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HEADER HYDROLASE 06-JUN-18 6A0W
TITLE CRYSTAL STRUCTURE OF LIPASE FROM RHIZOPUS MICROSPORUS VAR. CHINENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOPUS CHINENSIS;
SOURCE 3 ORGANISM_COMMON: BREAD MOLD;
SOURCE 4 ORGANISM_TAXID: 4843;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS RHIZOPUS MICROSPORUS VAR. CHINENSIS, LIPASE, N-TERMINAL POLYPEPTIDE
KEYWDS 2 SEGMENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHANG,X.W.YU,Y.XU,C.H.HUANG,R.T.GUO
REVDAT 1 09-OCT-19 6A0W 0
SPRSDE 09-OCT-19 6A0W 4L3W
JRNL AUTH M.ZHANG,X.W.YU,Y.XU,R.T.GUO,G.V.T.SWAPNA,T.SZYPERSKI,
JRNL AUTH 2 J.F.HUNT,G.T.MONTELIONE
JRNL TITL STRUCTURAL BASIS BY WHICH THE N-TERMINAL POLYPEPTIDE SEGMENT
JRNL TITL 2 OFRHIZOPUS CHINENSISLIPASE REGULATES ITS SUBSTRATE BINDING
JRNL TITL 3 AFFINITY.
JRNL REF BIOCHEMISTRY V. 58 3943 2019
JRNL REFN ISSN 0006-2960
JRNL PMID 31436959
JRNL DOI 10.1021/ACS.BIOCHEM.9B00462
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 28451
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1421
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2041
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2216
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.94000
REMARK 3 B22 (A**2) : 1.94000
REMARK 3 B33 (A**2) : -6.30000
REMARK 3 B12 (A**2) : 0.97000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.925
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2280 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2072 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3110 ; 1.505 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4820 ; 0.825 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 7.928 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;37.332 ;24.086
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 354 ;16.550 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;19.267 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 357 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2508 ; 0.018 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 455 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1146 ; 4.198 ; 3.556
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1145 ; 4.191 ; 3.555
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1429 ; 5.157 ; 5.304
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1430 ; 5.157 ; 5.305
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1134 ; 6.158 ; 3.984
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1130 ; 6.144 ; 3.969
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1675 ; 7.952 ; 5.755
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2672 ; 9.135 ;43.901
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2619 ; 9.051 ;43.448
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6A0W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1300007969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
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 : 30238
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.7200
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
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: PHASER
REMARK 200 STARTING MODEL: 1LGY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM TRIS PH 8.0, 150MM NACL, 0.25M
REMARK 280 (NH4)2SO4, 25% PEG 4000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 33.71700
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 67.43400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 67.43400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.71700
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 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 ASP A 1
REMARK 465 THR A 24
REMARK 465 ALA A 25
REMARK 465 PRO A 26
REMARK 465 SER A 27
REMARK 465 SER A 28
REMARK 465 ASP A 29
REMARK 465 SER A 30
REMARK 465 GLY A 31
REMARK 465 GLY A 297
REMARK 465 SER A 298
REMARK 465 SER A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 107 C ARG A 108 N 0.189
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 PRO A 13 171.48 -48.15
REMARK 500 PRO A 18 155.25 -45.20
REMARK 500 TRP A 65 71.33 -118.92
REMARK 500 SER A 172 -140.70 60.84
REMARK 500 LYS A 229 -112.05 42.04
REMARK 500 CYS A 271 -129.10 -100.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 108 -11.98
REMARK 500
REMARK 500 REMARK: NULL
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
DBREF 6A0W A 1 296 UNP A3FM73 A3FM73_RHICH 94 389
SEQADV 6A0W GLY A 297 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W SER A 298 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W SER A 299 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W HIS A 300 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W HIS A 301 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W HIS A 302 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W HIS A 303 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W HIS A 304 UNP A3FM73 EXPRESSION TAG
SEQADV 6A0W HIS A 305 UNP A3FM73 EXPRESSION TAG
SEQRES 1 A 305 ASP THR GLU THR VAL GLY GLY MET THR LEU ASP LEU PRO
SEQRES 2 A 305 GLU ASN PRO PRO PRO ILE PRO ALA THR SER THR ALA PRO
SEQRES 3 A 305 SER SER ASP SER GLY GLU VAL VAL THR ALA THR ALA ALA
SEQRES 4 A 305 GLN ILE LYS GLU LEU THR ASN TYR ALA GLY VAL ALA ALA
SEQRES 5 A 305 THR ALA TYR CYS ARG SER VAL VAL PRO GLY THR LYS TRP
SEQRES 6 A 305 ASP CYS LYS GLN CYS LEU LYS TYR VAL PRO ASP GLY LYS
SEQRES 7 A 305 LEU ILE LYS THR PHE THR SER LEU LEU THR ASP THR ASN
SEQRES 8 A 305 GLY PHE ILE LEU ARG SER ASP ALA GLN LYS THR ILE TYR
SEQRES 9 A 305 VAL THR PHE ARG GLY THR ASN SER PHE ARG SER ALA ILE
SEQRES 10 A 305 THR ASP MET VAL PHE THR PHE THR ASP TYR SER PRO VAL
SEQRES 11 A 305 LYS GLY ALA LYS VAL HIS ALA GLY PHE LEU SER SER TYR
SEQRES 12 A 305 ASN GLN VAL VAL LYS ASP TYR PHE PRO VAL VAL GLN ASP
SEQRES 13 A 305 GLN LEU THR ALA TYR PRO ASP TYR LYS VAL ILE VAL THR
SEQRES 14 A 305 GLY HIS SER LEU GLY GLY ALA GLN ALA LEU LEU ALA GLY
SEQRES 15 A 305 MET ASP LEU TYR GLN ARG GLU LYS ARG LEU SER PRO LYS
SEQRES 16 A 305 ASN LEU SER ILE TYR THR VAL GLY CYS PRO ARG VAL GLY
SEQRES 17 A 305 ASN ASN ALA PHE ALA TYR TYR VAL ASP SER THR GLY ILE
SEQRES 18 A 305 PRO PHE HIS ARG THR VAL HIS LYS ARG ASP ILE VAL PRO
SEQRES 19 A 305 HIS VAL PRO PRO GLN ALA PHE GLY TYR LEU HIS PRO GLY
SEQRES 20 A 305 VAL GLU SER TRP ILE LYS GLU ASP PRO ALA ASP VAL GLN
SEQRES 21 A 305 ILE CYS THR SER ASN ILE GLU THR LYS GLN CYS SER ASN
SEQRES 22 A 305 SER ILE VAL PRO PHE THR SER ILE ALA ASP HIS LEU THR
SEQRES 23 A 305 TYR PHE GLY ILE ASN GLU GLY SER CYS LEU GLY SER SER
SEQRES 24 A 305 HIS HIS HIS HIS HIS HIS
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 HOH *212(H2 O)
HELIX 1 AA1 THR A 37 ALA A 54 1 18
HELIX 2 AA2 CYS A 67 VAL A 74 1 8
HELIX 3 AA3 LEU A 86 ASP A 89 5 4
HELIX 4 AA4 SER A 112 ASP A 119 1 8
HELIX 5 AA5 ALA A 137 TYR A 161 1 25
HELIX 6 AA6 SER A 172 GLU A 189 1 18
HELIX 7 AA7 ASN A 209 THR A 219 1 11
HELIX 8 AA8 ILE A 232 VAL A 236 5 5
HELIX 9 AA9 PRO A 238 GLY A 242 5 5
HELIX 10 AB1 CYS A 271 VAL A 276 5 6
HELIX 11 AB2 ILE A 281 HIS A 284 5 4
SHEET 1 AA1 2 THR A 4 VAL A 5 0
SHEET 2 AA1 2 MET A 8 THR A 9 -1 O MET A 8 N VAL A 5
SHEET 1 AA2 9 VAL A 33 THR A 35 0
SHEET 2 AA2 9 ASP A 258 CYS A 262 -1 O ILE A 261 N VAL A 34
SHEET 3 AA2 9 VAL A 248 GLU A 254 -1 N TRP A 251 O GLN A 260
SHEET 4 AA2 9 PHE A 223 HIS A 228 1 N VAL A 227 O ILE A 252
SHEET 5 AA2 9 LEU A 197 VAL A 202 1 N ILE A 199 O HIS A 224
SHEET 6 AA2 9 LYS A 165 HIS A 171 1 N VAL A 168 O TYR A 200
SHEET 7 AA2 9 THR A 102 ARG A 108 1 N ILE A 103 O LYS A 165
SHEET 8 AA2 9 THR A 90 SER A 97 -1 N LEU A 95 O TYR A 104
SHEET 9 AA2 9 LYS A 78 SER A 85 -1 N SER A 85 O THR A 90
SHEET 1 AA3 2 PHE A 124 ASP A 126 0
SHEET 2 AA3 2 LYS A 134 HIS A 136 -1 O VAL A 135 N THR A 125
SHEET 1 AA4 2 THR A 286 TYR A 287 0
SHEET 2 AA4 2 ILE A 290 ASN A 291 -1 O ILE A 290 N TYR A 287
SSBOND 1 CYS A 56 CYS A 295 1555 1555 2.08
SSBOND 2 CYS A 67 CYS A 70 1555 1555 2.07
SSBOND 3 CYS A 262 CYS A 271 1555 1555 2.05
CISPEP 1 VAL A 60 PRO A 61 0 10.83
CISPEP 2 VAL A 236 PRO A 237 0 -15.67
CISPEP 3 ASP A 255 PRO A 256 0 4.90
CISPEP 4 VAL A 276 PRO A 277 0 18.63
SITE 1 AC1 5 GLN A 40 GLU A 43 HIS A 224 HOH A 640
SITE 2 AC1 5 HOH A 655
SITE 1 AC2 9 HIS A 228 LYS A 229 ILE A 252 ASP A 255
SITE 2 AC2 9 THR A 286 PHE A 288 GLY A 289 HOH A 599
SITE 3 AC2 9 HOH A 656
SITE 1 AC3 5 ASN A 210 TYR A 214 SER A 294 HOH A 526
SITE 2 AC3 5 HOH A 585
CRYST1 86.225 86.225 101.151 90.00 90.00 120.00 P 31 2 1 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 0.011598 0.006696 0.000000 0.00000
SCALE2 0.000000 0.013392 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009886 0.00000
TER 2217 LEU A 296
MASTER 342 0 3 11 15 0 7 6 2443 1 21 24
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