HEADER TRANSFERASE 19-JAN-04 1S4Y
TITLE CRYSTAL STRUCTURE OF THE ACTIVIN/ACTRIIB EXTRACELLULAR DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIVIN RECEPTOR TYPE IIB PRECURSOR;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: ACTR-IIB;
COMPND 6 EC: 2.7.1.37;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INHIBIN BETA A CHAIN;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: ACTIVIN BETA-A CHAIN, ERYTHROID DIFFERENTIATION PROTEIN,
COMPND 12 EDF;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACVR2B;
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: INHBA;
SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS STRUCTURAL GENOMICS, JCSG, TRANSFERASE, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, JOINT CENTER FOR STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GREENWALD,M.E.VEGA,G.P.ALLENDORPH,W.H.FISCHER,W.VALE,S.CHOE,JOINT
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 13-JUL-11 1S4Y 1 VERSN
REVDAT 4 24-FEB-09 1S4Y 1 VERSN
REVDAT 3 18-JAN-05 1S4Y 1 AUTHOR KEYWDS REMARK
REVDAT 2 17-AUG-04 1S4Y 1 JRNL
REVDAT 1 10-AUG-04 1S4Y 0
JRNL AUTH J.GREENWALD,M.E.VEGA,G.P.ALLENDORPH,W.H.FISCHER,W.VALE,
JRNL AUTH 2 S.CHOE
JRNL TITL A FLEXIBLE ACTIVIN EXPLAINS THE MEMBRANE-DEPENDENT
JRNL TITL 2 COOPERATIVE ASSEMBLY OF TGF-BETA FAMILY RECEPTORS.
JRNL REF MOL.CELL V. 15 485 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 15304227
JRNL DOI 10.1016/J.MOLCEL.2004.07.011
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 18101
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) : 0.206
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 988
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1262
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3102
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.72000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : 0.96000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.403
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.206
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.367
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3195 ; 0.031 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2606 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4326 ; 2.385 ; 1.928
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6090 ; 1.109 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 385 ; 9.264 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 436 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3603 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 675 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 626 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3072 ; 0.254 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1908 ; 0.103 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 135 ; 0.252 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 51 ; 0.261 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 133 ; 0.274 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 16 ; 0.378 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1946 ; 1.170 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3099 ; 2.086 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1249 ; 3.378 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1227 ; 5.037 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 95
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7191 27.3673 -1.8856
REMARK 3 T TENSOR
REMARK 3 T11: 0.0392 T22: 0.2876
REMARK 3 T33: 0.0963 T12: 0.0542
REMARK 3 T13: 0.0516 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 4.5825 L22: 6.7980
REMARK 3 L33: 5.7008 L12: 0.8426
REMARK 3 L13: -0.9667 L23: -1.3069
REMARK 3 S TENSOR
REMARK 3 S11: 0.1324 S12: -0.4428 S13: -0.1557
REMARK 3 S21: 0.2414 S22: -0.1950 S23: -0.4941
REMARK 3 S31: 0.1104 S32: 0.7250 S33: 0.0627
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 116
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8592 32.0502 17.3911
REMARK 3 T TENSOR
REMARK 3 T11: 0.1624 T22: 0.1430
REMARK 3 T33: 0.1216 T12: -0.0369
REMARK 3 T13: 0.0242 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 1.3398 L22: 0.1993
REMARK 3 L33: 10.4859 L12: 0.1686
REMARK 3 L13: -1.6345 L23: 0.0709
REMARK 3 S TENSOR
REMARK 3 S11: 0.1986 S12: -0.2073 S13: 0.1110
REMARK 3 S21: 0.2048 S22: -0.0731 S23: 0.0726
REMARK 3 S31: -0.3839 S32: -0.1986 S33: -0.1254
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 4 C 98
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3412 61.8163 27.0920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1050 T22: 0.0762
REMARK 3 T33: 0.1747 T12: -0.0754
REMARK 3 T13: 0.0355 T23: -0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 7.6593 L22: 7.8998
REMARK 3 L33: 4.4353 L12: -0.1698
REMARK 3 L13: 1.5670 L23: 0.0946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0469 S12: 0.4369 S13: -0.4348
REMARK 3 S21: -0.2361 S22: 0.0790 S23: -0.2023
REMARK 3 S31: -0.0837 S32: -0.0132 S33: -0.1259
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 4 D 116
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2145 47.6157 23.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.2827 T22: 0.2871
REMARK 3 T33: 0.2347 T12: -0.0882
REMARK 3 T13: -0.0231 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 10.8068 L22: 7.6229
REMARK 3 L33: 2.7752 L12: 7.5738
REMARK 3 L13: 4.8658 L23: 3.2454
REMARK 3 S TENSOR
REMARK 3 S11: 0.0842 S12: -0.0390 S13: 0.2878
REMARK 3 S21: -0.2309 S22: -0.0510 S23: 0.3190
REMARK 3 S31: 0.0779 S32: -0.3463 S33: -0.0331
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1S4Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-04.
REMARK 100 THE RCSB ID CODE IS RCSB021372.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19028
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21300
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM CHLORIDE, BIS
REMARK 280 TRIS, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 43.14500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.31350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.14500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.31350
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: 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 GLU A 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 GLU A 96
REMARK 465 PRO A 97
REMARK 465 GLY A 98
REMARK 465 GLY B 6
REMARK 465 LYS B 7
REMARK 465 GLY B 70
REMARK 465 HIS B 71
REMARK 465 SER B 72
REMARK 465 GLU C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 GLY D 1
REMARK 465 LEU D 2
REMARK 465 GLU D 3
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 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 465 LEU D 77
REMARK 465 LYS D 78
REMARK 465 SER D 79
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 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 67 CG CD OE1 OE2
REMARK 470 VAL B 8 CG1 CG2
REMARK 470 SER B 52 OG
REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 69 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 73 CG CD
REMARK 470 ASN B 76 CG OD1
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 30 CG CD OE1 OE2
REMARK 470 GLN C 31 CG CD OE1 NE2
REMARK 470 SER C 44 OG
REMARK 470 GLN C 76 CG CD OE1 NE2
REMARK 470 LYS D 7 CG CD CE NZ
REMARK 470 ASP D 22 CG OD1 OD2
REMARK 470 GLU D 41 CG CD OE1 OE2
REMARK 470 THR D 61 OG1 CG2
REMARK 470 ILE D 63 CG1 CG2 CD1
REMARK 470 ASN D 64 CG OD1
REMARK 470 ARG D 67 CG CD NE CZ NH1 NH2
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 O HOH A 130 O HOH A 160 1.53
REMARK 500 O HOH A 138 O HOH B 134 1.73
REMARK 500 O LEU A 50 O HOH A 130 1.99
REMARK 500 ND2 ASN C 20 O HOH C 111 2.00
REMARK 500 O HOH A 113 O HOH A 138 2.08
REMARK 500 O SER D 116 O HOH D 128 2.11
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 ALA D 49 O HOH A 136 4455 1.61
REMARK 500 NE2 GLN A 66 O ALA B 75 4556 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN A 31 C GLN A 31 O 0.248
REMARK 500 GLN A 31 C ASP A 32 N 0.155
REMARK 500 TRP A 56 CG TRP A 56 CD1 -0.101
REMARK 500 PHE A 60 CG PHE A 60 CD2 0.110
REMARK 500 PHE A 60 CG PHE A 60 CD1 0.102
REMARK 500 PHE A 60 CE1 PHE A 60 CZ 0.153
REMARK 500 CYS A 62 CB CYS A 62 SG 0.104
REMARK 500 ASP A 64 CA ASP A 64 CB 0.164
REMARK 500 GLY B 1 N GLY B 1 CA 0.093
REMARK 500 ALA D 49 C ALA D 49 O 0.556
REMARK 500 ASP D 96 CG ASP D 96 OD1 0.157
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 34 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 59 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 LEU B 2 CA - CB - CG ANGL. DEV. = 18.6 DEGREES
REMARK 500 LEU B 2 CB - CG - CD1 ANGL. DEV. = 14.6 DEGREES
REMARK 500 LEU B 2 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ASP B 104 CB - CG - OD2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 ASP C 58 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP C 59 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 CYS C 87 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 ALA D 49 CA - C - O ANGL. DEV. = -19.9 DEGREES
REMARK 500 CYS D 80 CA - CB - SG ANGL. DEV. = 7.1 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 ASN A 13 30.84 -99.13
REMARK 500 GLN A 31 -75.85 -3.52
REMARK 500 SER A 45 67.11 24.21
REMARK 500 ASP A 58 118.40 -37.61
REMARK 500 ASP A 64 37.32 30.27
REMARK 500 LEU B 2 -38.43 -165.19
REMARK 500 ASN B 9 -146.50 -155.69
REMARK 500 CYS B 11 115.92 -25.75
REMARK 500 ASN B 38 175.41 60.24
REMARK 500 MET B 68 26.21 -74.39
REMARK 500 GLU C 30 170.75 -55.15
REMARK 500 ASN C 43 81.93 -159.55
REMARK 500 SER C 45 15.37 -140.96
REMARK 500 VAL C 51 -71.81 -106.10
REMARK 500 ASP C 58 115.19 -22.72
REMARK 500 ASP C 64 33.03 70.83
REMARK 500 ASN C 74 64.07 -155.59
REMARK 500 LYS D 7 -44.43 -134.88
REMARK 500 PHE D 16 110.42 -161.81
REMARK 500 ASN D 38 -164.98 -66.44
REMARK 500 SER D 60 -76.74 -26.21
REMARK 500 ILE D 63 -77.81 -48.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS B 4 ASP B 5 144.18
REMARK 500 ASP C 32 LYS C 33 -149.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASP A 58 -11.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 356547 RELATED DB: TARGETDB
DBREF 1S4Y A 1 98 UNP P27040 AVR2B_MOUSE 23 120
DBREF 1S4Y B 1 116 UNP P08476 INHBA_HUMAN 311 426
DBREF 1S4Y C 1 98 UNP P27040 AVR2B_MOUSE 23 120
DBREF 1S4Y D 1 116 UNP P08476 INHBA_HUMAN 311 426
SEQRES 1 A 98 GLU ALA GLU THR ARG GLU CYS ILE TYR TYR ASN ALA ASN
SEQRES 2 A 98 TRP GLU LEU GLU ARG THR ASN GLN SER GLY LEU GLU ARG
SEQRES 3 A 98 CYS GLU GLY GLU GLN ASP LYS ARG LEU HIS CYS TYR ALA
SEQRES 4 A 98 SER TRP ARG ASN SER SER GLY THR ILE GLU LEU VAL LYS
SEQRES 5 A 98 LYS GLY CYS TRP LEU ASP ASP PHE ASN CYS TYR ASP ARG
SEQRES 6 A 98 GLN GLU CYS VAL ALA THR GLU GLU ASN PRO GLN VAL TYR
SEQRES 7 A 98 PHE CYS CYS CYS GLU GLY ASN PHE CYS ASN GLU ARG PHE
SEQRES 8 A 98 THR HIS LEU PRO GLU PRO GLY
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 98 GLU ALA GLU THR ARG GLU CYS ILE TYR TYR ASN ALA ASN
SEQRES 2 C 98 TRP GLU LEU GLU ARG THR ASN GLN SER GLY LEU GLU ARG
SEQRES 3 C 98 CYS GLU GLY GLU GLN ASP LYS ARG LEU HIS CYS TYR ALA
SEQRES 4 C 98 SER TRP ARG ASN SER SER GLY THR ILE GLU LEU VAL LYS
SEQRES 5 C 98 LYS GLY CYS TRP LEU ASP ASP PHE ASN CYS TYR ASP ARG
SEQRES 6 C 98 GLN GLU CYS VAL ALA THR GLU GLU ASN PRO GLN VAL TYR
SEQRES 7 C 98 PHE CYS CYS CYS GLU GLY ASN PHE CYS ASN GLU ARG PHE
SEQRES 8 C 98 THR HIS LEU PRO GLU PRO GLY
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
FORMUL 5 HOH *177(H2 O)
HELIX 1 1 ASN A 13 ARG A 18 1 6
HELIX 2 2 ASP A 59 TYR A 63 5 5
HELIX 3 3 GLY B 24 ASP B 27 5 4
HELIX 4 4 SER B 57 MET B 68 1 12
HELIX 5 5 ASN C 13 ARG C 18 1 6
HELIX 6 6 ASP C 59 TYR C 63 5 5
HELIX 7 7 PHE C 86 GLU C 89 5 4
HELIX 8 8 PHE D 20 GLY D 24 1 5
HELIX 9 9 TRP D 25 ASP D 27 5 3
HELIX 10 10 PHE D 58 MET D 68 1 11
SHEET 1 A 5 SER A 22 ARG A 26 0
SHEET 2 A 5 GLU A 6 ASN A 11 -1 N TYR A 9 O GLY A 23
SHEET 3 A 5 THR A 47 LEU A 57 -1 O LYS A 53 N TYR A 10
SHEET 4 A 5 LEU A 35 SER A 44 -1 N SER A 40 O VAL A 51
SHEET 5 A 5 TYR A 78 GLU A 83 -1 O TYR A 78 N TRP A 41
SHEET 1 B 2 CYS B 12 LYS B 14 0
SHEET 2 B 2 TYR B 39 GLU B 41 -1 O TYR B 39 N LYS B 14
SHEET 1 C 2 PHE B 17 SER B 19 0
SHEET 2 C 2 GLY B 34 HIS B 36 -1 O TYR B 35 N VAL B 18
SHEET 1 D 3 ILE B 29 ALA B 31 0
SHEET 2 D 3 CYS B 81 TYR B 94 -1 O LEU B 92 N ALA B 31
SHEET 3 D 3 ILE B 100 CYS B 115 -1 O ILE B 101 N TYR B 93
SHEET 1 E 5 SER C 22 ARG C 26 0
SHEET 2 E 5 GLU C 6 ASN C 11 -1 N CYS C 7 O GLU C 25
SHEET 3 E 5 GLU C 49 LEU C 57 -1 O LYS C 53 N TYR C 10
SHEET 4 E 5 LEU C 35 ARG C 42 -1 N ARG C 42 O GLU C 49
SHEET 5 E 5 TYR C 78 CYS C 82 -1 O TYR C 78 N TRP C 41
SHEET 1 F 2 CYS C 68 ALA C 70 0
SHEET 2 F 2 PHE C 91 HIS C 93 1 O THR C 92 N ALA C 70
SHEET 1 G 2 CYS D 12 LYS D 14 0
SHEET 2 G 2 TYR D 39 GLU D 41 -1 O TYR D 39 N LYS D 14
SHEET 1 H 2 PHE D 17 SER D 19 0
SHEET 2 H 2 GLY D 34 HIS D 36 -1 O TYR D 35 N VAL D 18
SHEET 1 I 3 ILE D 29 ALA D 31 0
SHEET 2 I 3 CYS D 81 TYR D 94 -1 O LEU D 92 N ALA D 31
SHEET 3 I 3 ILE D 100 CYS D 115 -1 O ILE D 101 N TYR D 93
SSBOND 1 CYS A 7 CYS A 37 1555 1555 2.12
SSBOND 2 CYS A 27 CYS A 55 1555 1555 2.08
SSBOND 3 CYS A 62 CYS A 81 1555 1555 2.11
SSBOND 4 CYS A 68 CYS A 80 1555 1555 2.07
SSBOND 5 CYS A 82 CYS A 87 1555 1555 2.07
SSBOND 6 CYS B 4 CYS B 12 1555 1555 2.07
SSBOND 7 CYS B 11 CYS B 81 1555 1555 2.00
SSBOND 8 CYS B 40 CYS B 113 1555 1555 2.04
SSBOND 9 CYS B 44 CYS B 115 1555 1555 2.06
SSBOND 10 CYS B 80 CYS D 80 1555 1555 2.04
SSBOND 11 CYS C 7 CYS C 37 1555 1555 2.07
SSBOND 12 CYS C 27 CYS C 55 1555 1555 2.11
SSBOND 13 CYS C 62 CYS C 81 1555 1555 2.05
SSBOND 14 CYS C 68 CYS C 80 1555 1555 2.19
SSBOND 15 CYS C 82 CYS C 87 1555 1555 2.05
SSBOND 16 CYS D 4 CYS D 12 1555 1555 2.06
SSBOND 17 CYS D 11 CYS D 81 1555 1555 2.07
SSBOND 18 CYS D 40 CYS D 113 1555 1555 2.03
SSBOND 19 CYS D 44 CYS D 115 1555 1555 2.06
CISPEP 1 ALA B 31 PRO B 32 0 -0.90
CISPEP 2 ALA D 31 PRO D 32 0 1.35
CISPEP 3 CYS D 44 PRO D 45 0 -1.31
CRYST1 86.290 120.627 43.550 90.00 90.00 90.00 P 21 21 2 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 0.011589 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008290 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022962 0.00000
(ATOM LINES ARE NOT SHOWN.)
END