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HEADER HYDROLASE 22-JUL-15 5CRI
TITLE WILD-TYPE BACILLUS SUBTILIS LIPASE A WITH 0% [BMIM][CL]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIPASE,LIPASE A;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: LIPA, QX56_01625;
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: PET21B
KEYWDS WILD-TYPE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR
REVDAT 1 04-NOV-15 5CRI 0
JRNL AUTH E.M.NORDWALD,J.G.PLAKS,J.R.SNELL,M.C.SOUSA,J.L.KAAR
JRNL TITL CRYSTALLOGRAPHIC INVESTIGATION OF IMIDAZOLIUM IONIC LIQUID
JRNL TITL 2 EFFECTS ON ENZYME STRUCTURE.
JRNL REF CHEMBIOCHEM 2015
JRNL REFN ESSN 1439-7633
JRNL PMID 26388426
JRNL DOI 10.1002/CBIC.201500398
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 38497
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.130
REMARK 3 R VALUE (WORKING SET) : 0.128
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1970
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 24.4238 - 3.9241 0.99 2823 153 0.1496 0.1468
REMARK 3 2 3.9241 - 3.1167 1.00 2743 147 0.1309 0.1677
REMARK 3 3 3.1167 - 2.7233 0.99 2690 145 0.1343 0.1609
REMARK 3 4 2.7233 - 2.4746 0.99 2638 142 0.1244 0.1587
REMARK 3 5 2.4746 - 2.2974 1.00 2653 142 0.1144 0.1436
REMARK 3 6 2.2974 - 2.1620 0.99 2645 142 0.1169 0.1471
REMARK 3 7 2.1620 - 2.0538 0.99 2639 143 0.1137 0.1670
REMARK 3 8 2.0538 - 1.9644 0.99 2590 141 0.1159 0.1663
REMARK 3 9 1.9644 - 1.8888 0.98 2609 141 0.1217 0.1851
REMARK 3 10 1.8888 - 1.8237 0.97 2573 138 0.1247 0.1927
REMARK 3 11 1.8237 - 1.7667 0.96 2495 135 0.1276 0.1924
REMARK 3 12 1.7667 - 1.7162 0.96 2524 134 0.1119 0.1978
REMARK 3 13 1.7162 - 1.6710 0.95 2516 134 0.1115 0.1888
REMARK 3 14 1.6710 - 1.6302 0.92 2389 133 0.1275 0.2122
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.950
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) : 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 : 0.010 2770
REMARK 3 ANGLE : 1.274 3754
REMARK 3 CHIRALITY : 0.074 416
REMARK 3 PLANARITY : 0.006 482
REMARK 3 DIHEDRAL : 12.805 976
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 5CRI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39315
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.630
REMARK 200 RESOLUTION RANGE LOW (A) : 30.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.20500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
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 (%): 38.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35 % PEG 3350, 0.1M ETHANOLAMINE, 20
REMARK 280 MM NASO4, 10 MM ZNCL2, PH 9.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 19.62700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.57500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.31100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.57500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.62700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.31100
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 ALA A 1
REMARK 465 GLU A 2
REMARK 465 ALA B 1
REMARK 465 GLU B 2
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 HG SER B 131 HD1 HIS B 152 1.35
REMARK 500 HZ2 LYS A 88 O HOH A 302 1.57
REMARK 500 HZ2 LYS A 122 O ASN A 181 1.59
REMARK 500 OE1 GLU A 65 O HOH A 301 1.88
REMARK 500 O HOH B 303 O HOH B 500 1.89
REMARK 500 O HOH A 484 O HOH A 519 1.92
REMARK 500 O HOH B 390 O HOH B 478 1.93
REMARK 500 O HOH B 496 O HOH B 517 1.95
REMARK 500 OH TYR B 49 O HOH B 301 1.97
REMARK 500 O HOH A 351 O HOH A 492 1.99
REMARK 500 O HOH A 359 O HOH A 450 1.99
REMARK 500 OH TYR B 161 O HOH B 302 2.04
REMARK 500 O HOH B 377 O HOH B 467 2.05
REMARK 500 O HOH B 473 O HOH B 511 2.16
REMARK 500 CZ TYR B 49 O HOH B 301 2.16
REMARK 500 O HOH B 342 O HOH B 452 2.16
REMARK 500 O HOH A 349 O HOH A 455 2.18
REMARK 500 O HOH B 302 O HOH B 319 2.18
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 O HOH A 445 O HOH B 381 3544 1.96
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 77 -131.91 63.16
REMARK 500 LEU A 90 -146.75 -109.30
REMARK 500 ALA A 97 -70.89 -106.44
REMARK 500 ALA B 15 178.42 172.18
REMARK 500 SER B 77 -127.70 59.69
REMARK 500 LEU B 90 -144.75 -117.87
REMARK 500 ALA B 97 -65.38 -102.59
REMARK 500 GLN B 121 117.11 -162.31
REMARK 500 TYR B 161 45.63 -140.96
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 531 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 542 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH B 543 DISTANCE = 6.79 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 201
DBREF 5CRI A 1 181 UNP I6V559 I6V559_BACIU 32 212
DBREF 5CRI B 1 181 UNP I6V559 I6V559_BACIU 32 212
SEQRES 1 A 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 A 181 GLY ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU
SEQRES 3 A 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 A 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 A 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 A 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 A 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP
SEQRES 8 A 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 A 181 ALA ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR
SEQRES 10 A 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 A 181 SER ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 A 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 A 181 ILE GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE
SEQRES 14 A 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 B 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 B 181 GLY ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU
SEQRES 3 B 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 B 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 B 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 B 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 B 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP
SEQRES 8 B 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 B 181 ALA ASN ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR
SEQRES 10 B 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 B 181 SER ALA ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 B 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 B 181 ILE GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE
SEQRES 14 B 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
HET SO4 A 201 5
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 A 204 5
HET SO4 B 201 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 HOH *474(H2 O)
HELIX 1 AA1 ALA A 15 ASN A 18 5 4
HELIX 2 AA2 PHE A 19 GLN A 29 1 11
HELIX 3 AA3 SER A 32 ASP A 34 5 3
HELIX 4 AA4 THR A 47 GLY A 67 1 21
HELIX 5 AA5 MET A 78 LEU A 90 1 13
HELIX 6 AA6 ASP A 91 ASN A 94 5 4
HELIX 7 AA7 ALA A 105 THR A 109 5 5
HELIX 8 AA8 MET A 137 ARG A 142 1 6
HELIX 9 AA9 ILE A 157 TYR A 161 5 5
HELIX 10 AB1 SER A 162 ASN A 174 1 13
HELIX 11 AB2 ALA B 15 ASN B 18 5 4
HELIX 12 AB3 PHE B 19 GLN B 29 1 11
HELIX 13 AB4 SER B 32 ASP B 34 5 3
HELIX 14 AB5 THR B 47 GLY B 67 1 21
HELIX 15 AB6 MET B 78 LEU B 90 1 13
HELIX 16 AB7 ASP B 91 ASN B 94 5 4
HELIX 17 AB8 ALA B 105 THR B 109 5 5
HELIX 18 AB9 MET B 137 ARG B 142 1 6
HELIX 19 AC1 HIS B 156 TYR B 161 5 6
HELIX 20 AC2 SER B 162 ASN B 174 1 13
SHEET 1 AA1 6 LEU A 36 ALA A 38 0
SHEET 2 AA1 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 AA1 6 VAL A 71 HIS A 76 1 O ASP A 72 N VAL A 7
SHEET 4 AA1 6 VAL A 96 LEU A 102 1 O ALA A 97 N VAL A 71
SHEET 5 AA1 6 LEU A 124 SER A 130 1 O ILE A 128 N THR A 101
SHEET 6 AA1 6 ARG A 147 ILE A 151 1 O VAL A 149 N SER A 127
SHEET 1 AA2 6 LEU B 36 ALA B 38 0
SHEET 2 AA2 6 VAL B 6 VAL B 9 1 N MET B 8 O TYR B 37
SHEET 3 AA2 6 VAL B 71 HIS B 76 1 O ASP B 72 N VAL B 7
SHEET 4 AA2 6 VAL B 96 LEU B 102 1 O VAL B 100 N ILE B 73
SHEET 5 AA2 6 LEU B 124 SER B 130 1 O ILE B 128 N THR B 101
SHEET 6 AA2 6 ARG B 147 ILE B 151 1 O VAL B 149 N SER B 127
SITE 1 AC1 4 VAL A 154 SER A 162 SER A 163 GLN A 164
SITE 1 AC2 9 ARG A 142 HOH A 304 HOH A 355 HOH A 398
SITE 2 AC2 9 HOH A 441 HOH A 446 ARG B 33 MET B 137
SITE 3 AC2 9 TYR B 139
SITE 1 AC3 8 LYS A 122 GLY A 155 HIS A 156 ILE A 157
SITE 2 AC3 8 GLY A 158 ASN A 181 HOH A 330 HOH A 351
SITE 1 AC4 7 ASN A 50 HOH A 314 HOH A 323 HOH A 449
SITE 2 AC4 7 SER B 162 SER B 163 HOH B 331
SITE 1 AC5 8 TYR B 129 ARG B 142 GLN B 150 HOH B 305
SITE 2 AC5 8 HOH B 327 HOH B 383 HOH B 393 HOH B 411
CRYST1 39.254 82.622 95.150 90.00 90.00 90.00 P 21 21 21 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 0.025475 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010510 0.00000
TER 2698 ASN A 181
TER 5396 ASN B 181
MASTER 327 0 5 20 12 0 10 6 3199 2 25 28
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