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HEADER HYDROLASE 23-AUG-21 7V8X
TITLE CRYSTAL STRUCTURE OF PSEST3 COMPLEXED WITH PHENYLMETHYLSULFONYL
TITLE 2 FLUORIDE (PMSF)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PAENIBACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 58172;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SON,H.KIM,H.W.KIM
REVDAT 1 31-AUG-22 7V8X 0
JRNL AUTH J.SON,H.W.KIM
JRNL TITL CRYSTAL STRUCTURE OF PSEST3 COMPLEXED WITH
JRNL TITL 2 PHENYLMETHYLSULFONYL FLUORIDE (PMSF)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.11
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.480
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 35.1100 - 5.6400 0.99 1607 158 0.1978 0.2271
REMARK 3 2 5.6400 - 4.4800 1.00 1503 146 0.1762 0.2315
REMARK 3 3 4.4800 - 3.9100 1.00 1479 145 0.1886 0.2067
REMARK 3 4 3.9100 - 3.5600 1.00 1471 144 0.2150 0.2217
REMARK 3 5 3.5500 - 3.3000 1.00 1444 143 0.2163 0.2520
REMARK 3 6 3.3000 - 3.1100 1.00 1449 142 0.2292 0.2582
REMARK 3 7 3.1100 - 2.9500 1.00 1443 142 0.2534 0.3069
REMARK 3 8 2.9500 - 2.8200 1.00 1444 140 0.2679 0.3016
REMARK 3 9 2.8200 - 2.7100 1.00 1441 142 0.2705 0.2967
REMARK 3 10 2.7100 - 2.6200 1.00 1426 140 0.2742 0.3400
REMARK 3 11 2.6200 - 2.5400 1.00 1418 139 0.2945 0.3571
REMARK 3 12 2.5400 - 2.4700 1.00 1416 138 0.3229 0.3395
REMARK 3 13 2.4700 - 2.4000 1.00 1430 141 0.3372 0.3705
REMARK 3 14 2.4000 - 2.3400 1.00 1431 140 0.3639 0.3930
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7V8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1300024284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22425
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 30.40
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 14.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
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: PHENIX
REMARK 200 STARTING MODEL: 7V8U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 2.0 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
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 72.38650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.38650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.38650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.38650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 72.38650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.38650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 72.38650
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 72.38650
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 72.38650
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 72.38650
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 72.38650
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 72.38650
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 72.38650
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 72.38650
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 72.38650
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 72.38650
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 72.38650
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 72.38650
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 108.57975
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 36.19325
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 36.19325
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 108.57975
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 108.57975
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 108.57975
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 36.19325
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 36.19325
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 108.57975
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 36.19325
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 108.57975
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 36.19325
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 108.57975
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 36.19325
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 36.19325
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 36.19325
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 108.57975
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 36.19325
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 108.57975
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 108.57975
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 108.57975
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 36.19325
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 36.19325
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 108.57975
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 108.57975
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 36.19325
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 36.19325
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 36.19325
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 36.19325
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 108.57975
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 36.19325
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 108.57975
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 36.19325
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 108.57975
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 108.57975
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 108.57975
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 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 1
REMARK 465 GLY A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 158
REMARK 465 ALA A 159
REMARK 465 ALA A 160
REMARK 465 GLY A 161
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N LEU A 103 O HOH A 401 1.86
REMARK 500 O LEU A 99 O HOH A 401 1.93
REMARK 500 O HOH A 448 O HOH A 454 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 405 O HOH A 445 22554 2.15
REMARK 500 OH TYR A 257 OH TYR A 257 22554 2.15
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 LEU A 15 -168.47 -111.06
REMARK 500 ASN A 17 -118.40 53.24
REMARK 500 SER A 128 -53.51 75.47
REMARK 500 ASP A 224 32.37 -96.21
REMARK 500 LEU A 258 56.31 -92.69
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7V8X A 1 265 PDB 7V8X 7V8X 1 265
SEQRES 1 A 265 MET GLY ASN ALA VAL VAL VAL LYS LYS ASP PHE ARG ILE
SEQRES 2 A 265 ASP LEU GLU ASN GLU LEU PHE ILE ARG GLY GLU VAL THR
SEQRES 3 A 265 LEU VAL GLU ASP GLN ILE LYS LYS PRO VAL LEU VAL ILE
SEQRES 4 A 265 SER HIS GLY PHE ARG GLY TYR LYS ASP TRP GLY PHE TRP
SEQRES 5 A 265 PRO TYR VAL ALA ALA TRP PHE ALA GLU ARG GLY PHE TYR
SEQRES 6 A 265 VAL VAL HIS PHE ASP PHE SER ARG VAL GLY ALA LEU ASN
SEQRES 7 A 265 SER GLY ALA ASP GLU ALA SER VAL GLN LYS LEU SER THR
SEQRES 8 A 265 VAL SER ARG GLU LEU SER ASP LEU ASP ALA ILE LEU SER
SEQRES 9 A 265 ASN LEU ARG GLU HIS ARG LEU PRO LEU ALA GLU GLN ALA
SEQRES 10 A 265 GLU THR GLU ARG ILE SER LEU LEU GLY HIS SER ARG ALA
SEQRES 11 A 265 GLY GLY SER ASN ILE ILE PHE ALA ALA GLU HIS SER TYR
SEQRES 12 A 265 ILE GLY SER VAL ILE ALA TRP ASN GLY GLY PRO PRO PRO
SEQRES 13 A 265 LYS ALA ALA ALA GLY ASN PRO ASN PRO PHE ILE ASN ASP
SEQRES 14 A 265 ASP VAL GLU HIS ASN LYS GLN ARG PHE ASP THR ALA ARG
SEQRES 15 A 265 LEU LEU ALA SER LEU THR ALA PRO VAL LEU ILE ILE GLN
SEQRES 16 A 265 GLY GLY LYS ASP ARG GLU ALA LEU LEU GLU GLY GLN GLN
SEQRES 17 A 265 LEU LEU LYS GLU ALA ALA PRO ASN GLN THR TYR ILE SER
SEQRES 18 A 265 ILE PRO ASP ALA ASP HIS SER PHE GLY GLY GLU HIS PRO
SEQRES 19 A 265 PHE HIS HIS THR THR PRO TYR LEU GLU GLU ALA LEU GLU
SEQRES 20 A 265 VAL THR HIS SER PHE ILE THR LYS HIS TYR LEU GLU HIS
SEQRES 21 A 265 HIS HIS HIS HIS HIS
HET PMS A 301 10
HETNAM PMS PHENYLMETHANESULFONIC ACID
FORMUL 2 PMS C7 H8 O3 S
FORMUL 3 HOH *55(H2 O)
HELIX 1 AA1 PHE A 51 ARG A 62 1 12
HELIX 2 AA2 PHE A 71 SER A 79 1 9
HELIX 3 AA3 ASP A 82 LEU A 89 1 8
HELIX 4 AA4 THR A 91 GLU A 108 1 18
HELIX 5 AA5 LEU A 113 GLU A 115 5 3
HELIX 6 AA6 ARG A 129 GLU A 140 1 12
HELIX 7 AA7 ASN A 164 ASN A 174 1 11
HELIX 8 AA8 ASP A 179 LEU A 187 1 9
HELIX 9 AA9 ARG A 200 ALA A 214 1 15
HELIX 10 AB1 THR A 239 HIS A 256 1 18
SHEET 1 AA1 8 VAL A 7 ASP A 14 0
SHEET 2 AA1 8 PHE A 20 LEU A 27 -1 O LEU A 27 N VAL A 7
SHEET 3 AA1 8 TYR A 65 PHE A 69 -1 O HIS A 68 N GLU A 24
SHEET 4 AA1 8 LYS A 34 SER A 40 1 N LEU A 37 O VAL A 67
SHEET 5 AA1 8 ALA A 117 HIS A 127 1 O LEU A 125 N SER A 40
SHEET 6 AA1 8 ILE A 144 TRP A 150 1 O TRP A 150 N GLY A 126
SHEET 7 AA1 8 VAL A 191 GLY A 196 1 O ILE A 194 N ALA A 149
SHEET 8 AA1 8 THR A 218 ILE A 222 1 O ILE A 220 N ILE A 193
LINK OG SER A 128 S PMS A 301 1555 1555 1.47
CISPEP 1 HIS A 233 PRO A 234 0 -1.37
CRYST1 144.773 144.773 144.773 90.00 90.00 90.00 P 41 3 2 24
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 0.006907 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006907 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006907 0.00000
TER 2002 GLU A 259
MASTER 354 0 1 10 8 0 0 6 2066 1 11 21
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