HEADER HYDROLASE 02-JUL-96 2HVM
TITLE HEVAMINE A AT 1.8 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEVAMINE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHITINASE/LYSOZYME;
COMPND 5 EC: 3.2.1.14, 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_TAXID: 3981;
SOURCE 4 TISSUE: LATEX
KEYWDS HYDROLASE, CHITINASE/LYSOZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.TERWISSCHA VAN SCHELTINGA,M.HENNIG,B.W.DIJKSTRA
REVDAT 3 24-FEB-09 2HVM 1 VERSN
REVDAT 2 01-APR-03 2HVM 1 JRNL
REVDAT 1 11-JAN-97 2HVM 0
SPRSDE 11-JAN-97 2HVM 1HVM
JRNL AUTH A.C.TERWISSCHA VAN SCHELTINGA,M.HENNIG,B.W.DIJKSTRA
JRNL TITL THE 1.8 A RESOLUTION STRUCTURE OF HEVAMINE, A
JRNL TITL 2 PLANT CHITINASE/LYSOZYME, AND ANALYSIS OF THE
JRNL TITL 3 CONSERVED SEQUENCE AND STRUCTURE MOTIFS OF
JRNL TITL 4 GLYCOSYL HYDROLASE FAMILY 18.
JRNL REF J.MOL.BIOL. V. 262 243 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8831791
JRNL DOI 10.1006/JMBI.1996.0510
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.C.TERWISSCHA VAN SCHELTINGA,S.ARMAND,K.H.KALK,
REMARK 1 AUTH 2 A.ISOGAI,B.HENRISSAT,B.W.DIJKSTRA
REMARK 1 TITL STEREOCHEMISTRY OF CHITIN HYDROLYSIS BY A PLANT
REMARK 1 TITL 2 CHITINASE/LYSOZYME AND X-RAY STRUCTURE OF A
REMARK 1 TITL 3 COMPLEX WITH ALLOSAMIDIN. EVIDENCE FOR SUBSTRATE
REMARK 1 TITL 4 ASSISTED CATALYSIS
REMARK 1 REF BIOCHEMISTRY V. 34 15619 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.C.TERWISSCHA VAN SCHELTINGA,K.H.KALK,
REMARK 1 AUTH 2 J.J.BEINTEMA,B.W.DIJKSTRA
REMARK 1 TITL CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE
REMARK 1 TITL 2 PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND
REMARK 1 TITL 3 ITS COMPLEX WITH AN INHIBITOR
REMARK 1 REF STRUCTURE V. 2 1181 1994
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.J.ROZEBOOM,A.BUDIANI,J.J.BEINTEMA,B.W.DIJKSTRA
REMARK 1 TITL CRYSTALLIZATION OF HEVAMINE, AN ENZYME WITH
REMARK 1 TITL 2 LYSOZYME/CHITINASE ACTIVITY FROM HEVEA
REMARK 1 TITL 3 BRASILIENSIS LATEX
REMARK 1 REF J.MOL.BIOL. V. 212 441 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.0
REMARK 3 NUMBER OF REFLECTIONS : 20520
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1480
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2087
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.010 ; 1.300 ; 4296
REMARK 3 BOND ANGLES (DEGREES) : 1.290 ; 1.200 ; 5826
REMARK 3 TORSION ANGLES (DEGREES) : 22.900; 0.000 ; 2492
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.010 ; 2.000 ; 102
REMARK 3 GENERAL PLANES (A) : 0.030 ; 0.000 ; 628
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 2.680 ; 60.000; 2148
REMARK 3 NON-BONDED CONTACTS (A) : 0.010 ; 40.000; 57
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : 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 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HVM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-93
REMARK 200 TEMPERATURE (KELVIN) : 279
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23188
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.15000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.02500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.02500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.15000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.86000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ALA A 47 -124.17 54.58
REMARK 500 SER A 84 48.30 -103.49
REMARK 500 LEU A 105 -141.78 -105.09
REMARK 500 ASP A 125 62.73 -113.50
REMARK 500 TYR A 133 -7.54 79.37
REMARK 500 PHE A 182 54.82 -90.33
REMARK 500 SER A 192 114.93 -36.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HVM A 1 273 UNP P23472 CHLY_HEVBR 1 273
SEQRES 1 A 273 GLY GLY ILE ALA ILE TYR TRP GLY GLN ASN GLY ASN GLU
SEQRES 2 A 273 GLY THR LEU THR GLN THR CYS SER THR ARG LYS TYR SER
SEQRES 3 A 273 TYR VAL ASN ILE ALA PHE LEU ASN LYS PHE GLY ASN GLY
SEQRES 4 A 273 GLN THR PRO GLN ILE ASN LEU ALA GLY HIS CYS ASN PRO
SEQRES 5 A 273 ALA ALA GLY GLY CYS THR ILE VAL SER ASN GLY ILE ARG
SEQRES 6 A 273 SER CYS GLN ILE GLN GLY ILE LYS VAL MET LEU SER LEU
SEQRES 7 A 273 GLY GLY GLY ILE GLY SER TYR THR LEU ALA SER GLN ALA
SEQRES 8 A 273 ASP ALA LYS ASN VAL ALA ASP TYR LEU TRP ASN ASN PHE
SEQRES 9 A 273 LEU GLY GLY LYS SER SER SER ARG PRO LEU GLY ASP ALA
SEQRES 10 A 273 VAL LEU ASP GLY ILE ASP PHE ASP ILE GLU HIS GLY SER
SEQRES 11 A 273 THR LEU TYR TRP ASP ASP LEU ALA ARG TYR LEU SER ALA
SEQRES 12 A 273 TYR SER LYS GLN GLY LYS LYS VAL TYR LEU THR ALA ALA
SEQRES 13 A 273 PRO GLN CYS PRO PHE PRO ASP ARG TYR LEU GLY THR ALA
SEQRES 14 A 273 LEU ASN THR GLY LEU PHE ASP TYR VAL TRP VAL GLN PHE
SEQRES 15 A 273 TYR ASN ASN PRO PRO CYS GLN TYR SER SER GLY ASN ILE
SEQRES 16 A 273 ASN ASN ILE ILE ASN SER TRP ASN ARG TRP THR THR SER
SEQRES 17 A 273 ILE ASN ALA GLY LYS ILE PHE LEU GLY LEU PRO ALA ALA
SEQRES 18 A 273 PRO GLU ALA ALA GLY SER GLY TYR VAL PRO PRO ASP VAL
SEQRES 19 A 273 LEU ILE SER ARG ILE LEU PRO GLU ILE LYS LYS SER PRO
SEQRES 20 A 273 LYS TYR GLY GLY VAL MET LEU TRP SER LYS PHE TYR ASP
SEQRES 21 A 273 ASP LYS ASN GLY TYR SER SER SER ILE LEU ASP SER VAL
FORMUL 2 HOH *206(H2 O)
HELIX 1 1 GLY A 11 GLU A 13 5 3
HELIX 2 2 LEU A 16 THR A 22 1 7
HELIX 3 3 ALA A 47 HIS A 49 5 3
HELIX 4 4 ALA A 53 GLY A 55 5 3
HELIX 5 5 THR A 58 GLN A 70 5 13
HELIX 6 6 GLN A 90 ASN A 103 1 14
HELIX 7 7 TRP A 134 GLN A 147 1 14
HELIX 8 8 GLY A 167 THR A 172 1 6
HELIX 9 9 PRO A 186 CYS A 188 5 3
HELIX 10 10 ASN A 196 SER A 208 1 13
HELIX 11 11 PRO A 222 ALA A 224 5 3
HELIX 12 12 PRO A 232 SER A 237 1 6
HELIX 13 13 LEU A 240 LYS A 245 1 6
HELIX 14 14 LYS A 257 ASN A 263 1 7
HELIX 15 15 TYR A 265 ILE A 269 1 5
SHEET 1 A 8 TYR A 152 ALA A 155 0
SHEET 2 A 8 GLY A 121 ASP A 125 1 N ILE A 122 O TYR A 152
SHEET 3 A 8 LYS A 73 GLY A 79 1 N LEU A 76 O GLY A 121
SHEET 4 A 8 TYR A 27 ILE A 30 1 N VAL A 28 O LYS A 73
SHEET 5 A 8 GLY A 2 TRP A 7 1 N ILE A 5 O TYR A 27
SHEET 6 A 8 TYR A 249 TRP A 255 1 N VAL A 252 O GLY A 2
SHEET 7 A 8 LYS A 213 PRO A 219 1 N ILE A 214 O GLY A 250
SHEET 8 A 8 TYR A 177 GLN A 181 1 N VAL A 178 O LYS A 213
SSBOND 1 CYS A 20 CYS A 67 1555 1555 2.03
SSBOND 2 CYS A 50 CYS A 57 1555 1555 2.03
SSBOND 3 CYS A 159 CYS A 188 1555 1555 2.03
CISPEP 1 ALA A 31 PHE A 32 0 12.40
CISPEP 2 PHE A 161 PRO A 162 0 -5.06
CISPEP 3 TRP A 255 SER A 256 0 -0.05
CRYST1 52.300 57.720 82.050 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019120 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012188 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
