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HEADER HYDROLASE 28-NOV-13 4NS4
TITLE CRYSTAL STRUCTURE OF COLD-ACTIVE ESTARASE FROM PSYCHROBACTER
TITLE 2 CRYOHALOLENTIS K5T
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSYCHROBACTER CRYOHALOLENTIS;
SOURCE 3 ORGANISM_TAXID: 335284;
SOURCE 4 STRAIN: K5T;
SOURCE 5 GENE: PCRYO_0023;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A(+)/ESTPC
KEYWDS ALPHA/BETA HYDROLASE FOLD, COLD-ACTIVE ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.BOYKO,L.E.PETROVSKAYA,M.A.GORBACHEVA,D.A.KORGENEVSKY,
AUTHOR 2 K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,D.A.DOLGIKH,M.P.KIRPICHNIKOV,
AUTHOR 3 A.V.LIPKIN,V.O.POPOV
REVDAT 1 07-JAN-15 4NS4 0
JRNL AUTH K.M.BOYKO,L.E.PETROVSKAYA,M.A.GORBACHEVA,D.A.KORGENEVSKY,
JRNL AUTH 2 K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,D.A.DOLGIKH,
JRNL AUTH 3 M.P.KIRPICHNIKOV,A.V.LIPKIN,V.O.POPOV
JRNL TITL THREE-DIMENTIONAL STRUCTURE OF AN ESTERSE FROM PSYCHROBACTER
JRNL TITL 2 CRYOHALOLENTIS K5T PROVIDES CLUES TO UNUSUAL THERMOSTABILITY
JRNL TITL 3 OF A COLD-ACTIVE ENZYME
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 17812
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 963
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1185
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2097
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 147
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : -0.28000
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): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.139
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.350
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2155 ; 0.020 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1437 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2919 ; 1.961 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3546 ; 1.503 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 8.266 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;36.240 ;25.484
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 378 ;17.346 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;19.322 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 332 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2370 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 401 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH MASK
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 4NS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083587.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-12
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 : KURCHATOV SNC
REMARK 200 BEAMLINE : K4.4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.984
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19246
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
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) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
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: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 1J1I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 14% PEG4000, 10% 2-
REMARK 280 PROPANOL, 15% GLYCEROL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.60000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.70000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 MET A -25
REMARK 465 LEU A -24
REMARK 465 LEU A -23
REMARK 465 LYS A -22
REMARK 465 ARG A -21
REMARK 465 LEU A -20
REMARK 465 GLY A -19
REMARK 465 LEU A -18
REMARK 465 ALA A -17
REMARK 465 THR A -16
REMARK 465 LEU A -15
REMARK 465 LEU A -14
REMARK 465 SER A -13
REMARK 465 PHE A -12
REMARK 465 SER A -11
REMARK 465 VAL A -10
REMARK 465 VAL A -9
REMARK 465 GLY A -8
REMARK 465 CYS A -7
REMARK 465 THR A -6
REMARK 465 THR A -5
REMARK 465 ALA A -4
REMARK 465 PRO A -3
REMARK 465 ASN A -2
REMARK 465 THR A -1
REMARK 465 LEU A 0
REMARK 465 ALA A 1
REMARK 465 ILE A 2
REMARK 465 ALA A 147
REMARK 465 GLY A 148
REMARK 465 VAL A 149
REMARK 465 PRO A 150
REMARK 465 LYS A 151
REMARK 465 SER A 152
REMARK 465 LEU A 153
REMARK 465 GLU A 154
REMARK 465 SER A 155
REMARK 465 ALA A 156
REMARK 465 THR A 157
REMARK 465 LEU A 158
REMARK 465 GLU A 159
REMARK 465 ASN A 160
REMARK 465 ASN A 161
REMARK 465 ASN A 315
REMARK 465 VAL A 316
REMARK 465 GLU A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
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 ASN A 3 CG OD1 ND2
REMARK 470 LYS A 7 CD CE NZ
REMARK 470 LYS A 131 CE NZ
REMARK 470 LYS A 167 CD CE NZ
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 LYS A 263 CE NZ
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 HIS A 48 CG HIS A 48 CD2 0.059
REMARK 500 HIS A 266 CG HIS A 266 CD2 0.078
REMARK 500 LYS A 274 C ASP A 301 N 0.140
REMARK 500
REMARK 500 REMARK: NULL
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 62 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 LEU A 163 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LYS A 274 O - C - N ANGL. DEV. = -15.6 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 THR A 4 149.41 -172.44
REMARK 500 ASN A 38 75.72 -65.78
REMARK 500 SER A 116 -129.65 59.28
REMARK 500 LEU A 163 -16.72 160.53
REMARK 500 TYR A 172 111.94 -34.01
REMARK 500 ALA A 173 -14.49 135.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 172 ALA A 173 -146.08
REMARK 500 ALA A 173 MET A 174 137.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TRP A 145 24.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 517 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH A 532 DISTANCE = 5.50 ANGSTROMS
DBREF 4NS4 A -25 315 UNP Q1QEU6 Q1QEU6_PSYCK 1 315
SEQADV 4NS4 VAL A 316 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 GLU A 317 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 HIS A 318 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 HIS A 319 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 HIS A 320 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 HIS A 321 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 HIS A 322 UNP Q1QEU6 EXPRESSION TAG
SEQADV 4NS4 HIS A 323 UNP Q1QEU6 EXPRESSION TAG
SEQRES 1 A 323 MET LEU LEU LYS ARG LEU GLY LEU ALA THR LEU LEU SER
SEQRES 2 A 323 PHE SER VAL VAL GLY CYS THR THR ALA PRO ASN THR LEU
SEQRES 3 A 323 ALA ILE ASN THR THR GLN LYS ILE ILE GLN TYR GLU ARG
SEQRES 4 A 323 SER LYS SER ASP LEU THR THR GLN SER PHE THR LEU SER
SEQRES 5 A 323 SER GLY ASP LYS ILE VAL TYR ALA GLU ASN GLY ASN VAL
SEQRES 6 A 323 ALA GLY GLU PRO LEU LEU LEU VAL HIS GLY PHE GLY GLY
SEQRES 7 A 323 ASN LYS ASP ASN PHE THR ARG ILE ALA ARG GLN LEU GLU
SEQRES 8 A 323 ASN TYR ASN LEU ILE ILE PRO ASP LEU LEU GLY PHE GLY
SEQRES 9 A 323 ASP SER SER LYS PRO MET ALA ALA ASP TYR HIS SER GLU
SEQRES 10 A 323 ALA GLN ALA THR ARG LEU HIS GLU LEU LEU GLN ALA LYS
SEQRES 11 A 323 GLY LEU ALA SER SER ILE HIS VAL GLY GLY ASN SER MET
SEQRES 12 A 323 GLY GLY ALA ILE SER VAL ALA TYR ALA ALA LYS TYR PRO
SEQRES 13 A 323 LYS GLU VAL LYS SER LEU TRP LEU ILE ASP SER ALA GLY
SEQRES 14 A 323 PHE TRP SER ALA GLY VAL PRO LYS SER LEU GLU SER ALA
SEQRES 15 A 323 THR LEU GLU ASN ASN PRO LEU LEU VAL ASP LYS LYS GLU
SEQRES 16 A 323 ASP PHE TYR ALA MET TYR ASP PHE VAL MET SER LYS PRO
SEQRES 17 A 323 PRO TYR ILE PRO LYS SER VAL LYS ALA VAL PHE ALA GLN
SEQRES 18 A 323 GLU ARG ILE ALA ASN LYS ALA LEU GLU SER LYS ILE LEU
SEQRES 19 A 323 ALA GLN ILE VAL GLU ASP ASN VAL GLU GLN ARG ALA LYS
SEQRES 20 A 323 VAL ILE THR GLU TYR ASN ILE PRO THR LEU VAL VAL TRP
SEQRES 21 A 323 GLY GLU GLU ASP LYS VAL ILE LYS PRO GLU THR VAL THR
SEQRES 22 A 323 LEU ILE LYS GLU ILE ILE PRO GLN SER GLN VAL ILE THR
SEQRES 23 A 323 MET PRO LYS ILE GLY HIS VAL PRO MET ILE GLU ALA VAL
SEQRES 24 A 323 LYS ASP THR ALA ASN ASP TYR LYS ALA PHE ARG GLU GLY
SEQRES 25 A 323 LEU LYS ASN VAL GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *147(H2 O)
HELIX 1 1 THR A 4 SER A 16 1 13
HELIX 2 2 ASN A 53 ASN A 56 5 4
HELIX 3 3 PHE A 57 ARG A 62 1 6
HELIX 4 4 HIS A 89 LYS A 104 1 16
HELIX 5 5 MET A 117 TYR A 129 1 13
HELIX 6 6 LYS A 168 TYR A 172 5 5
HELIX 7 7 ALA A 173 MET A 179 1 7
HELIX 8 8 PRO A 186 ASN A 200 1 15
HELIX 9 9 ASN A 200 GLU A 213 1 14
HELIX 10 10 VAL A 216 TYR A 226 1 11
HELIX 11 11 GLU A 244 ILE A 253 1 10
HELIX 12 12 VAL A 267 ALA A 272 1 6
HELIX 13 13 ALA A 272 LEU A 313 1 16
SHEET 1 A 8 THR A 19 THR A 24 0
SHEET 2 A 8 LYS A 30 GLU A 35 -1 O GLU A 35 N THR A 19
SHEET 3 A 8 TYR A 67 PRO A 72 -1 O ILE A 71 N ALA A 34
SHEET 4 A 8 GLU A 42 VAL A 47 1 N LEU A 44 O ILE A 70
SHEET 5 A 8 ILE A 110 ASN A 115 1 O GLY A 113 N VAL A 47
SHEET 6 A 8 VAL A 133 ILE A 139 1 O ILE A 139 N GLY A 114
SHEET 7 A 8 THR A 230 GLY A 235 1 O VAL A 233 N LEU A 138
SHEET 8 A 8 GLN A 257 MET A 261 1 O GLN A 257 N VAL A 232
CRYST1 53.200 59.400 105.500 90.00 90.00 90.00 P 21 21 21 4
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 0.018797 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016835 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009479 0.00000
TER 2114 LYS A 314
MASTER 419 0 0 13 8 0 0 6 2244 1 0 25
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