| 6qe2-pdb | HEADER HYDROLASE 04-JAN-19 6QE2
TITLE CRYSTAL STRUCTURE OF PALEOCOCCUS FERROPHILUS MONOACYLGLYCEROL LIPASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.23;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: HEXA-HISTIDINE TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PALAEOCOCCUS FERROPHILUS;
SOURCE 3 ORGANISM_TAXID: 83868;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET30B
KEYWDS MONOACYLGLYCEROL LIPASE, MONOGLYCERIDE LIPASE, MAGL, MGL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LABAR,M.DEMAREZ,N.BRANDT,J.WOUTERS,F.LEHERTE
REVDAT 1 05-FEB-20 6QE2 0
JRNL AUTH G.LABAR,M.DEMAREZ,N.BRANDT
JRNL TITL CRYSTAL STRUCTURE OF PALEOCOCCUS FERROPHILUS
JRNL TITL 2 MONOACYLGLYCEROL LIPASE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11_2563
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 60415
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3025
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 35.6713 - 4.8885 0.99 2708 143 0.1576 0.1630
REMARK 3 2 4.8885 - 3.8817 1.00 2655 140 0.1392 0.1585
REMARK 3 3 3.8817 - 3.3915 1.00 2639 139 0.1534 0.1638
REMARK 3 4 3.3915 - 3.0816 1.00 2646 139 0.1686 0.1936
REMARK 3 5 3.0816 - 2.8608 0.99 2608 138 0.1772 0.2033
REMARK 3 6 2.8608 - 2.6922 0.99 2633 137 0.1773 0.2101
REMARK 3 7 2.6922 - 2.5574 0.99 2596 138 0.1819 0.2160
REMARK 3 8 2.5574 - 2.4461 1.00 2591 136 0.1735 0.2314
REMARK 3 9 2.4461 - 2.3520 1.00 2646 140 0.1826 0.2306
REMARK 3 10 2.3520 - 2.2708 1.00 2624 138 0.1787 0.1784
REMARK 3 11 2.2708 - 2.1998 1.00 2620 138 0.1844 0.2125
REMARK 3 12 2.1998 - 2.1369 1.00 2622 137 0.1776 0.2144
REMARK 3 13 2.1369 - 2.0807 1.00 2614 138 0.1875 0.2410
REMARK 3 14 2.0807 - 2.0299 1.00 2606 138 0.1898 0.2387
REMARK 3 15 2.0299 - 1.9838 1.00 2620 137 0.1920 0.2617
REMARK 3 16 1.9838 - 1.9416 1.00 2651 139 0.2126 0.2519
REMARK 3 17 1.9416 - 1.9027 1.00 2603 138 0.2124 0.2485
REMARK 3 18 1.9027 - 1.8668 1.00 2611 137 0.2130 0.2627
REMARK 3 19 1.8668 - 1.8335 1.00 2622 139 0.2151 0.2446
REMARK 3 20 1.8335 - 1.8024 1.00 2621 138 0.2337 0.3015
REMARK 3 21 1.8024 - 1.7733 1.00 2619 139 0.2479 0.2764
REMARK 3 22 1.7733 - 1.7461 0.85 2235 119 0.3080 0.3937
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 4218
REMARK 3 ANGLE : 0.914 5696
REMARK 3 CHIRALITY : 0.061 608
REMARK 3 PLANARITY : 0.006 728
REMARK 3 DIHEDRAL : 17.253 1617
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 6QE2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1200013434.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9801
REMARK 200 MONOCHROMATOR : SI[111]
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60488
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.746
REMARK 200 RESOLUTION RANGE LOW (A) : 35.664
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.651
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.53
REMARK 200 R MERGE FOR SHELL (I) : 0.38200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.330
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3HJU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION ( 15 MG/ML IN HEPES
REMARK 280 20 MM PH 8.1, NACL 150 MM, LDAO 0.1 %, GLYCEROL 10% M/M) MIXED
REMARK 280 WITH AN EQUAL VOLUME OF PEG 3350 20 %, POTASSIUM FORMATE 0.2 M,
REMARK 280 MICROBATCH, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 60.30000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.73000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.30000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.73000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ARG A 258
REMARK 465 GLY A 259
REMARK 465 ASP A 260
REMARK 465 LEU A 261
REMARK 465 GLU A 262
REMARK 465 TRP A 263
REMARK 465 ALA A 264
REMARK 465 SER A 265
REMARK 465 ALA A 266
REMARK 465 GLU A 267
REMARK 465 ARG A 268
REMARK 465 ALA A 269
REMARK 465 SER A 270
REMARK 465 SER A 271
REMARK 465 ILE A 272
REMARK 465 MET A 273
REMARK 465 GLY A 274
REMARK 465 ASP A 275
REMARK 465 SER A 276
REMARK 465 ALA A 277
REMARK 465 HIS A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 ARG B 258
REMARK 465 GLY B 259
REMARK 465 ASP B 260
REMARK 465 LEU B 261
REMARK 465 GLU B 262
REMARK 465 TRP B 263
REMARK 465 ALA B 264
REMARK 465 SER B 265
REMARK 465 ALA B 266
REMARK 465 GLU B 267
REMARK 465 ARG B 268
REMARK 465 ALA B 269
REMARK 465 SER B 270
REMARK 465 SER B 271
REMARK 465 ILE B 272
REMARK 465 MET B 273
REMARK 465 GLY B 274
REMARK 465 ASP B 275
REMARK 465 SER B 276
REMARK 465 ALA B 277
REMARK 465 HIS B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 HIS B 282
REMARK 465 HIS B 283
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 B 475 O HOH B 635 1.95
REMARK 500 O HOH B 695 O HOH B 697 1.96
REMARK 500 O HOH B 578 O HOH B 632 2.05
REMARK 500 OD1 ASP A 179 O HOH A 401 2.12
REMARK 500 O HOH B 695 O HOH B 698 2.15
REMARK 500 O HOH B 427 O HOH B 617 2.16
REMARK 500 O HOH B 406 O HOH B 460 2.17
REMARK 500 O HOH B 453 O HOH B 603 2.19
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 GLU A 24 -153.37 -107.23
REMARK 500 THR A 61 -162.65 -167.18
REMARK 500 SER A 87 -118.77 62.77
REMARK 500 TYR A 232 -155.81 -87.44
REMARK 500 GLU B 24 -155.21 -109.22
REMARK 500 THR B 61 -160.67 -171.54
REMARK 500 SER B 87 -114.22 59.03
REMARK 500 TYR B 232 -158.08 -87.41
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 683 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 694 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B 695 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH B 696 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B 697 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH B 698 DISTANCE = 7.65 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LDA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LDA B 302
DBREF 6QE2 A 1 283 PDB 6QE2 6QE2 1 283
DBREF 6QE2 B 1 283 PDB 6QE2 6QE2 1 283
SEQRES 1 A 283 MET GLU LEU TYR ARG ALA LYS PHE GLY THR PRO GLU ARG
SEQRES 2 A 283 GLY TRP VAL VAL LEU VAL HIS GLY LEU GLY GLU HIS SER
SEQRES 3 A 283 GLY ARG TYR GLY LYS LEU ILE GLU LEU LEU ASN GLY ALA
SEQRES 4 A 283 GLY PHE GLY VAL TYR ALA PHE ASP TRP PRO GLY HIS GLY
SEQRES 5 A 283 LYS SER PRO GLY LYS ARG GLY HIS THR SER VAL GLU GLU
SEQRES 6 A 283 ALA MET LYS ILE ILE ASP SER ILE ILE GLU GLU LEU GLY
SEQRES 7 A 283 GLU LYS PRO PHE LEU PHE GLY HIS SER LEU GLY GLY LEU
SEQRES 8 A 283 THR VAL ILE ARG TYR ALA GLU THR ARG PRO ASP LYS ILE
SEQRES 9 A 283 MET GLY VAL VAL ALA SER SER PRO ALA LEU ALA LYS SER
SEQRES 10 A 283 PRO LYS THR PRO SER PHE MET VAL ALA LEU ALA LYS VAL
SEQRES 11 A 283 LEU GLY ARG ILE THR PRO GLY LEU SER LEU SER ASN GLY
SEQRES 12 A 283 LEU ASP PRO LYS LEU LEU SER ARG ASN PRO ASP ALA VAL
SEQRES 13 A 283 LYS ARG TYR ILE GLU ASP PRO LEU VAL HIS ASP ARG ILE
SEQRES 14 A 283 SER GLY LYS LEU GLY MET SER VAL PHE ASP ASN MET GLU
SEQRES 15 A 283 ARG ALA HIS LYS GLU ALA GLU ARG ILE LYS ALA PRO VAL
SEQRES 16 A 283 LEU LEU LEU VAL GLY THR ALA ASP ILE ILE THR PRO PRO
SEQRES 17 A 283 GLU GLY SER ARG ARG LEU PHE GLU GLU LEU LYS VAL LYS
SEQRES 18 A 283 ASP LYS THR ILE MET GLU PHE LYS GLY ALA TYR HIS GLU
SEQRES 19 A 283 ILE PHE GLU ASP PRO GLU TRP GLY GLU GLU PHE HIS ARG
SEQRES 20 A 283 ALA ILE VAL GLU TRP LEU VAL SER HIS SER ARG GLY ASP
SEQRES 21 A 283 LEU GLU TRP ALA SER ALA GLU ARG ALA SER SER ILE MET
SEQRES 22 A 283 GLY ASP SER ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 283 MET GLU LEU TYR ARG ALA LYS PHE GLY THR PRO GLU ARG
SEQRES 2 B 283 GLY TRP VAL VAL LEU VAL HIS GLY LEU GLY GLU HIS SER
SEQRES 3 B 283 GLY ARG TYR GLY LYS LEU ILE GLU LEU LEU ASN GLY ALA
SEQRES 4 B 283 GLY PHE GLY VAL TYR ALA PHE ASP TRP PRO GLY HIS GLY
SEQRES 5 B 283 LYS SER PRO GLY LYS ARG GLY HIS THR SER VAL GLU GLU
SEQRES 6 B 283 ALA MET LYS ILE ILE ASP SER ILE ILE GLU GLU LEU GLY
SEQRES 7 B 283 GLU LYS PRO PHE LEU PHE GLY HIS SER LEU GLY GLY LEU
SEQRES 8 B 283 THR VAL ILE ARG TYR ALA GLU THR ARG PRO ASP LYS ILE
SEQRES 9 B 283 MET GLY VAL VAL ALA SER SER PRO ALA LEU ALA LYS SER
SEQRES 10 B 283 PRO LYS THR PRO SER PHE MET VAL ALA LEU ALA LYS VAL
SEQRES 11 B 283 LEU GLY ARG ILE THR PRO GLY LEU SER LEU SER ASN GLY
SEQRES 12 B 283 LEU ASP PRO LYS LEU LEU SER ARG ASN PRO ASP ALA VAL
SEQRES 13 B 283 LYS ARG TYR ILE GLU ASP PRO LEU VAL HIS ASP ARG ILE
SEQRES 14 B 283 SER GLY LYS LEU GLY MET SER VAL PHE ASP ASN MET GLU
SEQRES 15 B 283 ARG ALA HIS LYS GLU ALA GLU ARG ILE LYS ALA PRO VAL
SEQRES 16 B 283 LEU LEU LEU VAL GLY THR ALA ASP ILE ILE THR PRO PRO
SEQRES 17 B 283 GLU GLY SER ARG ARG LEU PHE GLU GLU LEU LYS VAL LYS
SEQRES 18 B 283 ASP LYS THR ILE MET GLU PHE LYS GLY ALA TYR HIS GLU
SEQRES 19 B 283 ILE PHE GLU ASP PRO GLU TRP GLY GLU GLU PHE HIS ARG
SEQRES 20 B 283 ALA ILE VAL GLU TRP LEU VAL SER HIS SER ARG GLY ASP
SEQRES 21 B 283 LEU GLU TRP ALA SER ALA GLU ARG ALA SER SER ILE MET
SEQRES 22 B 283 GLY ASP SER ALA HIS HIS HIS HIS HIS HIS
HET GOL A 301 6
HET LDA A 302 16
HET GOL B 301 6
HET LDA B 302 16
HETNAM GOL GLYCEROL
HETNAM LDA LAURYL DIMETHYLAMINE-N-OXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 LDA 2(C14 H31 N O)
FORMUL 7 HOH *581(H2 O)
HELIX 1 AA1 HIS A 25 ARG A 28 5 4
HELIX 2 AA2 TYR A 29 ALA A 39 1 11
HELIX 3 AA3 SER A 62 GLY A 78 1 17
HELIX 4 AA4 SER A 87 ARG A 100 1 14
HELIX 5 AA5 PRO A 121 THR A 135 1 15
HELIX 6 AA6 ASP A 145 LEU A 149 5 5
HELIX 7 AA7 ASN A 152 ASP A 162 1 11
HELIX 8 AA8 GLY A 171 GLU A 187 1 17
HELIX 9 AA9 ALA A 188 ILE A 191 5 4
HELIX 10 AB1 PRO A 208 LEU A 218 1 11
HELIX 11 AB2 TRP A 241 SER A 257 1 17
HELIX 12 AB3 HIS B 25 ARG B 28 5 4
HELIX 13 AB4 TYR B 29 ALA B 39 1 11
HELIX 14 AB5 SER B 62 GLY B 78 1 17
HELIX 15 AB6 SER B 87 ARG B 100 1 14
HELIX 16 AB7 PRO B 121 THR B 135 1 15
HELIX 17 AB8 ASP B 145 LEU B 149 5 5
HELIX 18 AB9 ASN B 152 ASP B 162 1 11
HELIX 19 AC1 GLY B 171 GLU B 187 1 17
HELIX 20 AC2 ALA B 188 ILE B 191 5 4
HELIX 21 AC3 PRO B 208 LEU B 218 1 11
HELIX 22 AC4 TRP B 241 SER B 257 1 17
SHEET 1 AA1 7 ARG A 5 PHE A 8 0
SHEET 2 AA1 7 GLY A 42 PHE A 46 -1 O ALA A 45 N ALA A 6
SHEET 3 AA1 7 TRP A 15 VAL A 19 1 N LEU A 18 O TYR A 44
SHEET 4 AA1 7 PHE A 82 HIS A 86 1 O PHE A 82 N TRP A 15
SHEET 5 AA1 7 GLY A 106 SER A 110 1 O SER A 110 N GLY A 85
SHEET 6 AA1 7 VAL A 195 GLY A 200 1 O LEU A 196 N ALA A 109
SHEET 7 AA1 7 LYS A 223 PHE A 228 1 O MET A 226 N LEU A 197
SHEET 1 AA2 2 SER A 139 SER A 141 0
SHEET 2 AA2 2 ARG A 168 SER A 170 -1 O ILE A 169 N LEU A 140
SHEET 1 AA3 7 ARG B 5 PHE B 8 0
SHEET 2 AA3 7 GLY B 42 PHE B 46 -1 O ALA B 45 N ALA B 6
SHEET 3 AA3 7 TRP B 15 VAL B 19 1 N VAL B 16 O TYR B 44
SHEET 4 AA3 7 PHE B 82 HIS B 86 1 O PHE B 82 N TRP B 15
SHEET 5 AA3 7 GLY B 106 SER B 110 1 O SER B 110 N GLY B 85
SHEET 6 AA3 7 VAL B 195 GLY B 200 1 O LEU B 196 N ALA B 109
SHEET 7 AA3 7 LYS B 223 PHE B 228 1 O MET B 226 N LEU B 197
SHEET 1 AA4 2 SER B 139 SER B 141 0
SHEET 2 AA4 2 ARG B 168 SER B 170 -1 O ILE B 169 N LEU B 140
SITE 1 AC1 9 LEU A 22 GLU A 24 HIS A 86 SER A 87
SITE 2 AC1 9 LEU A 149 TYR A 159 HIS A 233 GLU A 234
SITE 3 AC1 9 HOH A 453
SITE 1 AC2 5 SER A 87 LEU A 88 ASN A 142 THR A 206
SITE 2 AC2 5 HOH A 453
SITE 1 AC3 9 LEU B 22 GLU B 24 HIS B 86 SER B 87
SITE 2 AC3 9 LEU B 149 TYR B 159 HIS B 233 GLU B 234
SITE 3 AC3 9 HOH B 472
SITE 1 AC4 9 SER B 87 LEU B 88 LEU B 138 LEU B 140
SITE 2 AC4 9 ASN B 142 ILE B 169 GLY B 171 THR B 206
SITE 3 AC4 9 HOH B 472
CRYST1 120.600 75.460 85.440 90.00 128.29 90.00 C 1 2 1 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 0.008292 0.000000 0.006546 0.00000
SCALE2 0.000000 0.013252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014912 0.00000
TER 2032 SER A 257
TER 4070 SER B 257
MASTER 353 0 4 22 18 0 11 6 4643 2 44 44
END
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