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HEADER HYDROLASE 25-OCT-07 3B5E
TITLE CRYSTAL STRUCTURE OF CARBOXYLESTERASE (NP_108484.1) FROM
TITLE 2 MESORHIZOBIUM LOTI AT 1.75 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MLL8374 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MESORHIZOBIUM LOTI MAFF303099;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: MAFF303099;
SOURCE 5 GENE: NP_108484.1, MLL8374;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS NP_108484.1, CARBOXYLESTERASE, STRUCTURAL GENOMICS, JOINT
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 13-NOV-07 3B5E 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYLESTERASE
JRNL TITL 2 (NP_108484.1) FROM MESORHIZOBIUM LOTI AT 1.75 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 62069
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3150
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4002
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 224
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3955
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.51000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.67000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.089
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.214
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3540 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2419 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4823 ; 1.526 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5875 ; 1.031 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 466 ; 6.011 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;29.334 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 527 ;12.266 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;15.624 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 550 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4031 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 730 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 675 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2599 ; 0.202 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1670 ; 0.168 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1872 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 343 ; 0.159 ; 0.200
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): 13 ; 0.083 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.171 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.112 ; 0.200
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): 2438 ; 1.914 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 895 ; 0.559 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3633 ; 2.629 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1364 ; 4.496 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1189 ; 6.715 ;11.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 215 4
REMARK 3 1 B 7 B 215 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2696 ; 0.330 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2696 ; 0.780 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 215
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5875 42.4243 24.6654
REMARK 3 T TENSOR
REMARK 3 T11: -0.0068 T22: -0.0339
REMARK 3 T33: -0.0161 T12: -0.0222
REMARK 3 T13: -0.0130 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.6717 L22: 0.7391
REMARK 3 L33: 1.2835 L12: 0.1943
REMARK 3 L13: 0.2092 L23: 0.5163
REMARK 3 S TENSOR
REMARK 3 S11: 0.0289 S12: -0.0640 S13: 0.0791
REMARK 3 S21: 0.1472 S22: -0.0566 S23: -0.0194
REMARK 3 S31: -0.0365 S32: -0.0580 S33: 0.0277
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 215
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4092 13.6202 12.2196
REMARK 3 T TENSOR
REMARK 3 T11: -0.0741 T22: -0.0553
REMARK 3 T33: -0.0250 T12: -0.0081
REMARK 3 T13: -0.0121 T23: 0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.6411 L22: 0.5458
REMARK 3 L33: 1.3922 L12: -0.0221
REMARK 3 L13: 0.0487 L23: -0.1244
REMARK 3 S TENSOR
REMARK 3 S11: 0.0289 S12: -0.0510 S13: -0.0757
REMARK 3 S21: 0.0813 S22: 0.0009 S23: -0.0207
REMARK 3 S31: 0.1145 S32: -0.0428 S33: -0.0298
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS
REMARK 3 ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO
REMARK 3 PARTIAL S-MET INCORPORATION. 4. SO4 AND ETHYLENE GLYCOL ARE
REMARK 3 MODELED BASED ON CRYSTALLIZATION AND CRYO CONDITIONS. 5.
REMARK 3 UNEXPLAINED ELECTRON DENSITIES NEAR RESIDUES 108 AND 209 IN
REMARK 3 SUBUNIT A WERE NOT MODELED.
REMARK 4
REMARK 4 3B5E COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB045099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 10.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000, 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62118
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 29.643
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 2.0M (NH4)2SO4, 0.2M
REMARK 280 LI2SO4, 0.1M CAPS PH 10.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 23.58000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.81000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.81000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.58000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.50000
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 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 300 REMARK: SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT
REMARK 300 SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A
REMARK 300 SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION BUT CRYSTAL
REMARK 300 PACKING ANALYSIS DOES NOT REVEAL ANY INTERFACES THAT ARE
REMARK 300 LIKELY STABLE AS A DIMER.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 GLY A 0
REMARK 465 MSE A 1
REMARK 465 ILE A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 GLY A 5
REMARK 465 ILE A 6
REMARK 465 ILE A 216
REMARK 465 ALA A 217
REMARK 465 ILE A 218
REMARK 465 ALA A 219
REMARK 465 GLN A 220
REMARK 465 ALA A 221
REMARK 465 ASP A 222
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 ILE B 2
REMARK 465 ILE B 216
REMARK 465 ALA B 217
REMARK 465 ILE B 218
REMARK 465 ALA B 219
REMARK 465 GLN B 220
REMARK 465 ALA B 221
REMARK 465 ASP B 222
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 GLU A 27 CD OE1 OE2
REMARK 470 ARG A 29 CD NE CZ NH1 NH2
REMARK 470 LYS A 85 CD CE NZ
REMARK 470 LYS A 103 CD CE NZ
REMARK 470 ARG A 184 CZ NH1 NH2
REMARK 470 ARG B 29 CD NE CZ NH1 NH2
REMARK 470 GLU B 68 OE1 OE2
REMARK 470 LYS B 103 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
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 GLU A 68 -124.17 55.34
REMARK 500 THR A 80 -6.54 77.11
REMARK 500 SER A 118 -118.36 59.31
REMARK 500 ALA B 53 79.26 -150.70
REMARK 500 GLU B 68 -121.48 54.20
REMARK 500 SER B 118 -113.98 59.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 377848 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3B5E A 1 222 UNP Q983D6 Q983D6_RHILO 1 222
DBREF 3B5E B 1 222 UNP Q983D6 Q983D6_RHILO 1 222
SEQADV 3B5E GLY A 0 UNP Q983D6 LEADER SEQUENCE
SEQADV 3B5E GLY B 0 UNP Q983D6 LEADER SEQUENCE
SEQRES 1 A 223 GLY MSE ILE GLY ASP GLY ILE GLU ASN SER PRO LEU LEU
SEQRES 2 A 223 THR ASP LEU ALA PHE PRO TYR ARG LEU LEU GLY ALA GLY
SEQRES 3 A 223 LYS GLU SER ARG GLU CYS LEU PHE LEU LEU HIS GLY SER
SEQRES 4 A 223 GLY VAL ASP GLU THR THR LEU VAL PRO LEU ALA ARG ARG
SEQRES 5 A 223 ILE ALA PRO THR ALA THR LEU VAL ALA ALA ARG GLY ARG
SEQRES 6 A 223 ILE PRO GLN GLU ASP GLY PHE ARG TRP PHE GLU ARG ILE
SEQRES 7 A 223 ASP PRO THR ARG PHE GLU GLN LYS SER ILE LEU ALA GLU
SEQRES 8 A 223 THR ALA ALA PHE ALA ALA PHE THR ASN GLU ALA ALA LYS
SEQRES 9 A 223 ARG HIS GLY LEU ASN LEU ASP HIS ALA THR PHE LEU GLY
SEQRES 10 A 223 TYR SER ASN GLY ALA ASN LEU VAL SER SER LEU MSE LEU
SEQRES 11 A 223 LEU HIS PRO GLY ILE VAL ARG LEU ALA ALA LEU LEU ARG
SEQRES 12 A 223 PRO MSE PRO VAL LEU ASP HIS VAL PRO ALA THR ASP LEU
SEQRES 13 A 223 ALA GLY ILE ARG THR LEU ILE ILE ALA GLY ALA ALA ASP
SEQRES 14 A 223 GLU THR TYR GLY PRO PHE VAL PRO ALA LEU VAL THR LEU
SEQRES 15 A 223 LEU SER ARG HIS GLY ALA GLU VAL ASP ALA ARG ILE ILE
SEQRES 16 A 223 PRO SER GLY HIS ASP ILE GLY ASP PRO ASP ALA ALA ILE
SEQRES 17 A 223 VAL ARG GLN TRP LEU ALA GLY PRO ILE ALA ILE ALA GLN
SEQRES 18 A 223 ALA ASP
SEQRES 1 B 223 GLY MSE ILE GLY ASP GLY ILE GLU ASN SER PRO LEU LEU
SEQRES 2 B 223 THR ASP LEU ALA PHE PRO TYR ARG LEU LEU GLY ALA GLY
SEQRES 3 B 223 LYS GLU SER ARG GLU CYS LEU PHE LEU LEU HIS GLY SER
SEQRES 4 B 223 GLY VAL ASP GLU THR THR LEU VAL PRO LEU ALA ARG ARG
SEQRES 5 B 223 ILE ALA PRO THR ALA THR LEU VAL ALA ALA ARG GLY ARG
SEQRES 6 B 223 ILE PRO GLN GLU ASP GLY PHE ARG TRP PHE GLU ARG ILE
SEQRES 7 B 223 ASP PRO THR ARG PHE GLU GLN LYS SER ILE LEU ALA GLU
SEQRES 8 B 223 THR ALA ALA PHE ALA ALA PHE THR ASN GLU ALA ALA LYS
SEQRES 9 B 223 ARG HIS GLY LEU ASN LEU ASP HIS ALA THR PHE LEU GLY
SEQRES 10 B 223 TYR SER ASN GLY ALA ASN LEU VAL SER SER LEU MSE LEU
SEQRES 11 B 223 LEU HIS PRO GLY ILE VAL ARG LEU ALA ALA LEU LEU ARG
SEQRES 12 B 223 PRO MSE PRO VAL LEU ASP HIS VAL PRO ALA THR ASP LEU
SEQRES 13 B 223 ALA GLY ILE ARG THR LEU ILE ILE ALA GLY ALA ALA ASP
SEQRES 14 B 223 GLU THR TYR GLY PRO PHE VAL PRO ALA LEU VAL THR LEU
SEQRES 15 B 223 LEU SER ARG HIS GLY ALA GLU VAL ASP ALA ARG ILE ILE
SEQRES 16 B 223 PRO SER GLY HIS ASP ILE GLY ASP PRO ASP ALA ALA ILE
SEQRES 17 B 223 VAL ARG GLN TRP LEU ALA GLY PRO ILE ALA ILE ALA GLN
SEQRES 18 B 223 ALA ASP
MODRES 3B5E MSE A 128 MET SELENOMETHIONINE
MODRES 3B5E MSE A 144 MET SELENOMETHIONINE
MODRES 3B5E MSE B 128 MET SELENOMETHIONINE
MODRES 3B5E MSE B 144 MET SELENOMETHIONINE
HET MSE A 128 8
HET MSE A 144 8
HET MSE B 128 8
HET MSE B 144 8
HET SO4 B 223 5
HET SO4 A 223 5
HET EDO B 224 4
HET EDO A 224 4
HET EDO A 225 4
HET EDO B 225 4
HET EDO A 226 4
HET EDO A 227 4
HET EDO A 228 4
HET EDO B 226 4
HET EDO B 227 4
HET EDO A 229 4
HET EDO A 230 4
HET EDO A 231 4
HET EDO A 232 4
HET EDO B 228 4
HET EDO B 229 4
HET EDO B 230 4
HET EDO B 231 4
HET EDO A 233 4
HET EDO A 234 4
HET EDO B 232 4
HET EDO B 233 4
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 EDO 21(C2 H6 O2)
FORMUL 26 HOH *482(H2 O)
HELIX 1 1 LEU A 45 ALA A 53 1 9
HELIX 2 2 GLU A 83 GLY A 106 1 24
HELIX 3 3 ASN A 108 ASP A 110 5 3
HELIX 4 4 SER A 118 HIS A 131 1 14
HELIX 5 5 TYR A 171 PRO A 173 5 3
HELIX 6 6 PHE A 174 HIS A 185 1 12
HELIX 7 7 GLY A 201 GLY A 214 1 14
HELIX 8 8 LEU B 45 ALA B 53 1 9
HELIX 9 9 GLU B 83 GLY B 106 1 24
HELIX 10 10 ASN B 108 ASP B 110 5 3
HELIX 11 11 SER B 118 HIS B 131 1 14
HELIX 12 12 TYR B 171 PRO B 173 5 3
HELIX 13 13 PHE B 174 HIS B 185 1 12
HELIX 14 14 GLY B 201 GLY B 214 1 14
SHEET 1 A 7 TYR A 19 LEU A 22 0
SHEET 2 A 7 THR A 57 ALA A 61 -1 O ALA A 60 N ARG A 20
SHEET 3 A 7 CYS A 31 LEU A 35 1 N LEU A 32 O VAL A 59
SHEET 4 A 7 ALA A 112 TYR A 117 1 O LEU A 115 N PHE A 33
SHEET 5 A 7 LEU A 137 LEU A 141 1 O ALA A 139 N PHE A 114
SHEET 6 A 7 ARG A 159 GLY A 165 1 O LEU A 161 N LEU A 140
SHEET 7 A 7 GLU A 188 ILE A 194 1 O ARG A 192 N ALA A 164
SHEET 1 B 2 ILE A 65 GLN A 67 0
SHEET 2 B 2 GLY A 70 ARG A 72 -1 O GLY A 70 N GLN A 67
SHEET 1 C 2 ARG A 76 ASP A 78 0
SHEET 2 C 2 ARG A 81 PHE A 82 -1 O ARG A 81 N ILE A 77
SHEET 1 D 7 TYR B 19 LEU B 22 0
SHEET 2 D 7 THR B 57 ALA B 61 -1 O LEU B 58 N LEU B 22
SHEET 3 D 7 CYS B 31 LEU B 35 1 N LEU B 34 O VAL B 59
SHEET 4 D 7 ALA B 112 TYR B 117 1 O LEU B 115 N PHE B 33
SHEET 5 D 7 LEU B 137 LEU B 141 1 O LEU B 141 N GLY B 116
SHEET 6 D 7 ARG B 159 GLY B 165 1 O LEU B 161 N LEU B 140
SHEET 7 D 7 GLU B 188 ILE B 194 1 O ARG B 192 N ALA B 164
SHEET 1 E 2 ILE B 65 GLN B 67 0
SHEET 2 E 2 GLY B 70 ARG B 72 -1 O GLY B 70 N GLN B 67
SHEET 1 F 2 ARG B 76 ASP B 78 0
SHEET 2 F 2 ARG B 81 PHE B 82 -1 O ARG B 81 N ILE B 77
CRYST1 47.160 105.000 123.620 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 0.021204 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009524 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008089 0.00000
TER 1680 PRO A 215
TER 3373 PRO B 215
MASTER 391 0 27 14 22 0 0 6 3955 2 126 36
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