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HEADER HYDROLASE 31-MAR-14 4Q05
TITLE CRYSTAL STRUCTURE OF AN ESTERASE E25
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE E25;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.Y.LI,C.Y.LI,Y.Z.ZHANG
REVDAT 1 04-JUN-14 4Q05 0
JRNL AUTH P.Y.LI,P.JI,C.Y.LI,Y.ZHANG,G.L.WANG,X.Y.ZHANG,B.B.XIE,
JRNL AUTH 2 Q.L.QIN,X.L.CHEN,B.C.ZHOU,Y.Z.ZHANG
JRNL TITL STRUCTURAL BASIS FOR DIMERIZATION AND CATALYSIS OF A NOVEL
JRNL TITL 2 ESTERASE FROM THE GTSAG MOTIF SUBFAMILY OF BACTERIAL
JRNL TITL 3 HORMONE-SENSITIVE LIPASE (HSL) FAMILY
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
JRNL DOI 10.1074/JBC.M114.574913
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : OVERALL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 64693
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3283
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 19.8075 - 5.7782 1.00 2737 163 0.1468 0.1546
REMARK 3 2 5.7782 - 4.6053 1.00 2730 150 0.1353 0.1502
REMARK 3 3 4.6053 - 4.0287 1.00 2771 134 0.1281 0.1324
REMARK 3 4 4.0287 - 3.6629 0.98 2692 148 0.1432 0.1695
REMARK 3 5 3.6629 - 3.4018 0.97 2658 138 0.1521 0.1677
REMARK 3 6 3.4018 - 3.2021 0.96 2622 154 0.1637 0.1991
REMARK 3 7 3.2021 - 3.0423 0.96 2675 136 0.1696 0.1823
REMARK 3 8 3.0423 - 2.9103 0.96 2627 143 0.1870 0.2181
REMARK 3 9 2.9103 - 2.7986 0.95 2629 135 0.1932 0.2016
REMARK 3 10 2.7986 - 2.7023 0.97 2641 158 0.1941 0.1961
REMARK 3 11 2.7023 - 2.6180 0.96 2627 149 0.1966 0.2256
REMARK 3 12 2.6180 - 2.5433 0.96 2651 150 0.1981 0.2428
REMARK 3 13 2.5433 - 2.4765 0.97 2631 138 0.1969 0.2229
REMARK 3 14 2.4765 - 2.4162 0.96 2708 127 0.2015 0.2153
REMARK 3 15 2.4162 - 2.3613 0.97 2618 129 0.1945 0.2005
REMARK 3 16 2.3613 - 2.3112 0.96 2687 139 0.1903 0.2738
REMARK 3 17 2.3112 - 2.2650 0.96 2649 131 0.2031 0.2470
REMARK 3 18 2.2650 - 2.2223 0.98 2703 146 0.1996 0.2970
REMARK 3 19 2.2223 - 2.1827 0.96 2653 146 0.2071 0.2476
REMARK 3 20 2.1827 - 2.1457 0.99 2696 151 0.2104 0.2577
REMARK 3 21 2.1457 - 2.1111 0.96 2653 139 0.2141 0.2786
REMARK 3 22 2.1111 - 2.0787 0.98 2676 139 0.2099 0.2623
REMARK 3 23 2.0787 - 2.0500 0.98 2676 140 0.2242 0.2424
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 36.82
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.390
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) : -0.05110
REMARK 3 B22 (A**2) : -0.05110
REMARK 3 B33 (A**2) : 0.10230
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.00000
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 5141
REMARK 3 ANGLE : 1.037 7025
REMARK 3 CHIRALITY : 0.067 815
REMARK 3 PLANARITY : 0.005 920
REMARK 3 DIHEDRAL : 11.142 1869
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 4Q05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : SSRF BEAMLINE BL17U
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64925
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: SEMET DERIVATIVES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE TRIHYDRATE, 0.1M
REMARK 280 SODIUM CACODYLATE TRIHYDRATE, 17% PEG8,000, PH 6.5, EVAPORATION,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 16.41567
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 32.83133
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 MET A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 GLN A 4
REMARK 465 ASN A 5
REMARK 465 GLU A 6
REMARK 465 SER A 7
REMARK 465 ALA A 8
REMARK 465 ASN A 9
REMARK 465 SER A 10
REMARK 465 LYS A 11
REMARK 465 THR A 12
REMARK 465 GLN A 13
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASN B 3
REMARK 465 GLN B 4
REMARK 465 ASN B 5
REMARK 465 GLU B 6
REMARK 465 SER B 7
REMARK 465 ALA B 8
REMARK 465 ASN B 9
REMARK 465 SER B 10
REMARK 465 LYS B 11
REMARK 465 THR B 12
REMARK 465 GLN B 13
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 A 780 O HOH A 785 1.94
REMARK 500 O HOH B 706 O HOH B 712 1.95
REMARK 500 O HOH A 772 O HOH B 643 1.97
REMARK 500 O HOH A 724 O HOH A 733 2.00
REMARK 500 O HOH A 744 O HOH A 747 2.03
REMARK 500 OE1 GLN A 169 O HOH A 741 2.06
REMARK 500 O HOH B 657 O HOH B 739 2.06
REMARK 500 O HOH A 708 O HOH B 643 2.09
REMARK 500 ND1 HIS B 170 O HOH B 733 2.10
REMARK 500 O HOH A 770 O HOH A 775 2.10
REMARK 500 O HOH A 683 O HOH A 722 2.13
REMARK 500 O HOH A 754 O HOH A 756 2.14
REMARK 500 O HOH A 681 O HOH A 776 2.16
REMARK 500 O HOH B 650 O HOH B 698 2.17
REMARK 500 O HOH B 770 O HOH B 786 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 PHE A 121 -13.61 73.80
REMARK 500 PRO A 158 34.78 -96.28
REMARK 500 SER A 186 -122.36 45.56
REMARK 500 THR A 214 59.33 30.47
REMARK 500 VAL A 237 -58.08 63.16
REMARK 500 THR A 278 -163.44 -160.62
REMARK 500 PHE B 121 -10.00 68.04
REMARK 500 PRO B 158 37.55 -97.67
REMARK 500 SER B 186 -123.30 44.76
REMARK 500 THR B 214 49.09 32.92
REMARK 500 VAL B 237 -53.81 62.44
REMARK 500 THR B 278 -166.02 -160.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 149 O
REMARK 620 2 ASP B 148 OD1 98.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 123 O
REMARK 620 2 GLY B 118 O 82.8
REMARK 620 3 HOH B 555 O 140.7 90.5
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT
REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION.
REMARK 999 AUTHORS STATE THAT THE GENEBANK ACCESSION NUMBER IS KJ624992 FOR
REMARK 999 THIS SEQUENCE.
DBREF 4Q05 A -19 340 PDB 4Q05 4Q05 -19 340
DBREF 4Q05 B -19 340 PDB 4Q05 4Q05 -19 340
SEQRES 1 A 360 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 360 LEU VAL PRO ARG GLY SER HIS MET THR ASN GLN ASN GLU
SEQRES 3 A 360 SER ALA ASN SER LYS THR GLN GLU ASN SER TRP GLN ILE
SEQRES 4 A 360 GLY PRO ARG THR LEU PRO ALA PRO SER GLY ALA SER ASP
SEQRES 5 A 360 VAL LEU TYR ASN ILE ILE SER LYS THR PRO THR PRO VAL
SEQRES 6 A 360 PRO THR ILE ASN LEU ASN LEU VAL PRO ARG THR GLU SER
SEQRES 7 A 360 GLU TRP ARG ALA ALA ILE THR GLN LEU ASP GLU GLY LYS
SEQRES 8 A 360 VAL ASP MET ALA ARG GLU ILE SER LYS GLN LEU SER VAL
SEQRES 9 A 360 SER VAL GLU HIS GLY VAL ILE GLU GLY VAL SER VAL TYR
SEQRES 10 A 360 TYR VAL THR PRO VAL GLU VAL ALA PRO ASP LEU GLU ASP
SEQRES 11 A 360 LYS LEU PHE VAL HIS THR HIS GLY GLY ALA PHE VAL LEU
SEQRES 12 A 360 ASN GLY GLY GLU ALA GLY THR ILE GLU ALA ILE VAL ILE
SEQRES 13 A 360 ALA THR LEU ALA LYS VAL ARG VAL LEU SER ILE ASP TYR
SEQRES 14 A 360 ARG MET PRO PRO SER HIS PRO ALA PRO ALA ALA ARG ASP
SEQRES 15 A 360 ASP VAL PHE THR VAL TYR GLN HIS LEU LEU LYS GLN GLY
SEQRES 16 A 360 SER ALA GLN LYS ILE ALA LEU GLY GLY SER SER GLY GLY
SEQRES 17 A 360 ALA ASN LEU THR MET GLY LEU VAL GLN HIS LEU ILE GLU
SEQRES 18 A 360 GLN GLU VAL ASP LEU PRO GLY ALA LEU PHE LEU GLY THR
SEQRES 19 A 360 PRO GLY ALA ASP MET SER LYS THR GLY ASP SER TYR TYR
SEQRES 20 A 360 ILE ASN ASP GLY ILE ASP ARG ASN LEU VAL THR TYR ASP
SEQRES 21 A 360 GLY PHE LEU GLU ALA ALA VAL ARG LEU TYR ALA ASN GLY
SEQRES 22 A 360 ARG ASP LEU LYS ASP PRO LEU VAL SER PRO LEU TYR GLY
SEQRES 23 A 360 ASP LEU HIS GLY PHE PRO PRO THR PHE LEU ILE THR GLY
SEQRES 24 A 360 THR ARG ASP LEU LEU LEU SER ALA THR VAL ARG THR HIS
SEQRES 25 A 360 ILE LYS LEU ARG GLN SER GLY VAL VAL ALA ASP LEU PHE
SEQRES 26 A 360 VAL TYR GLU GLY ILE ALA HIS GLY ASP TYR ALA VAL ASP
SEQRES 27 A 360 LEU THR ALA PRO GLU THR GLN HIS ALA PHE ALA GLU LEU
SEQRES 28 A 360 ASN ALA PHE LEU LEU GLN HIS LEU ARG
SEQRES 1 B 360 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 360 LEU VAL PRO ARG GLY SER HIS MET THR ASN GLN ASN GLU
SEQRES 3 B 360 SER ALA ASN SER LYS THR GLN GLU ASN SER TRP GLN ILE
SEQRES 4 B 360 GLY PRO ARG THR LEU PRO ALA PRO SER GLY ALA SER ASP
SEQRES 5 B 360 VAL LEU TYR ASN ILE ILE SER LYS THR PRO THR PRO VAL
SEQRES 6 B 360 PRO THR ILE ASN LEU ASN LEU VAL PRO ARG THR GLU SER
SEQRES 7 B 360 GLU TRP ARG ALA ALA ILE THR GLN LEU ASP GLU GLY LYS
SEQRES 8 B 360 VAL ASP MET ALA ARG GLU ILE SER LYS GLN LEU SER VAL
SEQRES 9 B 360 SER VAL GLU HIS GLY VAL ILE GLU GLY VAL SER VAL TYR
SEQRES 10 B 360 TYR VAL THR PRO VAL GLU VAL ALA PRO ASP LEU GLU ASP
SEQRES 11 B 360 LYS LEU PHE VAL HIS THR HIS GLY GLY ALA PHE VAL LEU
SEQRES 12 B 360 ASN GLY GLY GLU ALA GLY THR ILE GLU ALA ILE VAL ILE
SEQRES 13 B 360 ALA THR LEU ALA LYS VAL ARG VAL LEU SER ILE ASP TYR
SEQRES 14 B 360 ARG MET PRO PRO SER HIS PRO ALA PRO ALA ALA ARG ASP
SEQRES 15 B 360 ASP VAL PHE THR VAL TYR GLN HIS LEU LEU LYS GLN GLY
SEQRES 16 B 360 SER ALA GLN LYS ILE ALA LEU GLY GLY SER SER GLY GLY
SEQRES 17 B 360 ALA ASN LEU THR MET GLY LEU VAL GLN HIS LEU ILE GLU
SEQRES 18 B 360 GLN GLU VAL ASP LEU PRO GLY ALA LEU PHE LEU GLY THR
SEQRES 19 B 360 PRO GLY ALA ASP MET SER LYS THR GLY ASP SER TYR TYR
SEQRES 20 B 360 ILE ASN ASP GLY ILE ASP ARG ASN LEU VAL THR TYR ASP
SEQRES 21 B 360 GLY PHE LEU GLU ALA ALA VAL ARG LEU TYR ALA ASN GLY
SEQRES 22 B 360 ARG ASP LEU LYS ASP PRO LEU VAL SER PRO LEU TYR GLY
SEQRES 23 B 360 ASP LEU HIS GLY PHE PRO PRO THR PHE LEU ILE THR GLY
SEQRES 24 B 360 THR ARG ASP LEU LEU LEU SER ALA THR VAL ARG THR HIS
SEQRES 25 B 360 ILE LYS LEU ARG GLN SER GLY VAL VAL ALA ASP LEU PHE
SEQRES 26 B 360 VAL TYR GLU GLY ILE ALA HIS GLY ASP TYR ALA VAL ASP
SEQRES 27 B 360 LEU THR ALA PRO GLU THR GLN HIS ALA PHE ALA GLU LEU
SEQRES 28 B 360 ASN ALA PHE LEU LEU GLN HIS LEU ARG
HET NA A 401 1
HET NA B 401 1
HET NA B 402 1
HET NA B 403 1
HETNAM NA SODIUM ION
FORMUL 3 NA 4(NA 1+)
FORMUL 7 HOH *577(H2 O)
HELIX 1 1 SER A 31 LYS A 40 1 10
HELIX 2 2 PRO A 46 LEU A 52 1 7
HELIX 3 3 THR A 56 GLU A 69 1 14
HELIX 4 4 GLY A 70 SER A 83 1 14
HELIX 5 5 ALA A 105 GLU A 109 5 5
HELIX 6 6 GLY A 125 GLY A 129 5 5
HELIX 7 7 THR A 130 LYS A 141 1 12
HELIX 8 8 PRO A 158 GLY A 175 1 18
HELIX 9 9 SER A 176 GLN A 178 5 3
HELIX 10 10 SER A 186 GLN A 202 1 17
HELIX 11 11 GLY A 223 ASN A 229 1 7
HELIX 12 12 GLY A 241 ASN A 252 1 12
HELIX 13 13 SER A 262 GLY A 266 5 5
HELIX 14 14 LEU A 284 SER A 298 1 15
HELIX 15 15 GLY A 313 VAL A 317 5 5
HELIX 16 16 ALA A 321 LEU A 339 1 19
HELIX 17 17 SER B 31 LYS B 40 1 10
HELIX 18 18 PRO B 46 LEU B 52 1 7
HELIX 19 19 THR B 56 GLU B 69 1 14
HELIX 20 20 GLY B 70 SER B 83 1 14
HELIX 21 21 ALA B 105 GLU B 109 5 5
HELIX 22 22 GLY B 125 ALA B 128 5 4
HELIX 23 23 GLY B 129 LYS B 141 1 13
HELIX 24 24 PRO B 158 GLY B 175 1 18
HELIX 25 25 SER B 176 GLN B 178 5 3
HELIX 26 26 SER B 186 GLN B 202 1 17
HELIX 27 27 GLY B 223 ASN B 229 1 7
HELIX 28 28 GLY B 241 ASN B 252 1 12
HELIX 29 29 SER B 262 GLY B 266 5 5
HELIX 30 30 LEU B 284 SER B 298 1 15
HELIX 31 31 GLY B 313 VAL B 317 5 5
HELIX 32 32 ALA B 321 LEU B 339 1 19
SHEET 1 A 2 TRP A 17 ILE A 19 0
SHEET 2 A 2 ARG B 22 LEU B 24 -1 O ARG B 22 N ILE A 19
SHEET 1 B 2 ARG A 22 LEU A 24 0
SHEET 2 B 2 TRP B 17 ILE B 19 -1 O ILE B 19 N ARG A 22
SHEET 1 C 8 SER A 85 ILE A 91 0
SHEET 2 C 8 VAL A 94 THR A 100 -1 O TYR A 98 N GLU A 87
SHEET 3 C 8 VAL A 144 ASP A 148 -1 O VAL A 144 N VAL A 99
SHEET 4 C 8 LEU A 112 THR A 116 1 N HIS A 115 O ILE A 147
SHEET 5 C 8 ILE A 180 SER A 185 1 O ALA A 181 N VAL A 114
SHEET 6 C 8 ALA A 209 PRO A 215 1 O GLY A 213 N GLY A 184
SHEET 7 C 8 THR A 274 GLY A 279 1 O PHE A 275 N LEU A 212
SHEET 8 C 8 ALA A 302 TYR A 307 1 O ASP A 303 N LEU A 276
SHEET 1 D 8 SER B 85 ILE B 91 0
SHEET 2 D 8 VAL B 94 THR B 100 -1 O TYR B 98 N GLU B 87
SHEET 3 D 8 VAL B 144 ASP B 148 -1 O VAL B 144 N VAL B 99
SHEET 4 D 8 LEU B 112 THR B 116 1 N HIS B 115 O ILE B 147
SHEET 5 D 8 ILE B 180 SER B 185 1 O ALA B 181 N VAL B 114
SHEET 6 D 8 ALA B 209 PRO B 215 1 O GLY B 213 N GLY B 184
SHEET 7 D 8 THR B 274 GLY B 279 1 O PHE B 275 N LEU B 212
SHEET 8 D 8 ALA B 302 TYR B 307 1 O ASP B 303 N LEU B 276
LINK O TYR B 149 NA NA B 402 1555 1555 2.73
LINK O LEU B 123 NA NA B 403 1555 1555 2.75
LINK OD1 ASP B 148 NA NA B 402 1555 1555 2.77
LINK O VAL B 306 NA NA A 401 1555 1555 2.88
LINK O VAL A 306 NA NA B 401 1555 1555 2.91
LINK O GLY B 118 NA NA B 403 1555 1555 3.03
LINK NA NA B 403 O HOH B 555 1555 1555 2.79
CISPEP 1 PRO A 152 PRO A 153 0 4.07
CISPEP 2 ALA A 157 PRO A 158 0 3.20
CISPEP 3 PRO B 152 PRO B 153 0 5.26
CISPEP 4 ALA B 157 PRO B 158 0 3.86
SITE 1 AC1 5 VAL A 289 HIS A 292 ILE A 293 LEU A 304
SITE 2 AC1 5 VAL B 306
SITE 1 AC2 5 VAL A 306 VAL B 289 HIS B 292 ILE B 293
SITE 2 AC2 5 LEU B 304
SITE 1 AC3 4 HIS B 117 ASP B 148 TYR B 149 MET B 151
SITE 1 AC4 8 HIS B 117 GLY B 118 GLY B 119 PHE B 121
SITE 2 AC4 8 VAL B 122 LEU B 123 MET B 151 HOH B 555
CRYST1 138.796 138.796 49.247 90.00 90.00 120.00 P 31 6
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 0.007205 0.004160 0.000000 0.00000
SCALE2 0.000000 0.008319 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020306 0.00000
TER 2509 ARG A 340
TER 5026 ARG B 340
MASTER 380 0 4 32 20 0 7 6 5569 2 11 56
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