HEADER CHAPERONE 13-SEP-01 1GME
TITLE CRYSTAL STRUCTURE AND ASSEMBLY OF AN EUKARYOTIC SMALL HEAT SHOCK
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN 16.9B;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRITICUM AESTIVUM;
SOURCE 3 ORGANISM_COMMON: WHEAT;
SOURCE 4 ORGANISM_TAXID: 4565;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS SMALL HEAT SHOCK PROTEIN, CHAPERONE, ALPHA-CRYSTALLIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.L.M.VAN MONTFORT,E.BASHA,K.L.FRIEDRICH,C.SLINGSBY,E.VIERLING
REVDAT 3 05-JUL-17 1GME 1 REMARK
REVDAT 2 24-FEB-09 1GME 1 VERSN
REVDAT 1 29-NOV-01 1GME 0
JRNL AUTH R.L.M.VAN MONTFORT,E.BASHA,K.L.FRIEDRICH,C.SLINGSBY,
JRNL AUTH 2 E.VIERLING
JRNL TITL CRYSTAL STRUCTURE AND ASSEMBLY OF AN EUKARYOTIC SMALL HEAT
JRNL TITL 2 SHOCK PROTEIN
JRNL REF NAT.STRUCT.BIOL. V. 8 1025 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11702068
JRNL DOI 10.1038/NSB722
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 : MLF
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 19276
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) : 0.231
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 886
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1052
REMARK 3 BIN R VALUE (WORKING SET) : 0.3530
REMARK 3 BIN FREE R VALUE : 0.4240
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 49
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 : 4107
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.49600
REMARK 3 B22 (A**2) : -3.49600
REMARK 3 B33 (A**2) : 6.99300
REMARK 3 B12 (A**2) : -6.67700
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) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 1.490 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.709 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.558 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.599 ; 2.000
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GME COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1290008560.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.92
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19276
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.16400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SNB V. 2.1, SHARP, SOLOMON
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: MAD DATA COLLECTED ON BM14
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 26-29%
REMARK 280 PEG400, 0.2M SODIUM CITRATE, 0.1M TRIS/HCL PH8.5, PH 8.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 85.82250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.54964
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 41.38567
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 85.82250
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 49.54964
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 41.38567
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 85.82250
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 49.54964
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 41.38567
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 85.82250
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 49.54964
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 41.38567
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 85.82250
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 49.54964
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 41.38567
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 85.82250
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 49.54964
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 41.38567
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 99.09929
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 82.77133
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 99.09929
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 82.77133
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 99.09929
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 82.77133
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 99.09929
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 82.77133
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 99.09929
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 82.77133
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 99.09929
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 82.77133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PQS
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 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 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 124.15700
REMARK 350 BIOMT1 5 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 124.15700
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 124.15700
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 4 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 248.31400
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 248.31400
REMARK 350 BIOMT1 6 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 248.31400
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 MET A 1
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ILE B 3
REMARK 465 VAL B 4
REMARK 465 ARG B 5
REMARK 465 ARG B 6
REMARK 465 SER B 7
REMARK 465 ASN B 8
REMARK 465 VAL B 9
REMARK 465 PHE B 10
REMARK 465 ASP B 11
REMARK 465 PRO B 12
REMARK 465 PHE B 13
REMARK 465 ALA B 14
REMARK 465 ASP B 15
REMARK 465 LEU B 16
REMARK 465 TRP B 17
REMARK 465 ALA B 18
REMARK 465 ASP B 19
REMARK 465 PRO B 20
REMARK 465 PHE B 21
REMARK 465 ASP B 22
REMARK 465 THR B 23
REMARK 465 PHE B 24
REMARK 465 ARG B 25
REMARK 465 SER B 26
REMARK 465 ILE B 27
REMARK 465 VAL B 28
REMARK 465 PRO B 29
REMARK 465 ALA B 30
REMARK 465 ILE B 31
REMARK 465 SER B 32
REMARK 465 GLY B 33
REMARK 465 GLY B 34
REMARK 465 GLY B 35
REMARK 465 SER B 36
REMARK 465 GLU B 37
REMARK 465 THR B 38
REMARK 465 ALA B 39
REMARK 465 ALA B 40
REMARK 465 PHE B 41
REMARK 465 ALA B 42
REMARK 465 MET C 1
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ILE D 3
REMARK 465 VAL D 4
REMARK 465 ARG D 5
REMARK 465 ARG D 6
REMARK 465 SER D 7
REMARK 465 ASN D 8
REMARK 465 VAL D 9
REMARK 465 PHE D 10
REMARK 465 ASP D 11
REMARK 465 PRO D 12
REMARK 465 PHE D 13
REMARK 465 ALA D 14
REMARK 465 ASP D 15
REMARK 465 LEU D 16
REMARK 465 TRP D 17
REMARK 465 ALA D 18
REMARK 465 ASP D 19
REMARK 465 PRO D 20
REMARK 465 PHE D 21
REMARK 465 ASP D 22
REMARK 465 THR D 23
REMARK 465 PHE D 24
REMARK 465 ARG D 25
REMARK 465 SER D 26
REMARK 465 ILE D 27
REMARK 465 VAL D 28
REMARK 465 PRO D 29
REMARK 465 ALA D 30
REMARK 465 ILE D 31
REMARK 465 SER D 32
REMARK 465 GLY D 33
REMARK 465 GLY D 34
REMARK 465 GLY D 35
REMARK 465 SER D 36
REMARK 465 GLU D 37
REMARK 465 THR D 38
REMARK 465 ALA D 39
REMARK 465 ALA D 40
REMARK 465 PHE D 41
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 LYS A 141 N GLU A 143 2.16
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 OE1 GLU C 119 OE1 GLU C 119 16546 2.18
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 PRO A 142 C - N - CA ANGL. DEV. = 9.9 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 SER A 32 40.78 -74.50
REMARK 500 GLU A 84 113.47 -173.97
REMARK 500 LYS A 89 44.87 -68.43
REMARK 500 ASP A 91 104.45 -20.33
REMARK 500 ASN A 93 -11.40 116.35
REMARK 500 VAL A 118 -30.81 -38.02
REMARK 500 PRO A 142 31.40 -6.21
REMARK 500 GLU A 143 151.76 54.70
REMARK 500 SER A 150 -168.92 -69.87
REMARK 500 ASP B 75 25.91 41.48
REMARK 500 ASN B 77 26.57 -144.74
REMARK 500 GLU B 90 -152.10 62.53
REMARK 500 LYS B 117 65.76 -65.37
REMARK 500 LYS B 140 104.57 -179.06
REMARK 500 SER B 150 -83.95 -169.82
REMARK 500 PRO C 12 1.12 -62.23
REMARK 500 ALA C 30 52.04 -102.23
REMARK 500 GLU C 84 116.14 -169.53
REMARK 500 VAL C 118 -41.28 -22.42
REMARK 500 LYS C 140 -35.31 58.44
REMARK 500 LYS C 141 89.25 85.49
REMARK 500 LYS D 66 -34.36 -39.31
REMARK 500 LYS D 70 109.51 -165.18
REMARK 500 LYS D 92 -15.10 64.34
REMARK 500 ASN D 93 42.16 -108.98
REMARK 500 GLU D 143 89.25 -67.20
REMARK 500 ALA D 146 158.41 -44.76
REMARK 500 GLN D 148 139.83 -34.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE SHOWS SER AT POSITION 7 INSTEAD OF THR AS
REMARK 999 REPORTED IN THE SWISSPROT ENTRY. SUBSEQUENT RESEQUENCING
REMARK 999 HAS CONFIRMED A SERINE RESIDUE AT POSITION 7
DBREF 1GME A 1 151 UNP Q41560 Q41560 1 151
DBREF 1GME B 1 151 UNP Q41560 Q41560 1 151
DBREF 1GME C 1 151 UNP Q41560 Q41560 1 151
DBREF 1GME D 1 151 UNP Q41560 Q41560 1 151
SEQADV 1GME SER A 7 UNP Q41560 THR 7 CONFLICT
SEQADV 1GME SER B 7 UNP Q41560 THR 7 CONFLICT
SEQADV 1GME SER C 7 UNP Q41560 THR 7 CONFLICT
SEQADV 1GME SER D 7 UNP Q41560 THR 7 CONFLICT
SEQRES 1 A 151 MET SER ILE VAL ARG ARG SER ASN VAL PHE ASP PRO PHE
SEQRES 2 A 151 ALA ASP LEU TRP ALA ASP PRO PHE ASP THR PHE ARG SER
SEQRES 3 A 151 ILE VAL PRO ALA ILE SER GLY GLY GLY SER GLU THR ALA
SEQRES 4 A 151 ALA PHE ALA ASN ALA ARG MET ASP TRP LYS GLU THR PRO
SEQRES 5 A 151 GLU ALA HIS VAL PHE LYS ALA ASP LEU PRO GLY VAL LYS
SEQRES 6 A 151 LYS GLU GLU VAL LYS VAL GLU VAL GLU ASP GLY ASN VAL
SEQRES 7 A 151 LEU VAL VAL SER GLY GLU ARG THR LYS GLU LYS GLU ASP
SEQRES 8 A 151 LYS ASN ASP LYS TRP HIS ARG VAL GLU ARG SER SER GLY
SEQRES 9 A 151 LYS PHE VAL ARG ARG PHE ARG LEU LEU GLU ASP ALA LYS
SEQRES 10 A 151 VAL GLU GLU VAL LYS ALA GLY LEU GLU ASN GLY VAL LEU
SEQRES 11 A 151 THR VAL THR VAL PRO LYS ALA GLU VAL LYS LYS PRO GLU
SEQRES 12 A 151 VAL LYS ALA ILE GLN ILE SER GLY
SEQRES 1 B 151 MET SER ILE VAL ARG ARG SER ASN VAL PHE ASP PRO PHE
SEQRES 2 B 151 ALA ASP LEU TRP ALA ASP PRO PHE ASP THR PHE ARG SER
SEQRES 3 B 151 ILE VAL PRO ALA ILE SER GLY GLY GLY SER GLU THR ALA
SEQRES 4 B 151 ALA PHE ALA ASN ALA ARG MET ASP TRP LYS GLU THR PRO
SEQRES 5 B 151 GLU ALA HIS VAL PHE LYS ALA ASP LEU PRO GLY VAL LYS
SEQRES 6 B 151 LYS GLU GLU VAL LYS VAL GLU VAL GLU ASP GLY ASN VAL
SEQRES 7 B 151 LEU VAL VAL SER GLY GLU ARG THR LYS GLU LYS GLU ASP
SEQRES 8 B 151 LYS ASN ASP LYS TRP HIS ARG VAL GLU ARG SER SER GLY
SEQRES 9 B 151 LYS PHE VAL ARG ARG PHE ARG LEU LEU GLU ASP ALA LYS
SEQRES 10 B 151 VAL GLU GLU VAL LYS ALA GLY LEU GLU ASN GLY VAL LEU
SEQRES 11 B 151 THR VAL THR VAL PRO LYS ALA GLU VAL LYS LYS PRO GLU
SEQRES 12 B 151 VAL LYS ALA ILE GLN ILE SER GLY
SEQRES 1 C 151 MET SER ILE VAL ARG ARG SER ASN VAL PHE ASP PRO PHE
SEQRES 2 C 151 ALA ASP LEU TRP ALA ASP PRO PHE ASP THR PHE ARG SER
SEQRES 3 C 151 ILE VAL PRO ALA ILE SER GLY GLY GLY SER GLU THR ALA
SEQRES 4 C 151 ALA PHE ALA ASN ALA ARG MET ASP TRP LYS GLU THR PRO
SEQRES 5 C 151 GLU ALA HIS VAL PHE LYS ALA ASP LEU PRO GLY VAL LYS
SEQRES 6 C 151 LYS GLU GLU VAL LYS VAL GLU VAL GLU ASP GLY ASN VAL
SEQRES 7 C 151 LEU VAL VAL SER GLY GLU ARG THR LYS GLU LYS GLU ASP
SEQRES 8 C 151 LYS ASN ASP LYS TRP HIS ARG VAL GLU ARG SER SER GLY
SEQRES 9 C 151 LYS PHE VAL ARG ARG PHE ARG LEU LEU GLU ASP ALA LYS
SEQRES 10 C 151 VAL GLU GLU VAL LYS ALA GLY LEU GLU ASN GLY VAL LEU
SEQRES 11 C 151 THR VAL THR VAL PRO LYS ALA GLU VAL LYS LYS PRO GLU
SEQRES 12 C 151 VAL LYS ALA ILE GLN ILE SER GLY
SEQRES 1 D 151 MET SER ILE VAL ARG ARG SER ASN VAL PHE ASP PRO PHE
SEQRES 2 D 151 ALA ASP LEU TRP ALA ASP PRO PHE ASP THR PHE ARG SER
SEQRES 3 D 151 ILE VAL PRO ALA ILE SER GLY GLY GLY SER GLU THR ALA
SEQRES 4 D 151 ALA PHE ALA ASN ALA ARG MET ASP TRP LYS GLU THR PRO
SEQRES 5 D 151 GLU ALA HIS VAL PHE LYS ALA ASP LEU PRO GLY VAL LYS
SEQRES 6 D 151 LYS GLU GLU VAL LYS VAL GLU VAL GLU ASP GLY ASN VAL
SEQRES 7 D 151 LEU VAL VAL SER GLY GLU ARG THR LYS GLU LYS GLU ASP
SEQRES 8 D 151 LYS ASN ASP LYS TRP HIS ARG VAL GLU ARG SER SER GLY
SEQRES 9 D 151 LYS PHE VAL ARG ARG PHE ARG LEU LEU GLU ASP ALA LYS
SEQRES 10 D 151 VAL GLU GLU VAL LYS ALA GLY LEU GLU ASN GLY VAL LEU
SEQRES 11 D 151 THR VAL THR VAL PRO LYS ALA GLU VAL LYS LYS PRO GLU
SEQRES 12 D 151 VAL LYS ALA ILE GLN ILE SER GLY
FORMUL 5 HOH *33(H2 O)
HELIX 1 1 ALA A 14 ALA A 18 5 5
HELIX 2 2 ASP A 19 VAL A 28 1 10
HELIX 3 3 PRO A 29 ILE A 31 5 3
HELIX 4 4 GLU A 37 ALA A 42 1 6
HELIX 5 5 LYS A 65 GLU A 67 5 3
HELIX 6 6 LYS A 117 VAL A 121 5 5
HELIX 7 7 LYS B 117 VAL B 121 5 5
HELIX 8 8 ALA C 14 ALA C 18 5 5
HELIX 9 9 ASP C 19 VAL C 28 1 10
HELIX 10 10 PRO C 29 ILE C 31 5 3
HELIX 11 11 GLU C 37 ALA C 42 1 6
HELIX 12 12 LYS D 65 GLU D 67 5 3
HELIX 13 13 LYS D 117 VAL D 121 5 5
SHEET 1 AA 5 LYS A 122 GLU A 126 0
SHEET 2 AA 5 VAL A 129 PRO A 135 -1 O VAL A 129 N GLU A 126
SHEET 3 AA 5 ALA A 54 ASP A 60 -1 O HIS A 55 N VAL A 134
SHEET 4 AA 5 MET A 46 GLU A 50 -1 O ASP A 47 N LYS A 58
SHEET 5 AA 5 TRP B 96 ARG B 98 -1 N HIS B 97 O TRP A 48
SHEET 1 AB 3 VAL A 69 GLU A 74 0
SHEET 2 AB 3 VAL A 78 GLY A 83 -1 O VAL A 78 N GLU A 74
SHEET 3 AB 3 PHE A 106 ARG A 111 -1 O PHE A 106 N GLY A 83
SHEET 1 AC 5 LYS A 95 ARG A 98 0
SHEET 2 AC 5 MET B 46 GLU B 50 -1 O TRP B 48 N HIS A 97
SHEET 3 AC 5 ALA B 54 ASP B 60 -1 O VAL B 56 N LYS B 49
SHEET 4 AC 5 VAL B 129 PRO B 135 -1 O LEU B 130 N ALA B 59
SHEET 5 AC 5 LYS B 122 GLU B 126 -1 O LYS B 122 N THR B 133
SHEET 1 BA 3 VAL B 69 GLU B 74 0
SHEET 2 BA 3 VAL B 78 ARG B 85 -1 O VAL B 78 N GLU B 74
SHEET 3 BA 3 GLY B 104 ARG B 111 -1 O GLY B 104 N ARG B 85
SHEET 1 CA 4 VAL C 9 PHE C 10 0
SHEET 2 CA 4 PHE C 106 ARG C 111 1 O ARG C 109 N PHE C 10
SHEET 3 CA 4 VAL C 78 GLY C 83 -1 O LEU C 79 N PHE C 110
SHEET 4 CA 4 VAL C 69 GLU C 74 -1 O LYS C 70 N SER C 82
SHEET 1 CB 5 LYS C 122 GLU C 126 0
SHEET 2 CB 5 VAL C 129 PRO C 135 -1 O VAL C 129 N GLU C 126
SHEET 3 CB 5 ALA C 54 ASP C 60 -1 O HIS C 55 N VAL C 134
SHEET 4 CB 5 MET C 46 GLU C 50 -1 O ASP C 47 N LYS C 58
SHEET 5 CB 5 LYS D 95 VAL D 99 -1 O LYS D 95 N GLU C 50
SHEET 1 CC 5 LYS C 95 VAL C 99 0
SHEET 2 CC 5 MET D 46 GLU D 50 -1 O TRP D 48 N HIS C 97
SHEET 3 CC 5 ALA D 54 ASP D 60 -1 O VAL D 56 N LYS D 49
SHEET 4 CC 5 VAL D 129 PRO D 135 -1 O LEU D 130 N ALA D 59
SHEET 5 CC 5 LYS D 122 LEU D 125 -1 O LYS D 122 N THR D 133
SHEET 1 DA 3 VAL D 69 GLU D 74 0
SHEET 2 DA 3 VAL D 78 ARG D 85 -1 O VAL D 78 N GLU D 74
SHEET 3 DA 3 GLY D 104 ARG D 111 -1 O GLY D 104 N ARG D 85
CRYST1 171.645 171.645 124.157 90.00 90.00 120.00 H 3 2 72
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 0.005826 0.003364 0.000000 0.00000
SCALE2 0.000000 0.006727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008054 0.00000
MTRIX1 1 -0.780000 0.459500 0.424800 -19.05420 1
MTRIX2 1 0.461500 -0.036100 0.886400 -48.39810 1
MTRIX3 1 0.422600 0.887500 -0.183900 62.48180 1
MTRIX1 2 0.506600 0.862200 -0.001600 0.15700 1
MTRIX2 2 0.862200 -0.506600 -0.000800 0.05720 1
MTRIX3 2 -0.001500 -0.000900 -1.000000 186.45500 1
MTRIX1 3 -0.029300 -0.887100 -0.460600 65.24620 1
MTRIX2 3 0.220000 0.443800 -0.868700 114.12780 1
MTRIX3 3 0.975100 -0.126800 0.182200 28.12910 1
(ATOM LINES ARE NOT SHOWN.)
END
