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HEADER HYDROLASE 20-APR-11 3RM3
TITLE CRYSTAL STRUCTURE OF MONOACYLGLYCEROL LIPASE FROM BACILLUS SP. H257
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MGLP;
COMPND 5 EC: 3.1.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 129908;
SOURCE 4 STRAIN: H257;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.RENGACHARI,G.A.BEZERRA,K.GRUBER,M.OBERER
REVDAT 1 02-MAY-12 3RM3 0
JRNL AUTH S.RENGACHARI,G.A.BEZERRA,K.GRUBER,M.OBERER
JRNL TITL STRUCTURE OF MONOACYLGLYCEROL LIPASE FROM BACILLUS SP. H257
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 67516
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.158
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 3417
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 17.7251 - 3.4532 0.98 2690 134 0.1603 0.1777
REMARK 3 2 3.4532 - 2.7442 1.00 2681 146 0.1523 0.1627
REMARK 3 3 2.7442 - 2.3983 1.00 2709 129 0.1455 0.1588
REMARK 3 4 2.3983 - 2.1794 1.00 2675 159 0.1288 0.1352
REMARK 3 5 2.1794 - 2.0235 1.00 2679 140 0.1313 0.1611
REMARK 3 6 2.0235 - 1.9043 1.00 2653 166 0.1288 0.1591
REMARK 3 7 1.9043 - 1.8090 1.00 2680 140 0.1198 0.1432
REMARK 3 8 1.8090 - 1.7303 1.00 2681 133 0.1067 0.1267
REMARK 3 9 1.7303 - 1.6638 1.00 2681 128 0.1019 0.1376
REMARK 3 10 1.6638 - 1.6064 1.00 2679 140 0.0939 0.1323
REMARK 3 11 1.6064 - 1.5562 1.00 2684 139 0.0943 0.1279
REMARK 3 12 1.5562 - 1.5118 1.00 2655 145 0.0972 0.1239
REMARK 3 13 1.5118 - 1.4720 1.00 2653 164 0.0927 0.1502
REMARK 3 14 1.4720 - 1.4361 1.00 2694 131 0.1015 0.1170
REMARK 3 15 1.4361 - 1.4034 1.00 2642 146 0.1087 0.1396
REMARK 3 16 1.4034 - 1.3736 1.00 2665 146 0.1162 0.2045
REMARK 3 17 1.3736 - 1.3461 1.00 2646 157 0.1218 0.1547
REMARK 3 18 1.3461 - 1.3207 1.00 2665 129 0.1228 0.1668
REMARK 3 19 1.3207 - 1.2971 1.00 2713 131 0.1374 0.1834
REMARK 3 20 1.2971 - 1.2752 1.00 2627 160 0.1516 0.1713
REMARK 3 21 1.2752 - 1.2546 0.99 2658 147 0.1560 0.1889
REMARK 3 22 1.2546 - 1.2353 1.00 2687 124 0.1792 0.2064
REMARK 3 23 1.2353 - 1.2171 0.99 2649 128 0.1926 0.2042
REMARK 3 24 1.2171 - 1.2000 1.00 2653 155 0.2152 0.2345
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.45
REMARK 3 B_SOL : 82.85
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.890
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04770
REMARK 3 B22 (A**2) : 0.02210
REMARK 3 B33 (A**2) : -0.06970
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02260
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1997
REMARK 3 ANGLE : 1.191 2727
REMARK 3 CHIRALITY : 0.075 307
REMARK 3 PLANARITY : 0.007 353
REMARK 3 DIHEDRAL : 11.810 735
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RM3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB065099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : BARTELS MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67545
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 40.566
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.34600
REMARK 200 R SYM FOR SHELL (I) : 0.34600
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 1R1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES/IMIDAZOLE PH 6.5, 12.5% W/V
REMARK 280 PEG 1000, 12.5% W/V PEG 3350, 12.5% V/V MPD, AND 0.02 M OF
REMARK 280 MONOSACCHARIDES (D-GLUCOSE, D-MANNOSE, D-GALACTOSE, L-FUCTOSE, D-
REMARK 280 XYLOSE, AND N-ACETYL-D-GLUCOSAMINE), VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 35.60500
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 GLY A 135
REMARK 465 GLY A 136
REMARK 465 GLU A 137
REMARK 465 GLY A 250
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 LYS A 155 CD CE NZ
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 18 -117.03 -130.21
REMARK 500 THR A 30 -3.16 68.73
REMARK 500 THR A 60 -81.54 -125.19
REMARK 500 SER A 97 -122.79 65.32
REMARK 500 MET A 132 -167.78 -73.48
REMARK 500 THR A 133 169.45 63.50
REMARK 500 TYR A 225 -149.01 -101.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 624 DISTANCE = 6.37 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RLI RELATED DB: PDB
DBREF 3RM3 A 1 250 UNP P82597 MGLP_BAC25 1 250
SEQADV 3RM3 MET A -19 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 GLY A -18 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 SER A -17 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 SER A -16 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A -15 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A -14 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A -13 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A -12 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A -11 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A -10 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 SER A -9 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 SER A -8 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 GLY A -7 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 LEU A -6 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 VAL A -5 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 PRO A -4 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 ARG A -3 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 GLY A -2 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 SER A -1 UNP P82597 EXPRESSION TAG
SEQADV 3RM3 HIS A 0 UNP P82597 EXPRESSION TAG
SEQRES 1 A 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 270 LEU VAL PRO ARG GLY SER HIS MET SER GLU GLN TYR PRO
SEQRES 3 A 270 VAL LEU SER GLY ALA GLU PRO PHE TYR ALA GLU ASN GLY
SEQRES 4 A 270 PRO VAL GLY VAL LEU LEU VAL HIS GLY PHE THR GLY THR
SEQRES 5 A 270 PRO HIS SER MET ARG PRO LEU ALA GLU ALA TYR ALA LYS
SEQRES 6 A 270 ALA GLY TYR THR VAL CYS LEU PRO ARG LEU LYS GLY HIS
SEQRES 7 A 270 GLY THR HIS TYR GLU ASP MET GLU ARG THR THR PHE HIS
SEQRES 8 A 270 ASP TRP VAL ALA SER VAL GLU GLU GLY TYR GLY TRP LEU
SEQRES 9 A 270 LYS GLN ARG CYS GLN THR ILE PHE VAL THR GLY LEU SER
SEQRES 10 A 270 MET GLY GLY THR LEU THR LEU TYR LEU ALA GLU HIS HIS
SEQRES 11 A 270 PRO ASP ILE CYS GLY ILE VAL PRO ILE ASN ALA ALA VAL
SEQRES 12 A 270 ASP ILE PRO ALA ILE ALA ALA GLY MET THR GLY GLY GLY
SEQRES 13 A 270 GLU LEU PRO ARG TYR LEU ASP SER ILE GLY SER ASP LEU
SEQRES 14 A 270 LYS ASN PRO ASP VAL LYS GLU LEU ALA TYR GLU LYS THR
SEQRES 15 A 270 PRO THR ALA SER LEU LEU GLN LEU ALA ARG LEU MET ALA
SEQRES 16 A 270 GLN THR LYS ALA LYS LEU ASP ARG ILE VAL CYS PRO ALA
SEQRES 17 A 270 LEU ILE PHE VAL SER ASP GLU ASP HIS VAL VAL PRO PRO
SEQRES 18 A 270 GLY ASN ALA ASP ILE ILE PHE GLN GLY ILE SER SER THR
SEQRES 19 A 270 GLU LYS GLU ILE VAL ARG LEU ARG ASN SER TYR HIS VAL
SEQRES 20 A 270 ALA THR LEU ASP TYR ASP GLN PRO MET ILE ILE GLU ARG
SEQRES 21 A 270 SER LEU GLU PHE PHE ALA LYS HIS ALA GLY
HET MRD A 301 8
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 2 MRD C6 H14 O2
FORMUL 3 HOH *234(H2 O)
HELIX 1 1 THR A 32 SER A 35 5 4
HELIX 2 2 MET A 36 ALA A 46 1 11
HELIX 3 3 HIS A 61 ARG A 67 1 7
HELIX 4 4 THR A 69 GLN A 86 1 18
HELIX 5 5 SER A 97 HIS A 110 1 14
HELIX 6 6 ILE A 125 MET A 132 1 8
HELIX 7 7 THR A 164 LYS A 180 1 17
HELIX 8 8 LEU A 181 ILE A 184 5 4
HELIX 9 9 GLY A 202 ILE A 211 1 10
HELIX 10 10 VAL A 227 ASP A 231 5 5
HELIX 11 11 ASP A 233 ALA A 249 1 17
SHEET 1 A 5 PHE A 14 ALA A 16 0
SHEET 2 A 5 THR A 49 LEU A 52 -1 O LEU A 52 N PHE A 14
SHEET 3 A 5 VAL A 21 VAL A 26 1 N LEU A 25 O CYS A 51
SHEET 4 A 5 THR A 90 LEU A 96 1 O THR A 90 N GLY A 22
SHEET 5 A 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
SHEET 1 B 2 TYR A 141 ASP A 143 0
SHEET 2 B 2 LYS A 161 PRO A 163 -1 O THR A 162 N LEU A 142
SHEET 1 C 2 ALA A 188 SER A 193 0
SHEET 2 C 2 LYS A 216 LEU A 221 1 O LEU A 221 N VAL A 192
SITE 1 AC1 3 VAL A 21 ALA A 46 HOH A 411
CRYST1 38.150 71.210 43.660 90.00 111.70 90.00 P 1 21 1 2
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 0.026212 0.000000 0.010431 0.00000
SCALE2 0.000000 0.014043 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024651 0.00000
TER 1938 ALA A 249
MASTER 291 0 1 11 9 0 1 6 2142 1 8 21
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