| content |
HEADER HYDROLASE 05-FEB-14 4OPM
TITLE CRYSTAL STRUCTURE OF A PUTATIVE LIPASE (LIP1) FROM ACINETOBACTER
TITLE 2 BAUMANNII AYE AT 1.70 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 26-330;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII;
SOURCE 3 ORGANISM_TAXID: 509173;
SOURCE 4 STRAIN: AYE;
SOURCE 5 GENE: LIP1, ABAYE2810;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PF06342 FAMILY, DUF1057, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 19-FEB-14 4OPM 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE LIPASE (LIP1) FROM
JRNL TITL 2 ACINETOBACTER BAUMANNII AYE AT 1.70 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 77808
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3893
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.12
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5754
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2321
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5487
REMARK 3 BIN R VALUE (WORKING SET) : 0.2303
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.64
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 267
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4716
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 188
REMARK 3 SOLVENT ATOMS : 685
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.90200
REMARK 3 B22 (A**2) : -2.01140
REMARK 3 B33 (A**2) : 1.10950
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.64150
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.199
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5237 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7119 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2567 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 144 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 753 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5237 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 685 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6675 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.93
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.28
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.61
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|0 - 323}
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9441 4.0943 18.2781
REMARK 3 T TENSOR
REMARK 3 T11: -0.0737 T22: 0.0327
REMARK 3 T33: -0.0735 T12: 0.0059
REMARK 3 T13: 0.0241 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.6727 L22: 0.2929
REMARK 3 L33: 0.9575 L12: 0.0446
REMARK 3 L13: -0.0136 L23: 0.0792
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: 0.1197 S13: -0.0320
REMARK 3 S21: -0.0537 S22: -0.0074 S23: -0.0450
REMARK 3 S31: 0.0207 S32: 0.1194 S33: -0.0049
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {B|0 - 323}
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8152 7.3803 44.4854
REMARK 3 T TENSOR
REMARK 3 T11: -0.0630 T22: 0.0169
REMARK 3 T33: -0.0567 T12: -0.0013
REMARK 3 T13: 0.0153 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.5703 L22: 0.4570
REMARK 3 L33: 0.7693 L12: 0.0509
REMARK 3 L13: -0.0438 L23: -0.0614
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: -0.0314 S13: -0.0044
REMARK 3 S21: 0.0129 S22: 0.0152 S23: 0.0427
REMARK 3 S31: -0.0401 S32: -0.1373 S33: -0.0143
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. A MET-INHIBITION PROTOCOL WAS USED
REMARK 3 FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 3. THE MAD PHASES WERE USED AS RESTRAINTS DURING
REMARK 3 REFINEMENT. 4. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR
REMARK 3 RESTRAINT REPRESENTATION (-AUTONCS). 5. SULFATE(SO4),
REMARK 3 GLYCEROL(GOL) AND PEG FRAGMENTS (PE4 AND 15P) MODELED ARE PRESENT
REMARK 3 IN CRYSTALLIZATION CONDITIONS. PGX IS LOCATED IN THE ACTIVE SITES.
REMARK 4
REMARK 4 4OPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB084791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97895,0.97963,0.91837
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(111) BENT
REMARK 200 OPTICS : FLAT MIRROR (VERTICAL FOCUSING);
REMARK 200 SINGLE CRYSTAL SI(111) BENT
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING)
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77844
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 48.556
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD,SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.0500M LITHIUM SULFATE, 10.00%
REMARK 280 GLYCEROL, 30.00% POLYETHYLENE GLYCOL 600, 0.1M HEPES PH 7.5,
REMARK 280 NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 50.19900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.45100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.19900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.45100
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, 3
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 SER A 324
REMARK 465 SER A 325
REMARK 465 LYS A 326
REMARK 465 THR A 327
REMARK 465 THR A 328
REMARK 465 THR A 329
REMARK 465 PRO A 330
REMARK 465 SER B 324
REMARK 465 SER B 325
REMARK 465 LYS B 326
REMARK 465 THR B 327
REMARK 465 THR B 328
REMARK 465 THR B 329
REMARK 465 PRO B 330
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 B 135 CG CD CE NZ
REMARK 470 GLN B 323 CG CD OE1 NE2
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 144 -118.01 55.57
REMARK 500 ASN A 177 37.21 -147.25
REMARK 500 ALA A 304 52.07 -154.76
REMARK 500 SER B 144 -119.69 56.80
REMARK 500 ALA B 304 52.40 -154.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 15P A 401
REMARK 610 PE4 A 402
REMARK 610 PE4 A 403
REMARK 610 PE4 A 404
REMARK 610 PE4 A 405
REMARK 610 PE4 A 406
REMARK 610 PE4 A 407
REMARK 610 PE4 B 401
REMARK 610 PE4 B 402
REMARK 610 PE4 B 403
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 15P A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-420351 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT (26-330) WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 4OPM A 26 330 UNP B0V9K7 B0V9K7_ACIBY 26 330
DBREF 4OPM B 26 330 UNP B0V9K7 B0V9K7_ACIBY 26 330
SEQADV 4OPM GLY A 0 UNP B0V9K7 LEADER SEQUENCE
SEQADV 4OPM GLY B 0 UNP B0V9K7 LEADER SEQUENCE
SEQRES 1 A 306 GLY ALA ASP ASN ILE ASP VAL SER PHE GLN THR ILE LEU
SEQRES 2 A 306 GLN GLN GLU ARG ASN TRP ALA GLY LEU GLN SER LYS SER
SEQRES 3 A 306 LEU LYS VAL GLY ASP ILE THR TRP SER TYR SER GLU GLY
SEQRES 4 A 306 GLY SER SER THR LYS PRO THR LEU LEU LEU ILE HIS GLY
SEQRES 5 A 306 LEU ALA GLY SER ARG ASP ASN TRP ASN ARG VAL ALA HIS
SEQRES 6 A 306 TYR LEU THR THR ASN TYR HIS VAL ILE ILE PRO ASP LEU
SEQRES 7 A 306 PRO GLY SER GLY GLU THR ILE VAL SER GLN ASP PHE ASP
SEQRES 8 A 306 TYR SER VAL PRO ASN LEU ALA GLU LYS LEU ARG ARG PHE
SEQRES 9 A 306 VAL GLU ALA ALA ASN LEU LYS GLY PRO ILE HIS ILE ALA
SEQRES 10 A 306 GLY HIS SER LEU GLY GLY SER ILE ALA LEU LEU TYR ALA
SEQRES 11 A 306 GLY GLN TYR PRO PHE GLU THR LYS SER LEU PHE LEU VAL
SEQRES 12 A 306 ASP SER GLY GLY ILE PHE ARG SER ALA ASN THR ILE TYR
SEQRES 13 A 306 LEU LYS ASP PRO THR TYR LEU LYS GLN LEU LEU VAL SER
SEQRES 14 A 306 LYS LYS GLY ASP PHE ASN TYR LEU LEU LYS GLN THR MSE
SEQRES 15 A 306 PHE ASN PRO PRO PHE ILE PRO LYS GLU PHE LEU GLN ALA
SEQRES 16 A 306 GLN GLU LYS LEU MSE ILE ASN GLN ALA PRO GLN THR GLN
SEQRES 17 A 306 LYS LEU VAL ASP GLN LEU ILE ALA LEU ASN LYS VAL TYR
SEQRES 18 A 306 THR PRO ASP SER PHE ALA VAL LEU THR LYS THR ILE ASP
SEQRES 19 A 306 ALA PRO THR LEU ILE LEU TRP GLY LYS GLN ASP LYS ILE
SEQRES 20 A 306 ILE ASN VAL GLU VAL ALA ASN GLU LEU LYS ARG LEU LEU
SEQRES 21 A 306 LYS ASN ALA GLN PRO PRO VAL ILE LEU GLU ASN VAL GLY
SEQRES 22 A 306 HIS MSE PRO ILE LEU GLU ALA GLU GLN LEU VAL ILE GLN
SEQRES 23 A 306 GLN TYR VAL PRO PHE LEU LEU LYS VAL GLU THR ASN GLN
SEQRES 24 A 306 SER SER LYS THR THR THR PRO
SEQRES 1 B 306 GLY ALA ASP ASN ILE ASP VAL SER PHE GLN THR ILE LEU
SEQRES 2 B 306 GLN GLN GLU ARG ASN TRP ALA GLY LEU GLN SER LYS SER
SEQRES 3 B 306 LEU LYS VAL GLY ASP ILE THR TRP SER TYR SER GLU GLY
SEQRES 4 B 306 GLY SER SER THR LYS PRO THR LEU LEU LEU ILE HIS GLY
SEQRES 5 B 306 LEU ALA GLY SER ARG ASP ASN TRP ASN ARG VAL ALA HIS
SEQRES 6 B 306 TYR LEU THR THR ASN TYR HIS VAL ILE ILE PRO ASP LEU
SEQRES 7 B 306 PRO GLY SER GLY GLU THR ILE VAL SER GLN ASP PHE ASP
SEQRES 8 B 306 TYR SER VAL PRO ASN LEU ALA GLU LYS LEU ARG ARG PHE
SEQRES 9 B 306 VAL GLU ALA ALA ASN LEU LYS GLY PRO ILE HIS ILE ALA
SEQRES 10 B 306 GLY HIS SER LEU GLY GLY SER ILE ALA LEU LEU TYR ALA
SEQRES 11 B 306 GLY GLN TYR PRO PHE GLU THR LYS SER LEU PHE LEU VAL
SEQRES 12 B 306 ASP SER GLY GLY ILE PHE ARG SER ALA ASN THR ILE TYR
SEQRES 13 B 306 LEU LYS ASP PRO THR TYR LEU LYS GLN LEU LEU VAL SER
SEQRES 14 B 306 LYS LYS GLY ASP PHE ASN TYR LEU LEU LYS GLN THR MSE
SEQRES 15 B 306 PHE ASN PRO PRO PHE ILE PRO LYS GLU PHE LEU GLN ALA
SEQRES 16 B 306 GLN GLU LYS LEU MSE ILE ASN GLN ALA PRO GLN THR GLN
SEQRES 17 B 306 LYS LEU VAL ASP GLN LEU ILE ALA LEU ASN LYS VAL TYR
SEQRES 18 B 306 THR PRO ASP SER PHE ALA VAL LEU THR LYS THR ILE ASP
SEQRES 19 B 306 ALA PRO THR LEU ILE LEU TRP GLY LYS GLN ASP LYS ILE
SEQRES 20 B 306 ILE ASN VAL GLU VAL ALA ASN GLU LEU LYS ARG LEU LEU
SEQRES 21 B 306 LYS ASN ALA GLN PRO PRO VAL ILE LEU GLU ASN VAL GLY
SEQRES 22 B 306 HIS MSE PRO ILE LEU GLU ALA GLU GLN LEU VAL ILE GLN
SEQRES 23 B 306 GLN TYR VAL PRO PHE LEU LEU LYS VAL GLU THR ASN GLN
SEQRES 24 B 306 SER SER LYS THR THR THR PRO
MODRES 4OPM MSE A 206 MET SELENOMETHIONINE
MODRES 4OPM MSE A 224 MET SELENOMETHIONINE
MODRES 4OPM MSE A 299 MET SELENOMETHIONINE
MODRES 4OPM MSE B 206 MET SELENOMETHIONINE
MODRES 4OPM MSE B 224 MET SELENOMETHIONINE
MODRES 4OPM MSE B 299 MET SELENOMETHIONINE
HET MSE A 206 8
HET MSE A 224 8
HET MSE A 299 13
HET MSE B 206 8
HET MSE B 224 8
HET MSE B 299 13
HET 15P A 401 91
HET PE4 A 402 7
HET PE4 A 403 22
HET PE4 A 404 7
HET PE4 A 405 7
HET PE4 A 406 7
HET PE4 A 407 7
HET PE4 B 401 10
HET PE4 B 402 7
HET PE4 B 403 7
HET GOL B 404 6
HET SO4 B 405 5
HET SO4 B 406 5
HETNAM MSE SELENOMETHIONINE
HETNAM 15P POLYETHYLENE GLYCOL (N=34)
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN 15P PEG 1500
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 3 15P C69 H140 O35
FORMUL 4 PE4 9(C16 H34 O8)
FORMUL 13 GOL C3 H8 O3
FORMUL 14 SO4 2(O4 S 2-)
FORMUL 16 HOH *685(H2 O)
HELIX 1 1 PHE A 33 ALA A 44 1 12
HELIX 2 2 SER A 80 ASN A 83 5 4
HELIX 3 3 TRP A 84 HIS A 89 1 6
HELIX 4 4 SER A 117 ALA A 132 1 16
HELIX 5 5 SER A 144 TYR A 157 1 14
HELIX 6 6 THR A 178 ASP A 183 1 6
HELIX 7 7 PRO A 184 LEU A 191 5 8
HELIX 8 8 GLY A 196 MSE A 206 1 11
HELIX 9 9 PRO A 213 TYR A 245 1 33
HELIX 10 10 THR A 246 THR A 256 1 11
HELIX 11 11 VAL A 274 LEU A 284 1 11
HELIX 12 12 MSE A 299 ALA A 304 1 6
HELIX 13 13 ALA A 304 GLN A 323 1 20
HELIX 14 14 PHE B 33 ALA B 44 1 12
HELIX 15 15 SER B 80 ASN B 83 5 4
HELIX 16 16 TRP B 84 HIS B 89 1 6
HELIX 17 17 SER B 117 ALA B 132 1 16
HELIX 18 18 SER B 144 TYR B 157 1 14
HELIX 19 19 THR B 178 ASP B 183 1 6
HELIX 20 20 PRO B 184 LEU B 191 5 8
HELIX 21 21 GLY B 196 MSE B 206 1 11
HELIX 22 22 PRO B 213 TYR B 245 1 33
HELIX 23 23 THR B 246 THR B 256 1 11
HELIX 24 24 VAL B 274 LEU B 284 1 11
HELIX 25 25 MSE B 299 ALA B 304 1 6
HELIX 26 26 ALA B 304 GLN B 323 1 20
SHEET 1 A 2 ASN A 28 SER A 32 0
SHEET 2 A 2 ASN B 28 SER B 32 -1 O VAL B 31 N ILE A 29
SHEET 1 B 8 LEU A 46 VAL A 53 0
SHEET 2 B 8 ILE A 56 GLY A 63 -1 O ILE A 56 N VAL A 53
SHEET 3 B 8 HIS A 96 PRO A 100 -1 O ILE A 99 N SER A 61
SHEET 4 B 8 THR A 70 ILE A 74 1 N LEU A 71 O HIS A 96
SHEET 5 B 8 ILE A 138 HIS A 143 1 O HIS A 139 N LEU A 72
SHEET 6 B 8 THR A 161 VAL A 167 1 O VAL A 167 N GLY A 142
SHEET 7 B 8 THR A 261 GLY A 266 1 O LEU A 262 N LEU A 166
SHEET 8 B 8 VAL A 291 LEU A 293 1 O LEU A 293 N TRP A 265
SHEET 1 C 8 LEU B 46 VAL B 53 0
SHEET 2 C 8 ILE B 56 GLY B 63 -1 O ILE B 56 N VAL B 53
SHEET 3 C 8 HIS B 96 PRO B 100 -1 O ILE B 99 N SER B 61
SHEET 4 C 8 THR B 70 ILE B 74 1 N LEU B 71 O ILE B 98
SHEET 5 C 8 ILE B 138 HIS B 143 1 O HIS B 139 N LEU B 72
SHEET 6 C 8 THR B 161 VAL B 167 1 O LYS B 162 N ILE B 138
SHEET 7 C 8 THR B 261 GLY B 266 1 O LEU B 262 N LEU B 166
SHEET 8 C 8 VAL B 291 LEU B 293 1 O LEU B 293 N TRP B 265
LINK C THR A 205 N MSE A 206 1555 1555 1.34
LINK C MSE A 206 N PHE A 207 1555 1555 1.34
LINK C LEU A 223 N MSE A 224 1555 1555 1.34
LINK C MSE A 224 N ILE A 225 1555 1555 1.37
LINK C HIS A 298 N MSE A 299 1555 1555 1.36
LINK C MSE A 299 N PRO A 300 1555 1555 1.37
LINK C THR B 205 N MSE B 206 1555 1555 1.34
LINK C MSE B 206 N PHE B 207 1555 1555 1.35
LINK C LEU B 223 N MSE B 224 1555 1555 1.34
LINK C MSE B 224 N ILE B 225 1555 1555 1.37
LINK C HIS B 298 N MSE B 299 1555 1555 1.36
LINK C MSE B 299 N PRO B 300 1555 1555 1.36
SITE 1 AC1 16 LEU A 77 SER A 144 GLY A 171 PHE A 198
SITE 2 AC1 16 SER A 249 HOH A 535 HOH A 739 HOH A 781
SITE 3 AC1 16 HOH A 804 GLU B 40 LEU B 77 SER B 144
SITE 4 AC1 16 PHE B 198 PHE B 211 PHE B 216 MSE B 299
SITE 1 AC2 4 ILE A 179 GLN A 189 TYR A 200 HOH A 735
SITE 1 AC3 10 THR A 185 TYR A 186 LYS A 188 GLN A 189
SITE 2 AC3 10 LEU A 191 SER A 193 LYS A 194 ASP A 197
SITE 3 AC3 10 TYR A 200 HOH A 827
SITE 1 AC4 2 ASN A 42 GLY A 45
SITE 1 AC5 4 HIS A 89 THR A 92 THR A 93 PHE B 207
SITE 1 AC6 3 GLN A 310 GLN A 311 HOH A 816
SITE 1 AC7 4 LYS A 52 ASP A 55 ILE A 56 THR A 57
SITE 1 AC8 4 SER B 50 LYS B 52 THR B 185 TYR B 186
SITE 1 AC9 4 ASN B 42 GLY B 45 PE4 B 403 HOH B 766
SITE 1 BC1 5 PHE A 207 HIS B 89 THR B 92 THR B 93
SITE 2 BC1 5 PE4 B 402
SITE 1 BC2 8 ILE A 309 HOH A 695 ASN B 295 HOH B 545
SITE 2 BC2 8 HOH B 675 HOH B 765 HOH B 773 HOH B 806
SITE 1 BC3 9 LYS A 222 GLY B 0 ALA B 26 ASP B 27
SITE 2 BC3 9 LYS B 281 HOH B 616 HOH B 787 HOH B 802
SITE 3 BC3 9 HOH B 833
SITE 1 BC4 9 SER B 111 GLN B 112 ASP B 113 LYS B 203
SITE 2 BC4 9 PHE B 207 LYS B 270 HOH B 604 HOH B 763
SITE 3 BC4 9 HOH B 791
CRYST1 100.398 66.902 110.380 90.00 95.58 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 0.009960 0.000000 0.000973 0.00000
SCALE2 0.000000 0.014947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009103 0.00000
TER 2460 GLN A 323
TER 4918 GLN B 323
MASTER 405 0 19 26 18 0 24 6 5589 2 258 48
END |