.3 79.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E8S RELATED DB: PDB
REMARK 900 RELATED ID: 5E8T RELATED DB: PDB
REMARK 900 RELATED ID: 5E8U RELATED DB: PDB
REMARK 900 RELATED ID: 5E8V RELATED DB: PDB
REMARK 900 RELATED ID: 5E8W RELATED DB: PDB
REMARK 900 RELATED ID: 5E8X RELATED DB: PDB
REMARK 900 RELATED ID: 5E8Y RELATED DB: PDB
REMARK 900 RELATED ID: 5E8Z RELATED DB: PDB
REMARK 900 RELATED ID: 5E90 RELATED DB: PDB
REMARK 900 RELATED ID: 5E91 RELATED DB: PDB
DBREF 5E92 A 237 549 UNP P37173 TGFR2_HUMAN 237 549
SEQADV 5E92 GLY A 234 UNP P37173 EXPRESSION TAG
SEQADV 5E92 HIS A 235 UNP P37173 EXPRESSION TAG
SEQADV 5E92 MET A 236 UNP P37173 EXPRESSION TAG
SEQADV 5E92 ALA A 431 UNP P37173 GLU 431 ENGINEERED MUTATION
SEQADV 5E92 ALA A 433 UNP P37173 ARG 433 ENGINEERED MUTATION
SEQADV 5E92 ALA A 485 UNP P37173 GLU 485 ENGINEERED MUTATION
SEQADV 5E92 ALA A 488 UNP P37173 LYS 488 ENGINEERED MUTATION
SEQADV 5E92 ALA A 493 UNP P37173 ARG 493 ENGINEERED MUTATION
SEQADV 5E92 ALA A 495 UNP P37173 ARG 495 ENGINEERED MUTATION
SEQRES 1 A 316 GLY HIS MET HIS ASN THR GLU LEU LEU PRO ILE GLU LEU
SEQRES 2 A 316 ASP THR LEU VAL GLY LYS GLY ARG PHE ALA GLU VAL TYR
SEQRES 3 A 316 LYS ALA LYS LEU LYS GLN ASN THR SER GLU GLN PHE GLU
SEQRES 4 A 316 THR VAL ALA VAL LYS ILE PHE PRO TYR GLU GLU TYR ALA
SEQRES 5 A 316 SER TRP LYS THR GLU LYS ASP ILE PHE SER ASP ILE ASN
SEQRES 6 A 316 LEU LYS HIS GLU ASN ILE LEU GLN PHE LEU THR ALA GLU
SEQRES 7 A 316 GLU ARG LYS THR GLU LEU GLY LYS GLN TYR TRP LEU ILE
SEQRES 8 A 316 THR ALA PHE HIS ALA LYS GLY ASN LEU GLN GLU TYR LEU
SEQRES 9 A 316 THR ARG HIS VAL ILE SER TRP GLU ASP LEU ARG LYS LEU
SEQRES 10 A 316 GLY SER SER LEU ALA ARG GLY ILE ALA HIS LEU HIS SER
SEQRES 11 A 316 ASP HIS THR PRO CYS GLY ARG PRO LYS MET PRO ILE VAL
SEQRES 12 A 316 HIS ARG ASP LEU LYS SER SER ASN ILE LEU VAL LYS ASN
SEQRES 13 A 316 ASP LEU THR CYS CYS LEU CYS ASP PHE GLY LEU SER LEU
SEQRES 14 A 316 ARG LEU ASP PRO THR LEU SER VAL ASP ASP LEU ALA ASN
SEQRES 15 A 316 SER GLY GLN VAL GLY THR ALA ARG TYR MET ALA PRO GLU
SEQRES 16 A 316 VAL LEU ALA SER ALA MET ASN LEU GLU ASN VAL GLU SER
SEQRES 17 A 316 PHE LYS GLN THR ASP VAL TYR SER MET ALA LEU VAL LEU
SEQRES 18 A 316 TRP GLU MET THR SER ARG CYS ASN ALA VAL GLY GLU VAL
SEQRES 19 A 316 LYS ASP TYR GLU PRO PRO PHE GLY SER LYS VAL ARG GLU
SEQRES 20 A 316 HIS PRO CYS VAL ALA SER MET ALA ASP ASN VAL LEU ALA
SEQRES 21 A 316 ASP ALA GLY ARG PRO GLU ILE PRO SER PHE TRP LEU ASN
SEQRES 22 A 316 HIS GLN GLY ILE GLN MET VAL CYS GLU THR LEU THR GLU
SEQRES 23 A 316 CYS TRP ASP HIS ASP PRO GLU ALA ARG LEU THR ALA GLN
SEQRES 24 A 316 CYS VAL ALA GLU ARG PHE SER GLU LEU GLU HIS LEU ASP
SEQRES 25 A 316 ARG LEU SER GLY
HET ANP A 601 48
HET MG A 602 1
HET MG A 603 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 2 ANP C10 H17 N6 O12 P3
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *84(H2 O)
HELIX 1 AA1 GLU A 283 ASP A 296 1 14
HELIX 2 AA2 ASN A 332 HIS A 340 1 9
HELIX 3 AA3 SER A 343 SER A 363 1 21
HELIX 4 AA4 LYS A 381 SER A 383 5 3
HELIX 5 AA5 SER A 409 ASN A 415 1 7
HELIX 6 AA6 THR A 421 MET A 425 5 5
HELIX 7 AA7 ALA A 426 ALA A 431 1 6
HELIX 8 AA8 ASN A 438 SER A 459 1 22
HELIX 9 AA9 ARG A 460 GLY A 465 5 6
HELIX 10 AB1 CYS A 483 LEU A 492 1 10
HELIX 11 AB2 PRO A 501 ASN A 506 5 6
HELIX 12 AB3 HIS A 507 TRP A 521 1 15
HELIX 13 AB4 ASP A 524 ARG A 528 5 5
HELIX 14 AB5 THR A 530 GLU A 540 1 11
SHEET 1 AA1 5 ILE A 244 LYS A 252 0
SHEET 2 AA1 5 GLU A 257 LEU A 263 -1 O VAL A 258 N GLY A 251
SHEET 3 AA1 5 THR A 273 PRO A 280 -1 O ILE A 278 N GLU A 257
SHEET 4 AA1 5 GLY A 318 ALA A 326 -1 O TYR A 321 N PHE A 279
SHEET 5 AA1 5 PHE A 307 THR A 315 -1 N THR A 309 O ILE A 324
SHEET 1 AA2 2 ILE A 375 VAL A 376 0
SHEET 2 AA2 2 LEU A 402 ARG A 403 -1 O LEU A 402 N VAL A 376
SHEET 1 AA3 2 ILE A 385 VAL A 387 0
SHEET 2 AA3 2 CYS A 393 LEU A 395 -1 O CYS A 394 N LEU A 386
LINK OD1 ASN A 384 MG MG A 602 1555 1555 1.94
LINK OD2 ASP A 397 MG MG A 602 1555 1555 2.00
LINK OD1 ASP A 397 MG MG A 603 1555 1555 2.10
LINK OD2 ASP A 397 MG MG A 603 1555 1555 2.11
LINK O2G ANP A 601 MG MG A 602 1555 1555 2.07
LINK O2A ANP A 601 MG MG A 602 1555 1555 2.05
LINK O1G ANP A 601 MG MG A 603 1555 1555 1.94
LINK O2B ANP A 601 MG MG A 603 1555 1555 2.17
LINK MG MG A 602 O HOH A 739 1555 1555 2.13
LINK MG MG A 603 O HOH A 721 1555 1555 2.10
LINK MG MG A 603 O HOH A 740 1555 1555 2.09
CISPEP 1 ASN A 415 SER A 416 0 -4.38
SITE 1 AC1 26 GLY A 251 GLY A 253 ARG A 254 PHE A 255
SITE 2 AC1 26 ALA A 256 VAL A 258 ALA A 275 LYS A 277
SITE 3 AC1 26 LEU A 305 THR A 325 ALA A 326 PHE A 327
SITE 4 AC1 26 HIS A 328 ASN A 332 ASP A 379 LYS A 381
SITE 5 AC1 26 SER A 383 ASN A 384 LEU A 386 ASP A 397
SITE 6 AC1 26 MG A 602 MG A 603 HOH A 723 HOH A 726
SITE 7 AC1 26 HOH A 739 HOH A 740
SITE 1 AC2 5 ASN A 384 ASP A 397 ANP A 601 MG A 603
SITE 2 AC2 5 HOH A 739
SITE 1 AC3 5 ASP A 397 ANP A 601 MG A 602 HOH A 721
SITE 2 AC3 5 HOH A 740
CRYST1 62.760 75.480 77.870 90.00 90.00 90.00 P 21 21 21 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 0.015934 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012842 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
