HEADER HORMONE/GROWTH FACTOR 30-MAY-06 2H64
TITLE CRYSTAL STRUCTURE OF A TERNARY LIGAND-RECEPTOR COMPLEX OF
TITLE 2 BMP-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BONE MORPHOGENETIC PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BMP-2, BMP-2A;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE IA;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 11 SYNONYM: SERINE/THREONINE-PROTEIN KINASE RECEPTOR R5, SKR5,
COMPND 12 ACTIVIN RECEPTOR-LIKE KINASE 3, ALK-3, CD292 ANTIGEN;
COMPND 13 EC: 2.7.11.30;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: ACVR2B PROTEIN;
COMPND 17 CHAIN: C;
COMPND 18 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 19 SYNONYM: ACTIVIN RECEPTOR TYPE IIB;
COMPND 20 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: BMP2, BMP2A;
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: BMPR1A, ACVRLK3, ALK3;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 17 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 18 ORGANISM_TAXID: 10090;
SOURCE 19 GENE: ACVR2B;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TGF-BETA SUPERFAMILY, LIGAND-RECEPTOR COMPLEX,
KEYWDS 2 HORMONE/GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.MUELLER,W.SEBALD,D.WEBER
REVDAT 2 24-FEB-09 2H64 1 VERSN
REVDAT 1 10-APR-07 2H64 0
JRNL AUTH D.WEBER,A.KOTZSCH,J.NICKEL,S.HARTH,A.SEHER,
JRNL AUTH 2 U.MUELLER,W.SEBALD,T.D.MUELLER
JRNL TITL A SILENT H-BOND CAN BE MUTATIONALLY ACTIVATED FOR
JRNL TITL 2 HIGH-AFFINITY INTERACTION OF BMP-2 AND ACTIVIN
JRNL TITL 3 TYPE IIB RECEPTOR.
JRNL REF BMC STRUCT.BIOL. V. 7 6 2007
JRNL REFN ESSN 1472-6807
JRNL PMID 17295905
JRNL DOI 10.1186/1472-6807-7-6
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 500.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 34058
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 SET) : 0.228
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1701
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2295
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.45
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.25
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.31
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H64 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB037976.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.75
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC VARIMAX HR
REMARK 200 OPTICS : OSMIC VARIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42606
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.51400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.1M TRIS-HCL PH 8.75,
REMARK 280 0.2M NH4CH3COO, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 74.08000
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 37.04000
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 37.04000
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 74.08000
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS HALF OF THE HEXAMERIC
REMARK 300 ASSEMBLY. THE BIOLOGICAL UNIT CAN BE OBTAINED BY APPLYING THE
REMARK 300 SYMMETRY OPERATION: Y, X, -Z+1
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 111.12000
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 GLN A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 HIS A 4
REMARK 465 LYS A 5
REMARK 465 GLN A 6
REMARK 465 ARG A 7
REMARK 465 LYS A 8
REMARK 465 ARG A 9
REMARK 465 GLN B 1
REMARK 465 ASN B 2
REMARK 465 LEU B 3
REMARK 465 ASP B 4
REMARK 465 SER B 5
REMARK 465 MET B 6
REMARK 465 LEU B 7
REMARK 465 HIS B 8
REMARK 465 GLY B 9
REMARK 465 THR B 10
REMARK 465 GLY B 11
REMARK 465 MET B 12
REMARK 465 LYS B 13
REMARK 465 SER B 14
REMARK 465 ASP B 15
REMARK 465 SER B 16
REMARK 465 ASP B 17
REMARK 465 GLN B 18
REMARK 465 LYS B 19
REMARK 465 LYS B 20
REMARK 465 SER B 21
REMARK 465 GLU B 22
REMARK 465 ASN B 23
REMARK 465 GLY B 24
REMARK 465 VAL B 25
REMARK 465 THR B 26
REMARK 465 LEU B 27
REMARK 465 ALA B 28
REMARK 465 PRO B 29
REMARK 465 GLU B 30
REMARK 465 ASP B 31
REMARK 465 PHE B 124
REMARK 465 ASP B 125
REMARK 465 GLY B 126
REMARK 465 SER B 127
REMARK 465 ILE B 128
REMARK 465 ARG B 129
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 GLU C 5
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 THR B 32 OG1 CG2
REMARK 470 LEU B 33 CG CD1 CD2
REMARK 470 PHE B 123 CG CD1 CD2 CE1 CE2 CZ
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 LEU A 19 111.65 -167.30
REMARK 500 PHE A 41 175.89 65.40
REMARK 500 CYS A 47 74.41 -115.02
REMARK 500 ASN A 56 59.01 32.14
REMARK 500 ASP B 89 -171.90 60.97
REMARK 500 LEU B 106 24.08 49.71
REMARK 500 ASN C 17 52.80 -104.23
REMARK 500 GLU C 19 -76.42 -64.21
REMARK 500 SER C 49 81.45 46.91
REMARK 500 ASP C 62 118.34 -25.27
REMARK 500 GLU C 77 -76.00 -44.37
REMARK 500 PHE C 90 15.64 58.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 111 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH B 181 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH A 221 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH A 224 DISTANCE = 6.47 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1REU RELATED DB: PDB
REMARK 900 BINARY COMPLEX OF BMP-2 BOUND TO EXTRACELLULAR DOMAIN OF
REMARK 900 THE TYPE I RECEPTOR BMPR-IA
REMARK 900 RELATED ID: 2H62 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A TERNARY LIGAND-RECEPTOR COMPLEX OF
REMARK 900 BMP-2
DBREF 2H64 A 1 114 UNP P12643 BMP2_HUMAN 283 396
DBREF 2H64 B 1 129 UNP P36894 BMR1A_HUMAN 24 152
DBREF 2H64 C 1 99 UNP Q3KQI1 Q3KQI1_MOUSE 19 117
SEQADV 2H64 LYS A 100 UNP P12643 LEU 382 ENGINEERED
SEQADV 2H64 ASP A 102 UNP P12643 ASN 384 ENGINEERED
SEQRES 1 A 114 GLN ALA LYS HIS LYS GLN ARG LYS ARG LEU LYS SER SER
SEQRES 2 A 114 CYS LYS ARG HIS PRO LEU TYR VAL ASP PHE SER ASP VAL
SEQRES 3 A 114 GLY TRP ASN ASP TRP ILE VAL ALA PRO PRO GLY TYR HIS
SEQRES 4 A 114 ALA PHE TYR CYS HIS GLY GLU CYS PRO PHE PRO LEU ALA
SEQRES 5 A 114 ASP HIS LEU ASN SER THR ASN HIS ALA ILE VAL GLN THR
SEQRES 6 A 114 LEU VAL ASN SER VAL ASN SER LYS ILE PRO LYS ALA CYS
SEQRES 7 A 114 CYS VAL PRO THR GLU LEU SER ALA ILE SER MET LEU TYR
SEQRES 8 A 114 LEU ASP GLU ASN GLU LYS VAL VAL LYS LYS ASP TYR GLN
SEQRES 9 A 114 ASP MET VAL VAL GLU GLY CYS GLY CYS ARG
SEQRES 1 B 129 GLN ASN LEU ASP SER MET LEU HIS GLY THR GLY MET LYS
SEQRES 2 B 129 SER ASP SER ASP GLN LYS LYS SER GLU ASN GLY VAL THR
SEQRES 3 B 129 LEU ALA PRO GLU ASP THR LEU PRO PHE LEU LYS CYS TYR
SEQRES 4 B 129 CYS SER GLY HIS CYS PRO ASP ASP ALA ILE ASN ASN THR
SEQRES 5 B 129 CYS ILE THR ASN GLY HIS CYS PHE ALA ILE ILE GLU GLU
SEQRES 6 B 129 ASP ASP GLN GLY GLU THR THR LEU ALA SER GLY CYS MET
SEQRES 7 B 129 LYS TYR GLU GLY SER ASP PHE GLN CYS LYS ASP SER PRO
SEQRES 8 B 129 LYS ALA GLN LEU ARG ARG THR ILE GLU CYS CYS ARG THR
SEQRES 9 B 129 ASN LEU CYS ASN GLN TYR LEU GLN PRO THR LEU PRO PRO
SEQRES 10 B 129 VAL VAL ILE GLY PRO PHE PHE ASP GLY SER ILE ARG
SEQRES 1 C 99 SER GLY ARG GLY GLU ALA GLU THR ARG GLU CYS ILE TYR
SEQRES 2 C 99 TYR ASN ALA ASN TRP GLU LEU GLU ARG THR ASN GLN SER
SEQRES 3 C 99 GLY LEU GLU ARG CYS GLU GLY GLU GLN ASP LYS ARG LEU
SEQRES 4 C 99 HIS CYS TYR ALA SER TRP ARG ASN SER SER GLY THR ILE
SEQRES 5 C 99 GLU LEU VAL LYS LYS GLY CYS TRP LEU ASP ASP PHE ASN
SEQRES 6 C 99 CYS TYR ASP ARG GLN GLU CYS VAL ALA THR GLU GLU ASN
SEQRES 7 C 99 PRO GLN VAL TYR PHE CYS CYS CYS GLU GLY ASN PHE CYS
SEQRES 8 C 99 ASN GLU ARG PHE THR HIS LEU PRO
FORMUL 4 HOH *209(H2 O)
HELIX 1 1 PHE A 23 GLY A 27 1 5
HELIX 2 2 ALA A 52 ASN A 56 5 5
HELIX 3 3 THR A 58 ASN A 71 1 14
HELIX 4 4 GLY B 82 ASP B 89 1 8
HELIX 5 5 ASP C 63 TYR C 67 5 5
SHEET 1 A 2 LYS A 15 HIS A 17 0
SHEET 2 A 2 TYR A 42 HIS A 44 -1 O TYR A 42 N HIS A 17
SHEET 1 B 2 TYR A 20 ASP A 22 0
SHEET 2 B 2 GLY A 37 HIS A 39 -1 O TYR A 38 N VAL A 21
SHEET 1 C 3 ILE A 32 ALA A 34 0
SHEET 2 C 3 CYS A 78 LEU A 92 -1 O LEU A 90 N VAL A 33
SHEET 3 C 3 VAL A 98 ARG A 114 -1 O VAL A 99 N TYR A 91
SHEET 1 D 2 LEU B 36 TYR B 39 0
SHEET 2 D 2 THR B 52 THR B 55 -1 O CYS B 53 N CYS B 38
SHEET 1 E 3 THR B 71 MET B 78 0
SHEET 2 E 3 HIS B 58 GLU B 65 -1 N ILE B 62 O ALA B 74
SHEET 3 E 3 ARG B 97 CYS B 102 -1 O CYS B 102 N CYS B 59
SHEET 1 F 5 SER C 26 ARG C 30 0
SHEET 2 F 5 GLU C 10 ASN C 15 -1 N TYR C 13 O GLY C 27
SHEET 3 F 5 THR C 51 LEU C 61 -1 O LYS C 57 N TYR C 14
SHEET 4 F 5 LEU C 39 SER C 48 -1 N ARG C 46 O GLU C 53
SHEET 5 F 5 TYR C 82 CYS C 86 -1 O TYR C 82 N TRP C 45
SHEET 1 G 2 CYS C 72 ALA C 74 0
SHEET 2 G 2 PHE C 95 HIS C 97 1 O THR C 96 N ALA C 74
SSBOND 1 CYS A 14 CYS A 79 1555 1555 2.03
SSBOND 2 CYS A 43 CYS A 111 1555 1555 2.03
SSBOND 3 CYS A 47 CYS A 113 1555 1555 2.03
SSBOND 4 CYS B 38 CYS B 59 1555 1555 2.03
SSBOND 5 CYS B 40 CYS B 44 1555 1555 2.03
SSBOND 6 CYS B 53 CYS B 77 1555 1555 2.02
SSBOND 7 CYS B 87 CYS B 101 1555 1555 2.03
SSBOND 8 CYS B 102 CYS B 107 1555 1555 2.03
SSBOND 9 CYS C 11 CYS C 41 1555 1555 2.03
SSBOND 10 CYS C 31 CYS C 59 1555 1555 2.03
SSBOND 11 CYS C 66 CYS C 85 1555 1555 2.03
SSBOND 12 CYS C 72 CYS C 84 1555 1555 2.02
SSBOND 13 CYS C 86 CYS C 91 1555 1555 2.03
CISPEP 1 ALA A 34 PRO A 35 0 -0.04
CISPEP 2 PHE A 49 PRO A 50 0 -0.63
CISPEP 3 GLY B 121 PRO B 122 0 0.01
CRYST1 82.790 82.790 111.120 90.00 90.00 120.00 P 32 2 1 6
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 0.012079 0.006974 0.000000 0.00000
SCALE2 0.000000 0.013947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008999 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
