HEADER MEMBRANE PROTEIN/HORMONE/GROWTH FACTOR 13-FEB-03 1NYS
TITLE CRYSTAL STRUCTURE OF ACTIVIN A BOUND TO THE ECD OF ACTRIIB P41
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIVIN RECEPTOR;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: N-TERMINAL EXTRACELLULAR DOMAIN (RESIDUES 19-119);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INHIBIN BETA A CHAIN;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: MATURE DOMAIN (RESIDUES 311-426);
COMPND 10 SYNONYM: ACTIVIN BETA-A CHAIN, ERYTHROID DIFFERENTIATION PROTEIN,
COMPND 11 EDF;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ACTRIIB;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF+;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PVL1392;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: INHBA;
SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 18 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BA83.6-02
KEYWDS ACTIVIN, TYPE II, TGF BETA, ACTRIIB, EXTRACELLULAR DOMAIN, MEMBRANE
KEYWDS 2 PROTEIN-HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.B.THOMPSON,T.K.WOODRUFF,T.S.JARDETZKY
REVDAT 4 16-AUG-23 1NYS 1 SEQADV
REVDAT 3 11-OCT-17 1NYS 1 REMARK
REVDAT 2 24-FEB-09 1NYS 1 VERSN
REVDAT 1 08-APR-03 1NYS 0
JRNL AUTH T.B.THOMPSON,T.K.WOODRUFF,T.S.JARDETZKY
JRNL TITL STRUCTURES OF AN ACTRIIB:ACTIVIN A COMPLEX REVEAL A NOVEL
JRNL TITL 2 BINDING MODE FOR TGF-BETA LIGAND:RECEPTOR INTERACTIONS
JRNL REF EMBO J. V. 22 1555 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12660162
JRNL DOI 10.1093/EMBOJ/CDG156
REMARK 2
REMARK 2 RESOLUTION. 3.05 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.74
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) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 9254
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) : 0.252
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 484
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.014
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1346
REMARK 3 BIN R VALUE (WORKING SET) : 0.3570
REMARK 3 BIN FREE R VALUE : 0.4350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 61
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.056
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 77.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.51000
REMARK 3 B22 (A**2) : 2.51000
REMARK 3 B33 (A**2) : -5.03000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
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) : 0.52
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.72
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.960
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 30.68
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018361.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9789
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS, BRUTE, BEAST
REMARK 200 STARTING MODEL: PDB ENTRY 1BTE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CHLORIDE, HEPES, PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 23.09950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 11.54975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.64925
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SER A 19
REMARK 465 GLY A 20
REMARK 465 ARG A 21
REMARK 465 GLY A 22
REMARK 465 GLU A 23
REMARK 465 ALA A 24
REMARK 465 GLU A 52
REMARK 465 GLN A 53
REMARK 465 GLU A 118
REMARK 465 PRO A 119
REMARK 465 LEU A 120
REMARK 465 VAL A 121
REMARK 465 PRO A 122
REMARK 465 ARG A 123
REMARK 465 GLY B 1
REMARK 465 LYS B 7
REMARK 465 VAL B 8
REMARK 465 ALA B 49
REMARK 465 GLY B 50
REMARK 465 THR B 51
REMARK 465 SER B 52
REMARK 465 GLY B 53
REMARK 465 SER B 54
REMARK 465 SER B 55
REMARK 465 LEU B 56
REMARK 465 SER B 57
REMARK 465 PHE B 58
REMARK 465 HIS B 59
REMARK 465 SER B 60
REMARK 465 THR B 61
REMARK 465 VAL B 62
REMARK 465 ILE B 63
REMARK 465 ASN B 64
REMARK 465 HIS B 65
REMARK 465 TYR B 66
REMARK 465 ARG B 67
REMARK 465 MET B 68
REMARK 465 ARG B 69
REMARK 465 GLY B 70
REMARK 465 HIS B 71
REMARK 465 SER B 72
REMARK 465 PRO B 73
REMARK 465 PHE B 74
REMARK 465 ALA B 75
REMARK 465 ASN B 76
REMARK 465 SER C 19
REMARK 465 GLY C 20
REMARK 465 ARG C 21
REMARK 465 GLY C 22
REMARK 465 GLU C 23
REMARK 465 ALA C 24
REMARK 465 PRO C 117
REMARK 465 GLU C 118
REMARK 465 PRO C 119
REMARK 465 LEU C 120
REMARK 465 VAL C 121
REMARK 465 PRO C 122
REMARK 465 ARG C 123
REMARK 465 GLY D 1
REMARK 465 LEU D 2
REMARK 465 GLU D 3
REMARK 465 CYS D 4
REMARK 465 ASP D 5
REMARK 465 GLY D 6
REMARK 465 LYS D 7
REMARK 465 VAL D 8
REMARK 465 ASN D 9
REMARK 465 GLY D 24
REMARK 465 GLU D 41
REMARK 465 HIS D 47
REMARK 465 ILE D 48
REMARK 465 ALA D 49
REMARK 465 GLY D 50
REMARK 465 THR D 51
REMARK 465 SER D 52
REMARK 465 GLY D 53
REMARK 465 SER D 54
REMARK 465 SER D 55
REMARK 465 LEU D 56
REMARK 465 SER D 57
REMARK 465 PHE D 58
REMARK 465 HIS D 59
REMARK 465 SER D 60
REMARK 465 THR D 61
REMARK 465 VAL D 62
REMARK 465 ILE D 63
REMARK 465 ASN D 64
REMARK 465 HIS D 65
REMARK 465 TYR D 66
REMARK 465 ARG D 67
REMARK 465 MET D 68
REMARK 465 ARG D 69
REMARK 465 GLY D 70
REMARK 465 HIS D 71
REMARK 465 SER D 72
REMARK 465 PRO D 73
REMARK 465 PHE D 74
REMARK 465 ALA D 75
REMARK 465 ASN D 76
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 25 CG CD OE1 OE2
REMARK 470 THR A 26 OG1 CG2
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 SER A 66 OG
REMARK 470 SER A 67 OG
REMARK 470 THR A 69 OG1 CG2
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 GLN A 98 CG CD OE1 NE2
REMARK 470 ARG A 112 CG CD NE CZ NH1 NH2
REMARK 470 PRO A 117 CG CD
REMARK 470 GLU B 3 CG CD OE1 OE2
REMARK 470 ASP B 5 CG OD1 OD2
REMARK 470 ASN B 9 CG OD1 ND2
REMARK 470 LYS B 14 CG CD CE NZ
REMARK 470 GLU B 41 CG CD OE1 OE2
REMARK 470 LEU B 77 CG CD1 CD2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 GLU C 25 CG CD OE1 OE2
REMARK 470 GLN C 53 CG CD OE1 NE2
REMARK 470 ASP C 54 CG OD1 OD2
REMARK 470 SER C 66 OG
REMARK 470 SER C 67 OG
REMARK 470 THR C 69 OG1 CG2
REMARK 470 GLU C 71 CG CD OE1 OE2
REMARK 470 PHE C 82 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 95 CG CD OE1 OE2
REMARK 470 HIS C 115 CG ND1 CD2 CE1 NE2
REMARK 470 LEU C 116 CG CD1 CD2
REMARK 470 ILE D 10 CG1 CG2 CD1
REMARK 470 CYS D 12 SG
REMARK 470 LYS D 14 CG CD CE NZ
REMARK 470 GLN D 15 CG CD OE1 NE2
REMARK 470 VAL D 18 CG1 CG2
REMARK 470 SER D 19 OG
REMARK 470 LYS D 21 CG CD CE NZ
REMARK 470 HIS D 36 CG ND1 CD2 CE1 NE2
REMARK 470 TYR D 39 OH
REMARK 470 GLU D 43 CG CD OE1 OE2
REMARK 470 LEU D 77 CG CD1 CD2
REMARK 470 LYS D 78 CG CD CE NZ
REMARK 470 SER D 79 OG
REMARK 470 THR D 84 OG1 CG2
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 ARG D 87 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 98 CG CD OE1 NE2
REMARK 470 LYS D 103 CG CD CE NZ
REMARK 470 GLU D 111 CG CD OE1 OE2
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 OD1 ASP A 80 OH TYR A 85 2.18
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 OE2 GLU A 111 OE2 GLU C 111 2764 2.06
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 27 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 CYS A 59 CA - CB - SG ANGL. DEV. = -12.8 DEGREES
REMARK 500 CYS B 12 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU C 46 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 CYS C 59 CA - CB - SG ANGL. DEV. = -16.4 DEGREES
REMARK 500 GLY C 68 N - CA - C ANGL. DEV. = -15.3 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 THR A 26 135.12 -39.44
REMARK 500 ARG A 27 124.27 26.75
REMARK 500 TRP A 36 -46.57 -26.09
REMARK 500 SER A 44 -169.98 -162.53
REMARK 500 HIS A 58 -168.66 -112.64
REMARK 500 ASP A 80 72.70 2.23
REMARK 500 ASP A 86 29.88 40.09
REMARK 500 ASN A 107 133.22 -29.79
REMARK 500 PHE A 108 10.70 52.18
REMARK 500 LEU A 116 -152.74 -137.75
REMARK 500 GLU B 3 -75.70 -51.52
REMARK 500 CYS B 4 72.23 101.31
REMARK 500 ASP B 5 -65.30 -107.95
REMARK 500 CYS B 11 93.58 -17.83
REMARK 500 PRO B 32 -168.06 -77.13
REMARK 500 PRO B 45 -178.86 -49.63
REMARK 500 GLN B 98 19.25 49.05
REMARK 500 ASN B 107 56.11 34.28
REMARK 500 GLN C 53 -61.86 -23.00
REMARK 500 VAL C 73 -68.04 -93.87
REMARK 500 ASP C 80 92.26 10.29
REMARK 500 ASP C 86 21.47 41.12
REMARK 500 ASN C 107 146.35 -38.73
REMARK 500 PHE C 108 13.16 40.69
REMARK 500 CYS D 11 128.70 -39.06
REMARK 500 PRO D 32 -166.70 -78.16
REMARK 500 ASN D 38 157.30 69.89
REMARK 500 ASP D 95 -73.13 -74.37
REMARK 500 ASP D 96 91.73 177.56
REMARK 500 GLN D 98 23.01 46.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NYU RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO THE DEPOSITOR, PRO64 IS A
REMARK 999 DNA SEQUENCE ERROR IN THE DATABASE
REMARK 999 (PIR JQ1484). THE CORRECT
REMARK 999 RESIDUE IS ARG64. THIS HAS BEEN
REMARK 999 CONFIRMED BY SEQUENCE ALIGNMENT
REMARK 999 OF ORTHOLOGOUS PROTEINS.
DBREF 1NYS A 19 119 UNP P38444 ACVR2_RAT 34 114
DBREF 1NYS B 1 116 UNP P08476 INHBA_HUMAN 311 426
DBREF 1NYS C 19 119 UNP P38444 ACVR2_RAT 34 114
DBREF 1NYS D 1 116 UNP P08476 INHBA_HUMAN 311 426
SEQADV 1NYS ARG A 64 UNP P38444 PRO 64 SEE REMARK 999
SEQADV 1NYS LEU A 120 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS VAL A 121 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS PRO A 122 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS ARG A 123 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS ARG C 64 UNP P38444 PRO 64 SEE REMARK 999
SEQADV 1NYS LEU C 120 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS VAL C 121 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS PRO C 122 UNP P38444 CLONING ARTIFACT
SEQADV 1NYS ARG C 123 UNP P38444 CLONING ARTIFACT
SEQRES 1 A 105 SER GLY ARG GLY GLU ALA GLU THR ARG GLU CYS ILE TYR
SEQRES 2 A 105 TYR ASN ALA ASN TRP GLU LEU GLU ARG THR ASN GLN SER
SEQRES 3 A 105 GLY LEU GLU ARG CYS GLU GLY GLU GLN ASP LYS ARG LEU
SEQRES 4 A 105 HIS CYS TYR ALA SER TRP ARG ASN SER SER GLY THR ILE
SEQRES 5 A 105 GLU LEU VAL LYS LYS GLY CYS TRP LEU ASP ASP PHE ASN
SEQRES 6 A 105 CYS TYR ASP ARG GLN GLU CYS VAL ALA THR GLU GLU ASN
SEQRES 7 A 105 PRO GLN VAL TYR PHE CYS CYS CYS GLU GLY ASN PHE CYS
SEQRES 8 A 105 ASN GLU ARG PHE THR HIS LEU PRO GLU PRO LEU VAL PRO
SEQRES 9 A 105 ARG
SEQRES 1 B 116 GLY LEU GLU CYS ASP GLY LYS VAL ASN ILE CYS CYS LYS
SEQRES 2 B 116 LYS GLN PHE PHE VAL SER PHE LYS ASP ILE GLY TRP ASN
SEQRES 3 B 116 ASP TRP ILE ILE ALA PRO SER GLY TYR HIS ALA ASN TYR
SEQRES 4 B 116 CYS GLU GLY GLU CYS PRO SER HIS ILE ALA GLY THR SER
SEQRES 5 B 116 GLY SER SER LEU SER PHE HIS SER THR VAL ILE ASN HIS
SEQRES 6 B 116 TYR ARG MET ARG GLY HIS SER PRO PHE ALA ASN LEU LYS
SEQRES 7 B 116 SER CYS CYS VAL PRO THR LYS LEU ARG PRO MET SER MET
SEQRES 8 B 116 LEU TYR TYR ASP ASP GLY GLN ASN ILE ILE LYS LYS ASP
SEQRES 9 B 116 ILE GLN ASN MET ILE VAL GLU GLU CYS GLY CYS SER
SEQRES 1 C 105 SER GLY ARG GLY GLU ALA GLU THR ARG GLU CYS ILE TYR
SEQRES 2 C 105 TYR ASN ALA ASN TRP GLU LEU GLU ARG THR ASN GLN SER
SEQRES 3 C 105 GLY LEU GLU ARG CYS GLU GLY GLU GLN ASP LYS ARG LEU
SEQRES 4 C 105 HIS CYS TYR ALA SER TRP ARG ASN SER SER GLY THR ILE
SEQRES 5 C 105 GLU LEU VAL LYS LYS GLY CYS TRP LEU ASP ASP PHE ASN
SEQRES 6 C 105 CYS TYR ASP ARG GLN GLU CYS VAL ALA THR GLU GLU ASN
SEQRES 7 C 105 PRO GLN VAL TYR PHE CYS CYS CYS GLU GLY ASN PHE CYS
SEQRES 8 C 105 ASN GLU ARG PHE THR HIS LEU PRO GLU PRO LEU VAL PRO
SEQRES 9 C 105 ARG
SEQRES 1 D 116 GLY LEU GLU CYS ASP GLY LYS VAL ASN ILE CYS CYS LYS
SEQRES 2 D 116 LYS GLN PHE PHE VAL SER PHE LYS ASP ILE GLY TRP ASN
SEQRES 3 D 116 ASP TRP ILE ILE ALA PRO SER GLY TYR HIS ALA ASN TYR
SEQRES 4 D 116 CYS GLU GLY GLU CYS PRO SER HIS ILE ALA GLY THR SER
SEQRES 5 D 116 GLY SER SER LEU SER PHE HIS SER THR VAL ILE ASN HIS
SEQRES 6 D 116 TYR ARG MET ARG GLY HIS SER PRO PHE ALA ASN LEU LYS
SEQRES 7 D 116 SER CYS CYS VAL PRO THR LYS LEU ARG PRO MET SER MET
SEQRES 8 D 116 LEU TYR TYR ASP ASP GLY GLN ASN ILE ILE LYS LYS ASP
SEQRES 9 D 116 ILE GLN ASN MET ILE VAL GLU GLU CYS GLY CYS SER
HELIX 1 1 ASP A 81 TYR A 85 5 5
HELIX 2 2 PHE A 108 GLU A 111 5 4
HELIX 3 3 GLY B 24 ASP B 27 5 4
HELIX 4 4 ASN C 35 ARG C 40 1 6
HELIX 5 5 PHE C 108 GLU C 111 5 4
SHEET 1 A 5 SER A 44 ARG A 48 0
SHEET 2 A 5 GLU A 28 ASN A 33 -1 N CYS A 29 O GLU A 47
SHEET 3 A 5 ILE A 70 LEU A 79 -1 O LYS A 75 N TYR A 32
SHEET 4 A 5 LEU A 57 ASN A 65 -1 N SER A 62 O VAL A 73
SHEET 5 A 5 TYR A 100 CYS A 104 -1 O TYR A 100 N TRP A 63
SHEET 1 B 2 CYS A 90 ALA A 92 0
SHEET 2 B 2 PHE A 113 HIS A 115 1 O THR A 114 N ALA A 92
SHEET 1 C 2 CYS B 12 LYS B 14 0
SHEET 2 C 2 TYR B 39 GLU B 41 -1 O GLU B 41 N CYS B 12
SHEET 1 D 2 PHE B 17 SER B 19 0
SHEET 2 D 2 GLY B 34 HIS B 36 -1 O TYR B 35 N VAL B 18
SHEET 1 E 3 ILE B 29 ALA B 31 0
SHEET 2 E 3 CYS B 81 TYR B 94 -1 O LEU B 92 N ALA B 31
SHEET 3 E 3 ILE B 100 CYS B 115 -1 O ILE B 101 N TYR B 93
SHEET 1 F 5 SER C 44 CYS C 49 0
SHEET 2 F 5 ARG C 27 ASN C 33 -1 N TYR C 31 O GLY C 45
SHEET 3 F 5 ILE C 70 LEU C 79 -1 O LYS C 75 N TYR C 32
SHEET 4 F 5 LEU C 57 ASN C 65 -1 N HIS C 58 O TRP C 78
SHEET 5 F 5 TYR C 100 CYS C 104 -1 O CYS C 104 N CYS C 59
SHEET 1 G 2 CYS C 90 ALA C 92 0
SHEET 2 G 2 PHE C 113 HIS C 115 1 O THR C 114 N ALA C 92
SHEET 1 H 3 ILE D 29 ALA D 31 0
SHEET 2 H 3 CYS D 81 TYR D 94 -1 O LEU D 92 N ALA D 31
SHEET 3 H 3 ILE D 100 CYS D 115 -1 O ILE D 101 N TYR D 93
SSBOND 1 CYS A 29 CYS A 59 1555 1555 1.98
SSBOND 2 CYS A 49 CYS A 77 1555 1555 2.03
SSBOND 3 CYS A 84 CYS A 103 1555 1555 2.01
SSBOND 4 CYS A 90 CYS A 102 1555 1555 2.04
SSBOND 5 CYS A 104 CYS A 109 1555 1555 2.03
SSBOND 6 CYS B 4 CYS B 12 1555 1555 2.02
SSBOND 7 CYS B 11 CYS B 81 1555 1555 2.03
SSBOND 8 CYS B 40 CYS B 113 1555 1555 2.04
SSBOND 9 CYS B 44 CYS B 115 1555 1555 2.03
SSBOND 10 CYS B 80 CYS D 80 1555 1555 2.03
SSBOND 11 CYS C 29 CYS C 59 1555 1555 2.01
SSBOND 12 CYS C 49 CYS C 77 1555 1555 2.03
SSBOND 13 CYS C 84 CYS C 103 1555 1555 2.02
SSBOND 14 CYS C 90 CYS C 102 1555 1555 2.03
SSBOND 15 CYS C 104 CYS C 109 1555 1555 2.04
SSBOND 16 CYS D 11 CYS D 81 1555 1555 2.03
SSBOND 17 CYS D 40 CYS D 113 1555 1555 2.03
SSBOND 18 CYS D 44 CYS D 115 1555 1555 2.03
CISPEP 1 ALA B 31 PRO B 32 0 -0.11
CISPEP 2 ALA D 31 PRO D 32 0 -0.55
CRYST1 104.954 104.954 46.199 90.00 90.00 90.00 P 41 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 0.009528 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009528 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021645 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
