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HEADER HYDROLASE 25-FEB-11 3QVM
TITLE THE STRUCTURE OF OLEI00960, A HYDROLASE FROM OLEISPIRA ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLEI00960;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OLEISPIRA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 188908;
SOURCE 4 GENE: OLEI00960;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TVLIC
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, ALPHA-BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.U.SINGER,O.KAGAN,Y.KIM,A.M.EDWARDS,A.JOACHIMIAK,A.SAVCHENKO,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 13-APR-11 3QVM 0
JRNL AUTH A.U.SINGER,O.KAGAN,Y.KIM,A.M.EDWARDS,A.JOACHIMIAK,
JRNL AUTH 2 A.SAVCHENKO
JRNL TITL THE STRUCTURE OF OLEI00960, A HYDROLASE FROM OLEISPIRA
JRNL TITL 2 ANTARCTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 96971
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3906
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 18.7135 - 5.3827 0.96 4692 193 0.1447 0.1414
REMARK 3 2 5.3827 - 4.2893 0.96 4686 200 0.1098 0.1406
REMARK 3 3 4.2893 - 3.7521 0.96 4701 190 0.1165 0.1263
REMARK 3 4 3.7521 - 3.4113 0.96 4695 194 0.1318 0.1580
REMARK 3 5 3.4113 - 3.1681 0.96 4698 191 0.1495 0.1702
REMARK 3 6 3.1681 - 2.9821 0.96 4708 202 0.1598 0.2001
REMARK 3 7 2.9821 - 2.8333 0.96 4689 202 0.1615 0.1778
REMARK 3 8 2.8333 - 2.7103 0.96 4644 200 0.1520 0.2269
REMARK 3 9 2.7103 - 2.6062 0.96 4701 191 0.1691 0.1968
REMARK 3 10 2.6062 - 2.5165 0.96 4709 187 0.1684 0.1974
REMARK 3 11 2.5165 - 2.4380 0.96 4642 196 0.1691 0.2310
REMARK 3 12 2.4380 - 2.3685 0.96 4638 196 0.1735 0.2461
REMARK 3 13 2.3685 - 2.3062 0.95 4733 206 0.1752 0.1937
REMARK 3 14 2.3062 - 2.2501 0.95 4608 192 0.1824 0.2354
REMARK 3 15 2.2501 - 2.1990 0.95 4679 189 0.1898 0.2258
REMARK 3 16 2.1990 - 2.1523 0.95 4570 196 0.1935 0.1786
REMARK 3 17 2.1523 - 2.1093 0.95 4674 186 0.2011 0.2514
REMARK 3 18 2.1093 - 2.0695 0.94 4550 191 0.2085 0.2435
REMARK 3 19 2.0695 - 2.0326 0.93 4620 193 0.2139 0.2887
REMARK 3 20 2.0326 - 1.9982 0.90 4355 189 0.2210 0.2758
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 : 0.37
REMARK 3 B_SOL : 30.92
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.31060
REMARK 3 B22 (A**2) : -3.31060
REMARK 3 B33 (A**2) : 6.62120
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 4427
REMARK 3 ANGLE : 0.964 6019
REMARK 3 CHIRALITY : 0.069 683
REMARK 3 PLANARITY : 0.004 779
REMARK 3 DIHEDRAL : 17.342 1578
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 3QVM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-09
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 : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50298
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.53100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASER
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: MODEL BASED ON 1WOM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CALCIUM CHLORIDE, 0.1M BIS-TRIS
REMARK 280 PH6.5, 1.6M AMMONIUM SULFATE. CRYOPROTECTED WITH PARATONE-N OIL,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLY A 0
REMARK 465 MSE A 1
REMARK 465 ILE A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 GLN A 278
REMARK 465 THR A 279
REMARK 465 ARG A 280
REMARK 465 ALA A 281
REMARK 465 ARG B 280
REMARK 465 ALA B 281
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 ASP A 5 CG OD1 OD2
REMARK 470 GLU A 10 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 30 N CA C O CB CG1 CG2
REMARK 480 ILE B 243 N CA C O CB CG1 CG2
REMARK 480 ILE B 243 CD1
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 CYS A 38 -169.50 -118.33
REMARK 500 SER A 105 -116.43 53.96
REMARK 500 CYS A 133 130.60 -174.13
REMARK 500 ASN A 160 85.81 -154.04
REMARK 500 ALA A 231 103.29 -163.34
REMARK 500 ASP B 95 66.61 40.00
REMARK 500 SER B 105 -122.31 67.19
REMARK 500 CYS B 133 131.10 -175.97
REMARK 500 ALA B 231 107.21 -161.02
REMARK 500 ASP B 262 41.96 -141.55
REMARK 500 GLN B 278 71.34 122.59
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 284 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 62 O
REMARK 620 2 TYR B 83 OH 104.4
REMARK 620 3 SER B 64 OG 106.7 135.3
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 SO4 A 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 286
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC40628 RELATED DB: TARGETDB
DBREF 3QVM A 0 281 PDB 3QVM 3QVM 0 281
DBREF 3QVM B 0 281 PDB 3QVM 3QVM 0 281
SEQRES 1 A 282 GLY MSE ILE LYS GLN ASP VAL ILE CYS TYR GLU LYS GLU
SEQRES 2 A 282 ASP VAL VAL LYS ARG ASN ASN ILE ASN ILE THR GLY GLY
SEQRES 3 A 282 GLY GLU LYS THR VAL LEU LEU ALA HIS GLY PHE GLY CYS
SEQRES 4 A 282 ASP GLN ASN MSE TRP ARG PHE MSE LEU PRO GLU LEU GLU
SEQRES 5 A 282 LYS GLN PHE THR VAL ILE VAL PHE ASP TYR VAL GLY SER
SEQRES 6 A 282 GLY GLN SER ASP LEU GLU SER PHE SER THR LYS ARG TYR
SEQRES 7 A 282 SER SER LEU GLU GLY TYR ALA LYS ASP VAL GLU GLU ILE
SEQRES 8 A 282 LEU VAL ALA LEU ASP LEU VAL ASN VAL SER ILE ILE GLY
SEQRES 9 A 282 HIS SER VAL SER SER ILE ILE ALA GLY ILE ALA SER THR
SEQRES 10 A 282 HIS VAL GLY ASP ARG ILE SER ASP ILE THR MSE ILE CYS
SEQRES 11 A 282 PRO SER PRO CYS PHE MSE ASN PHE PRO PRO ASP TYR VAL
SEQRES 12 A 282 GLY GLY PHE GLU ARG ASP ASP LEU GLU GLU LEU ILE ASN
SEQRES 13 A 282 LEU MSE ASP LYS ASN TYR ILE GLY TRP ALA ASN TYR LEU
SEQRES 14 A 282 ALA PRO LEU VAL MSE GLY ALA SER HIS SER SER GLU LEU
SEQRES 15 A 282 ILE GLY GLU LEU SER GLY SER PHE CYS THR THR ASP PRO
SEQRES 16 A 282 ILE VAL ALA LYS THR PHE ALA LYS ALA THR PHE PHE SER
SEQRES 17 A 282 ASP TYR ARG SER LEU LEU GLU ASP ILE SER THR PRO ALA
SEQRES 18 A 282 LEU ILE PHE GLN SER ALA LYS ASP SER LEU ALA SER PRO
SEQRES 19 A 282 GLU VAL GLY GLN TYR MSE ALA GLU ASN ILE PRO ASN SER
SEQRES 20 A 282 GLN LEU GLU LEU ILE GLN ALA GLU GLY HIS CYS LEU HIS
SEQRES 21 A 282 MSE THR ASP ALA GLY LEU ILE THR PRO LEU LEU ILE HIS
SEQRES 22 A 282 PHE ILE GLN ASN ASN GLN THR ARG ALA
SEQRES 1 B 282 GLY MSE ILE LYS GLN ASP VAL ILE CYS TYR GLU LYS GLU
SEQRES 2 B 282 ASP VAL VAL LYS ARG ASN ASN ILE ASN ILE THR GLY GLY
SEQRES 3 B 282 GLY GLU LYS THR VAL LEU LEU ALA HIS GLY PHE GLY CYS
SEQRES 4 B 282 ASP GLN ASN MSE TRP ARG PHE MSE LEU PRO GLU LEU GLU
SEQRES 5 B 282 LYS GLN PHE THR VAL ILE VAL PHE ASP TYR VAL GLY SER
SEQRES 6 B 282 GLY GLN SER ASP LEU GLU SER PHE SER THR LYS ARG TYR
SEQRES 7 B 282 SER SER LEU GLU GLY TYR ALA LYS ASP VAL GLU GLU ILE
SEQRES 8 B 282 LEU VAL ALA LEU ASP LEU VAL ASN VAL SER ILE ILE GLY
SEQRES 9 B 282 HIS SER VAL SER SER ILE ILE ALA GLY ILE ALA SER THR
SEQRES 10 B 282 HIS VAL GLY ASP ARG ILE SER ASP ILE THR MSE ILE CYS
SEQRES 11 B 282 PRO SER PRO CYS PHE MSE ASN PHE PRO PRO ASP TYR VAL
SEQRES 12 B 282 GLY GLY PHE GLU ARG ASP ASP LEU GLU GLU LEU ILE ASN
SEQRES 13 B 282 LEU MSE ASP LYS ASN TYR ILE GLY TRP ALA ASN TYR LEU
SEQRES 14 B 282 ALA PRO LEU VAL MSE GLY ALA SER HIS SER SER GLU LEU
SEQRES 15 B 282 ILE GLY GLU LEU SER GLY SER PHE CYS THR THR ASP PRO
SEQRES 16 B 282 ILE VAL ALA LYS THR PHE ALA LYS ALA THR PHE PHE SER
SEQRES 17 B 282 ASP TYR ARG SER LEU LEU GLU ASP ILE SER THR PRO ALA
SEQRES 18 B 282 LEU ILE PHE GLN SER ALA LYS ASP SER LEU ALA SER PRO
SEQRES 19 B 282 GLU VAL GLY GLN TYR MSE ALA GLU ASN ILE PRO ASN SER
SEQRES 20 B 282 GLN LEU GLU LEU ILE GLN ALA GLU GLY HIS CYS LEU HIS
SEQRES 21 B 282 MSE THR ASP ALA GLY LEU ILE THR PRO LEU LEU ILE HIS
SEQRES 22 B 282 PHE ILE GLN ASN ASN GLN THR ARG ALA
MODRES 3QVM MSE A 42 MET SELENOMETHIONINE
MODRES 3QVM MSE A 46 MET SELENOMETHIONINE
MODRES 3QVM MSE A 127 MET SELENOMETHIONINE
MODRES 3QVM MSE A 135 MET SELENOMETHIONINE
MODRES 3QVM MSE A 157 MET SELENOMETHIONINE
MODRES 3QVM MSE A 173 MET SELENOMETHIONINE
MODRES 3QVM MSE A 239 MET SELENOMETHIONINE
MODRES 3QVM MSE A 260 MET SELENOMETHIONINE
MODRES 3QVM MSE B 1 MET SELENOMETHIONINE
MODRES 3QVM MSE B 42 MET SELENOMETHIONINE
MODRES 3QVM MSE B 46 MET SELENOMETHIONINE
MODRES 3QVM MSE B 127 MET SELENOMETHIONINE
MODRES 3QVM MSE B 135 MET SELENOMETHIONINE
MODRES 3QVM MSE B 157 MET SELENOMETHIONINE
MODRES 3QVM MSE B 173 MET SELENOMETHIONINE
MODRES 3QVM MSE B 239 MET SELENOMETHIONINE
MODRES 3QVM MSE B 260 MET SELENOMETHIONINE
HET MSE A 42 8
HET MSE A 46 8
HET MSE A 127 8
HET MSE A 135 8
HET MSE A 157 8
HET MSE A 173 8
HET MSE A 239 8
HET MSE A 260 8
HET MSE B 1 8
HET MSE B 42 8
HET MSE B 46 8
HET MSE B 127 8
HET MSE B 135 8
HET MSE B 157 8
HET MSE B 173 8
HET MSE B 239 8
HET MSE B 260 8
HET SO4 A 282 5
HET SO4 A 283 5
HET SO4 A 284 5
HET NA A 285 1
HET SO4 B 282 5
HET SO4 B 283 5
HET NA B 284 1
HET CL B 285 1
HET CA B 286 1
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
FORMUL 1 MSE 17(C5 H11 N O2 SE)
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 6 NA 2(NA 1+)
FORMUL 10 CL CL 1-
FORMUL 11 CA CA 2+
FORMUL 12 HOH *240(H2 O)
HELIX 1 1 GLU A 10 ASN A 18 1 9
HELIX 2 2 ASP A 39 ARG A 44 5 6
HELIX 3 3 MSE A 46 LYS A 52 1 7
HELIX 4 4 ASP A 68 PHE A 72 5 5
HELIX 5 5 LYS A 75 SER A 78 5 4
HELIX 6 6 SER A 79 LEU A 94 1 16
HELIX 7 7 SER A 105 GLY A 119 1 15
HELIX 8 8 GLU A 146 ASN A 160 1 15
HELIX 9 9 ASN A 160 GLY A 174 1 15
HELIX 10 10 SER A 178 THR A 192 1 15
HELIX 11 11 ASP A 193 PHE A 206 1 14
HELIX 12 12 TYR A 209 ILE A 216 5 8
HELIX 13 13 SER A 232 ILE A 243 1 12
HELIX 14 14 CYS A 257 ASP A 262 1 6
HELIX 15 15 ASP A 262 ASN A 277 1 16
HELIX 16 16 GLU B 10 ASN B 18 1 9
HELIX 17 17 ASP B 39 ARG B 44 5 6
HELIX 18 18 MSE B 46 LYS B 52 1 7
HELIX 19 19 ASP B 68 PHE B 72 5 5
HELIX 20 20 LYS B 75 SER B 78 5 4
HELIX 21 21 SER B 79 LEU B 94 1 16
HELIX 22 22 SER B 105 GLY B 119 1 15
HELIX 23 23 GLU B 146 ASN B 160 1 15
HELIX 24 24 ASN B 160 GLY B 174 1 15
HELIX 25 25 SER B 178 THR B 191 1 14
HELIX 26 26 ASP B 193 PHE B 206 1 14
HELIX 27 27 TYR B 209 ILE B 216 5 8
HELIX 28 28 SER B 232 ILE B 243 1 12
HELIX 29 29 CYS B 257 ASP B 262 1 6
HELIX 30 30 ASP B 262 ASN B 277 1 16
SHEET 1 A 7 ASN A 21 GLY A 24 0
SHEET 2 A 7 THR A 55 VAL A 58 -1 O VAL A 56 N THR A 23
SHEET 3 A 7 THR A 29 ALA A 33 1 N LEU A 32 O ILE A 57
SHEET 4 A 7 VAL A 99 HIS A 104 1 O ILE A 102 N LEU A 31
SHEET 5 A 7 ILE A 122 ILE A 128 1 O THR A 126 N ILE A 101
SHEET 6 A 7 ALA A 220 LYS A 227 1 O LEU A 221 N MSE A 127
SHEET 7 A 7 SER A 246 GLU A 254 1 O ILE A 251 N GLN A 224
SHEET 1 B 2 ASN A 136 PHE A 137 0
SHEET 2 B 2 TYR A 141 VAL A 142 -1 O TYR A 141 N PHE A 137
SHEET 1 C 7 ASN B 21 GLY B 24 0
SHEET 2 C 7 THR B 55 VAL B 58 -1 O VAL B 56 N THR B 23
SHEET 3 C 7 THR B 29 ALA B 33 1 N LEU B 32 O ILE B 57
SHEET 4 C 7 VAL B 99 HIS B 104 1 O ILE B 102 N LEU B 31
SHEET 5 C 7 ILE B 122 ILE B 128 1 O THR B 126 N ILE B 101
SHEET 6 C 7 ALA B 220 LYS B 227 1 O LEU B 221 N MSE B 127
SHEET 7 C 7 SER B 246 GLU B 254 1 O ILE B 251 N GLN B 224
SHEET 1 D 2 ASN B 136 PHE B 137 0
SHEET 2 D 2 TYR B 141 VAL B 142 -1 O TYR B 141 N PHE B 137
LINK C ASN A 41 N MSE A 42 1555 1555 1.33
LINK C MSE A 42 N TRP A 43 1555 1555 1.33
LINK C PHE A 45 N MSE A 46 1555 1555 1.33
LINK C MSE A 46 N LEU A 47 1555 1555 1.33
LINK C THR A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N ILE A 128 1555 1555 1.32
LINK C PHE A 134 N MSE A 135 1555 1555 1.33
LINK C MSE A 135 N ASN A 136 1555 1555 1.33
LINK C LEU A 156 N MSE A 157 1555 1555 1.33
LINK C MSE A 157 N ASP A 158 1555 1555 1.33
LINK C VAL A 172 N MSE A 173 1555 1555 1.33
LINK C MSE A 173 N GLY A 174 1555 1555 1.33
LINK C TYR A 238 N MSE A 239 1555 1555 1.33
LINK C MSE A 239 N ALA A 240 1555 1555 1.33
LINK C HIS A 259 N MSE A 260 1555 1555 1.33
LINK C MSE A 260 N THR A 261 1555 1555 1.33
LINK C GLY B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N ILE B 2 1555 1555 1.33
LINK C ASN B 41 N MSE B 42 1555 1555 1.33
LINK C MSE B 42 N TRP B 43 1555 1555 1.33
LINK C PHE B 45 N MSE B 46 1555 1555 1.34
LINK C MSE B 46 N LEU B 47 1555 1555 1.33
LINK C THR B 126 N MSE B 127 1555 1555 1.33
LINK C MSE B 127 N ILE B 128 1555 1555 1.33
LINK C PHE B 134 N MSE B 135 1555 1555 1.33
LINK C MSE B 135 N ASN B 136 1555 1555 1.33
LINK C LEU B 156 N MSE B 157 1555 1555 1.33
LINK C MSE B 157 N ASP B 158 1555 1555 1.33
LINK C VAL B 172 N MSE B 173 1555 1555 1.33
LINK C MSE B 173 N GLY B 174 1555 1555 1.32
LINK C TYR B 238 N MSE B 239 1555 1555 1.32
LINK C MSE B 239 N ALA B 240 1555 1555 1.33
LINK C HIS B 259 N MSE B 260 1555 1555 1.33
LINK C MSE B 260 N THR B 261 1555 1555 1.33
LINK O VAL B 62 NA NA B 284 1555 1555 2.97
LINK OH TYR B 83 NA NA B 284 1555 1555 3.02
LINK OG SER B 64 NA NA B 284 1555 1555 3.02
CISPEP 1 PRO A 138 PRO A 139 0 2.28
CISPEP 2 PRO B 138 PRO B 139 0 -1.98
SITE 1 AC1 4 LYS A 16 ASN A 136 GLU A 146 ARG A 147
SITE 1 AC2 3 HIS A 177 SER A 178 LEU A 181
SITE 1 AC3 2 ARG A 44 GLU A 180
SITE 1 AC4 1 GLN A 275
SITE 1 AC5 4 ASN B 136 GLU B 146 ARG B 147 HOH B 406
SITE 1 AC6 4 HIS B 177 SER B 178 LEU B 181 HOH B 425
SITE 1 AC7 3 VAL B 62 SER B 64 TYR B 83
SITE 1 AC8 5 PRO B 268 HOH B 329 HOH B 333 HOH B 343
SITE 2 AC8 5 HOH B 371
CRYST1 123.067 123.067 49.218 90.00 90.00 90.00 P 4 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 0.008126 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020318 0.00000
TER 2117 ASN A 277
TER 4315 THR B 279
MASTER 331 0 26 30 18 0 9 6 4534 2 199 44
END |