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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 06-DEC-93 1TIA 1TIA 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL ACYLHYDROLASE) 1TIA 3
SOURCE (PENICILLIUM CAMEMBERTII) 1TIA 4
AUTHOR U.DEREWENDA,L.SWENSON,S.YAMAGUCHI,Y.WEI,Z.S.DEREWENDA 1TIA 5
REVDAT 1 26-JAN-95 1TIA 0 1TIA 6
JRNL AUTH U.DEREWENDA,L.SWENSON,R.GREEN,Y.WEI,G.G.DODSON, 1TIA 7
JRNL AUTH 2 S.YAMAGUCHI,M.J.HAAS,Z.S.DEREWENDA 1TIA 8
JRNL TITL AN UNUSUAL BURIED POLAR CLUSTER IN A FAMILY OF 1TIA 9
JRNL TITL 2 FUNGAL LIPASES 1TIA 10
JRNL REF NAT.STRUCT.BIOL. V. 1 36 1994 1TIA 11
JRNL REFN ASTM NSBIEW US ISSN 1072-8368 2024 1TIA 12
REMARK 1 1TIA 13
REMARK 1 REFERENCE 1 1TIA 14
REMARK 1 AUTH U.DEREWENDA,L.SWENSON,R.GREEN,Y.WEI,S.YAMAGUCHI, 1TIA 15
REMARK 1 AUTH 2 R.JOERGER,M.J.HAAS,Z.S.DEREWENDA 1TIA 16
REMARK 1 TITL CURRENT PROGRESS IN CRYSTALLOGRAPHIC STUDIES OF NEW 1TIA 17
REMARK 1 TITL 2 LIPASES FROM FILAMENTOUS FUNGI 1TIA 18
REMARK 1 REF PROTEIN ENG. V. 7 551 1994 1TIA 19
REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 0859 1TIA 20
REMARK 2 1TIA 21
REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1TIA 22
REMARK 3 1TIA 23
REMARK 3 REFINEMENT. 1TIA 24
REMARK 3 PROGRAM 1 X-PLOR 1TIA 25
REMARK 3 AUTHORS 1 BRUNGER 1TIA 26
REMARK 3 PROGRAM 2 PROLSQ 1TIA 27
REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON 1TIA 28
REMARK 3 R VALUE 0.19 1TIA 29
REMARK 3 RMSD BOND DISTANCES 0.022 ANGSTROMS 1TIA 30
REMARK 3 RMSD BOND ANGLES 4.50 DEGREES 1TIA 31
REMARK 3 1TIA 32
REMARK 3 NUMBER OF REFLECTIONS 12586 1TIA 33
REMARK 3 RESOLUTION RANGE 7.5 - 2.1 ANGSTROMS 1TIA 34
REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1TIA 35
REMARK 3 PERCENT COMPLETION 84.2 1TIA 36
REMARK 3 1TIA 37
REMARK 3 NUMBER OF PROTEIN ATOMS 2069 1TIA 38
REMARK 3 NUMBER OF NUCLEIC ACID ATOMS 0 1TIA 39
REMARK 3 NUMBER OF SOLVENT ATOMS 276 1TIA 40
REMARK 3 1TIA 41
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1TIA 42
REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1TIA 43
REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1TIA 44
REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1TIA 45
REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1TIA 46
REMARK 3 BOND DISTANCE 0.019(0.015) 1TIA 47
REMARK 3 ANGLE DISTANCE 0.061(0.030) 1TIA 48
REMARK 3 PLANAR 1-4 DISTANCE 0.052(0.030) 1TIA 49
REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.017(0.015) 1TIA 50
REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.116(0.060) 1TIA 51
REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1TIA 52
REMARK 3 SINGLE TORSION CONTACT 0.125(0.150) 1TIA 53
REMARK 3 MULTIPLE TORSION CONTACT 0.205(0.150) 1TIA 54
REMARK 3 POSSIBLE HYDROGEN BOND 0.159(0.150) 1TIA 55
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1TIA 56
REMARK 3 PLANAR 2.900(5.000) 1TIA 57
REMARK 3 STAGGERED 17.8(15.0) 1TIA 58
REMARK 3 ORTHONORMAL 28.3(25.0) 1TIA 59
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1TIA 60
REMARK 3 MAIN-CHAIN BOND 1.413(2.000) 1TIA 61
REMARK 3 MAIN-CHAIN ANGLE 2.052(2.500) 1TIA 62
REMARK 3 SIDE-CHAIN BOND 2.504(2.500) 1TIA 63
REMARK 3 SIDE-CHAIN ANGLE 3.734(4.000) 1TIA 64
REMARK 4 1TIA 65
REMARK 4 THE COORDINATES PRESENTED IN THIS ENTRY ARE PRELIMINARY AND 1TIA 66
REMARK 4 CONSIST OF ALPHA CARBON COORDINATES PLUS THE COORDINATES 1TIA 67
REMARK 4 FOR THE CATALYTIC AMINO ACIDS. 1TIA 68
REMARK 5 1TIA 69
REMARK 5 CROSS REFERENCE TO SEQUENCE DATABASE 1TIA 70
REMARK 5 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1TIA 71
REMARK 5 MDLA_PENCA 1TIA 72
SEQRES 1 279 ASP VAL SER THR SER GLU LEU ASP GLN PHE GLU PHE TRP 1TIA 73
SEQRES 2 279 VAL GLN TYR ALA ALA ALA SER TYR TYR GLU ALA ASP TYR 1TIA 74
SEQRES 3 279 THR ALA GLN VAL GLY ASP LYS LEU SER CYS SER LYS GLY 1TIA 75
SEQRES 4 279 ASN CYS PRO GLU VAL GLU ALA THR GLY ALA THR VAL SER 1TIA 76
SEQRES 5 279 TYR ASP PHE SER ASP SER THR ILE THR ASP THR ALA GLY 1TIA 77
SEQRES 6 279 TYR ILE ALA VAL ASP HIS THR ASN SER ALA VAL VAL LEU 1TIA 78
SEQRES 7 279 ALA PHE ARG GLY SER TYR SER VAL ARG ASN TRP VAL ALA 1TIA 79
SEQRES 8 279 ASP ALA THR PHE VAL HIS THR ASN PRO GLY LEU CYS ASP 1TIA 80
SEQRES 9 279 GLY CYS LEU ALA GLU LEU GLY PHE TRP SER SER TRP LYS 1TIA 81
SEQRES 10 279 LEU VAL ARG ASP ASP ILE ILE LYS GLU LEU LYS GLU VAL 1TIA 82
SEQRES 11 279 VAL ALA GLN ASN PRO ASN TYR GLU LEU VAL VAL VAL GLY 1TIA 83
SEQRES 12 279 HIS SER LEU GLY ALA ALA VAL ALA THR LEU ALA ALA THR 1TIA 84
SEQRES 13 279 ASP LEU ARG GLY LYS GLY TYR PRO SER ALA LYS LEU TYR 1TIA 85
SEQRES 14 279 ALA TYR ALA SER PRO ARG VAL GLY ASN ALA ALA LEU ALA 1TIA 86
SEQRES 15 279 LYS TYR ILE THR ALA GLN GLY ASN ASN PHE ARG PHE THR 1TIA 87
SEQRES 16 279 HIS THR ASN ASP PRO VAL PRO LYS LEU PRO LEU LEU SER 1TIA 88
SEQRES 17 279 MET GLY TYR VAL HIS VAL SER PRO GLU TYR TRP ILE THR 1TIA 89
SEQRES 18 279 SER PRO ASN ASN ALA THR VAL SER THR SER ASP ILE LYS 1TIA 90
SEQRES 19 279 VAL ILE ASP GLY ASP VAL SER PHE ASP GLY ASN THR GLY 1TIA 91
SEQRES 20 279 THR GLY LEU PRO LEU LEU THR ASP PHE GLU ALA HIS ILE 1TIA 92
SEQRES 21 279 TRP TYR PHE VAL GLN VAL ASP ALA GLY LYS GLY PRO GLY 1TIA 93
SEQRES 22 279 LEU PRO PHE LYS ARG VAL 1TIA 94
CRYST1 45.570 47.100 33.500 79.05 112.14 70.28 P 1 1 1TIA 95
ORIGX1 1.000000 0.000000 0.000000 0.00000 1TIA 96
ORIGX2 0.000000 1.000000 0.000000 0.00000 1TIA 97
ORIGX3 0.000000 0.000000 1.000000 0.00000 1TIA 98
SCALE1 0.021944 -0.007866 0.012656 0.00000 1TIA 99
SCALE2 0.000000 0.022554 -0.008806 0.00000 1TIA 100
SCALE3 0.000000 0.000000 0.034596 0.00000 1TIA 101 |