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HEADER HYDROLASE 26-MAR-09 3GRO
TITLE HUMAN PALMITOYL-PROTEIN THIOESTERASE 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PALMITOYL-PROTEIN THIOESTERASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PPT-1, PALMITOYL-PROTEIN HYDROLASE 1;
COMPND 5 EC: 3.1.2.22;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PPT1, PPT;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC-C
KEYWDS NEURONAL CEROID LIPOFUSCINOSIS, NEURODEGENERATION,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, DISEASE MUTATION,
KEYWDS 3 DISULFIDE BOND, GLYCOPROTEIN, HYDROLASE, LYSOSOME,
KEYWDS 4 POLYMORPHISM, SENSORY TRANSDUCTION, VISION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DOBROVETSKY,A.SEITOVA,Y.TONG,W.TEMPEL,A.DONG,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,
AUTHOR 3 D.COSSAR,H.PARK,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 1 07-APR-09 3GRO 0
JRNL AUTH E.DOBROVETSKY,A.SEITOVA,Y.TONG,W.TEMPEL,A.DONG,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,
JRNL AUTH 3 A.BOCHKAREV,D.COSSAR,H.PARK
JRNL TITL HUMAN PALMITOYL-PROTEIN THIOESTERASE 1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 21649
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.695
REMARK 3 FREE R VALUE TEST SET COUNT : 1233
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) : 2.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.60
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1428
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4235
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.10000
REMARK 3 B22 (A**2) : -1.06100
REMARK 3 B33 (A**2) : -0.04000
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): 0.581
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.281
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.202
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.194
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4342 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2878 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5902 ; 1.081 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7023 ; 0.861 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 550 ; 5.644 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;36.039 ;24.792
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 693 ;14.941 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.237 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 651 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4887 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 862 ; 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): 2744 ; 1.022 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1119 ; 0.131 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4402 ; 1.801 ; 3.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1598 ; 1.045 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1500 ; 1.613 ; 3.000
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 : 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 : MASK BULK SOLVENT
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: REFINED INDIVIDUALLY. PROGRAMS
REMARK 3 COOT, MOLPROBITY HAVE ALSO BEEN USED IN REFINEMENT.
REMARK 4
REMARK 4 3GRO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97940
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21818
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.530
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 0.99300
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1EI9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3350, 0.2M AMMONIUM
REMARK 280 SULFATE, 0.1M SODIUM CACODYLATE. CRYOPROTECTANT: 9 PARTS
REMARK 280 RESERVOIR + 1 PART 80% GLYCEROL, PH 5.4, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 291K
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 26.85500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.58250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.32100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.58250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.85500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.32100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.8 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 ALA A 21
REMARK 465 ARG A 22
REMARK 465 ALA A 23
REMARK 465 LEU A 24
REMARK 465 GLN A 25
REMARK 465 HIS A 26
REMARK 465 LEU A 27
REMARK 465 ASP A 28
REMARK 465 PRO A 29
REMARK 465 GLU A 307
REMARK 465 PHE A 308
REMARK 465 VAL A 309
REMARK 465 GLU A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 ALA B 21
REMARK 465 ARG B 22
REMARK 465 ALA B 23
REMARK 465 LEU B 24
REMARK 465 GLN B 25
REMARK 465 HIS B 26
REMARK 465 LEU B 27
REMARK 465 ASP B 28
REMARK 465 PRO B 29
REMARK 465 PRO B 30
REMARK 465 GLY B 306
REMARK 465 GLU B 307
REMARK 465 PHE B 308
REMARK 465 VAL B 309
REMARK 465 GLU B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 HIS B 316
REMARK 465 HIS B 317
REMARK 465 HIS B 318
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 A 55 NZ
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 LYS A 61 CD CE NZ
REMARK 470 LYS A 74 CD CE NZ
REMARK 470 GLN A 107 CG CD OE1 NE2
REMARK 470 LYS A 174 CG CD CE NZ
REMARK 470 LYS A 191 CE NZ
REMARK 470 LYS A 223 CE NZ
REMARK 470 LYS A 253 CE NZ
REMARK 470 GLU A 294 CG CD OE1 OE2
REMARK 470 GLU A 295 CD OE1 OE2
REMARK 470 TYR A 298 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 55 NZ
REMARK 470 LYS B 56 CG CD CE NZ
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 LYS B 61 CG CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 LYS B 101 CG CD CE NZ
REMARK 470 GLN B 106 CG CD OE1 NE2
REMARK 470 LYS B 174 CE NZ
REMARK 470 GLU B 178 CG CD OE1 OE2
REMARK 470 LYS B 191 CE NZ
REMARK 470 ASP B 193 CG OD1 OD2
REMARK 470 GLU B 213 CG CD OE1 OE2
REMARK 470 LYS B 217 CD CE NZ
REMARK 470 LYS B 224 CD CE NZ
REMARK 470 ARG B 248 NE CZ NH1 NH2
REMARK 470 LYS B 253 CG CD CE NZ
REMARK 470 GLU B 254 CG CD OE1 OE2
REMARK 470 LYS B 272 CE NZ
REMARK 470 GLU B 273 CG CD OE1 OE2
REMARK 470 GLU B 294 CG CD OE1 OE2
REMARK 470 GLU B 295 CG CD OE1 OE2
REMARK 470 TYR B 298 CG CD1 CD2 CE1 CE2 CZ OH
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 115 -133.24 51.62
REMARK 500 PHE A 201 -73.48 -129.00
REMARK 500 ALA A 252 40.22 -141.38
REMARK 500 LYS A 253 -55.62 -122.04
REMARK 500 LEU A 290 14.47 58.59
REMARK 500 CYS B 46 30.77 -142.57
REMARK 500 ILE B 72 78.37 -105.64
REMARK 500 SER B 115 -129.40 55.30
REMARK 500 SER B 156 31.60 -149.13
REMARK 500 LYS B 191 54.62 -119.18
REMARK 500 PHE B 201 -69.55 -132.05
REMARK 500 ALA B 252 34.74 -142.43
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3GRO A 22 306 UNP P50897 PPT1_HUMAN 22 306
DBREF 3GRO B 22 306 UNP P50897 PPT1_HUMAN 22 306
SEQADV 3GRO ALA A 21 UNP P50897 EXPRESSION TAG
SEQADV 3GRO GLU A 307 UNP P50897 EXPRESSION TAG
SEQADV 3GRO PHE A 308 UNP P50897 EXPRESSION TAG
SEQADV 3GRO VAL A 309 UNP P50897 EXPRESSION TAG
SEQADV 3GRO GLU A 310 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 311 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 312 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 313 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 314 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 315 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 316 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 317 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS A 318 UNP P50897 EXPRESSION TAG
SEQADV 3GRO ALA B 21 UNP P50897 EXPRESSION TAG
SEQADV 3GRO GLU B 307 UNP P50897 EXPRESSION TAG
SEQADV 3GRO PHE B 308 UNP P50897 EXPRESSION TAG
SEQADV 3GRO VAL B 309 UNP P50897 EXPRESSION TAG
SEQADV 3GRO GLU B 310 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 311 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 312 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 313 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 314 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 315 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 316 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 317 UNP P50897 EXPRESSION TAG
SEQADV 3GRO HIS B 318 UNP P50897 EXPRESSION TAG
SEQRES 1 A 298 ALA ARG ALA LEU GLN HIS LEU ASP PRO PRO ALA PRO LEU
SEQRES 2 A 298 PRO LEU VAL ILE TRP HIS GLY MSE GLY ASP SER CYS CYS
SEQRES 3 A 298 ASN PRO LEU SER MSE GLY ALA ILE LYS LYS MSE VAL GLU
SEQRES 4 A 298 LYS LYS ILE PRO GLY ILE TYR VAL LEU SER LEU GLU ILE
SEQRES 5 A 298 GLY LYS THR LEU MSE GLU ASP VAL GLU ASN SER PHE PHE
SEQRES 6 A 298 LEU ASN VAL ASN SER GLN VAL THR THR VAL CYS GLN ALA
SEQRES 7 A 298 LEU ALA LYS ASP PRO LYS LEU GLN GLN GLY TYR ASN ALA
SEQRES 8 A 298 MSE GLY PHE SER GLN GLY GLY GLN PHE LEU ARG ALA VAL
SEQRES 9 A 298 ALA GLN ARG CYS PRO SER PRO PRO MSE ILE ASN LEU ILE
SEQRES 10 A 298 SER VAL GLY GLY GLN HIS GLN GLY VAL PHE GLY LEU PRO
SEQRES 11 A 298 ARG CYS PRO GLY GLU SER SER HIS ILE CYS ASP PHE ILE
SEQRES 12 A 298 ARG LYS THR LEU ASN ALA GLY ALA TYR SER LYS VAL VAL
SEQRES 13 A 298 GLN GLU ARG LEU VAL GLN ALA GLU TYR TRP HIS ASP PRO
SEQRES 14 A 298 ILE LYS GLU ASP VAL TYR ARG ASN HIS SER ILE PHE LEU
SEQRES 15 A 298 ALA ASP ILE ASN GLN GLU ARG GLY ILE ASN GLU SER TYR
SEQRES 16 A 298 LYS LYS ASN LEU MSE ALA LEU LYS LYS PHE VAL MSE VAL
SEQRES 17 A 298 LYS PHE LEU ASN ASP SER ILE VAL ASP PRO VAL ASP SER
SEQRES 18 A 298 GLU TRP PHE GLY PHE TYR ARG SER GLY GLN ALA LYS GLU
SEQRES 19 A 298 THR ILE PRO LEU GLN GLU THR SER LEU TYR THR GLN ASP
SEQRES 20 A 298 ARG LEU GLY LEU LYS GLU MSE ASP ASN ALA GLY GLN LEU
SEQRES 21 A 298 VAL PHE LEU ALA THR GLU GLY ASP HIS LEU GLN LEU SER
SEQRES 22 A 298 GLU GLU TRP PHE TYR ALA HIS ILE ILE PRO PHE LEU GLY
SEQRES 23 A 298 GLU PHE VAL GLU HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 298 ALA ARG ALA LEU GLN HIS LEU ASP PRO PRO ALA PRO LEU
SEQRES 2 B 298 PRO LEU VAL ILE TRP HIS GLY MSE GLY ASP SER CYS CYS
SEQRES 3 B 298 ASN PRO LEU SER MSE GLY ALA ILE LYS LYS MSE VAL GLU
SEQRES 4 B 298 LYS LYS ILE PRO GLY ILE TYR VAL LEU SER LEU GLU ILE
SEQRES 5 B 298 GLY LYS THR LEU MSE GLU ASP VAL GLU ASN SER PHE PHE
SEQRES 6 B 298 LEU ASN VAL ASN SER GLN VAL THR THR VAL CYS GLN ALA
SEQRES 7 B 298 LEU ALA LYS ASP PRO LYS LEU GLN GLN GLY TYR ASN ALA
SEQRES 8 B 298 MSE GLY PHE SER GLN GLY GLY GLN PHE LEU ARG ALA VAL
SEQRES 9 B 298 ALA GLN ARG CYS PRO SER PRO PRO MSE ILE ASN LEU ILE
SEQRES 10 B 298 SER VAL GLY GLY GLN HIS GLN GLY VAL PHE GLY LEU PRO
SEQRES 11 B 298 ARG CYS PRO GLY GLU SER SER HIS ILE CYS ASP PHE ILE
SEQRES 12 B 298 ARG LYS THR LEU ASN ALA GLY ALA TYR SER LYS VAL VAL
SEQRES 13 B 298 GLN GLU ARG LEU VAL GLN ALA GLU TYR TRP HIS ASP PRO
SEQRES 14 B 298 ILE LYS GLU ASP VAL TYR ARG ASN HIS SER ILE PHE LEU
SEQRES 15 B 298 ALA ASP ILE ASN GLN GLU ARG GLY ILE ASN GLU SER TYR
SEQRES 16 B 298 LYS LYS ASN LEU MSE ALA LEU LYS LYS PHE VAL MSE VAL
SEQRES 17 B 298 LYS PHE LEU ASN ASP SER ILE VAL ASP PRO VAL ASP SER
SEQRES 18 B 298 GLU TRP PHE GLY PHE TYR ARG SER GLY GLN ALA LYS GLU
SEQRES 19 B 298 THR ILE PRO LEU GLN GLU THR SER LEU TYR THR GLN ASP
SEQRES 20 B 298 ARG LEU GLY LEU LYS GLU MSE ASP ASN ALA GLY GLN LEU
SEQRES 21 B 298 VAL PHE LEU ALA THR GLU GLY ASP HIS LEU GLN LEU SER
SEQRES 22 B 298 GLU GLU TRP PHE TYR ALA HIS ILE ILE PRO PHE LEU GLY
SEQRES 23 B 298 GLU PHE VAL GLU HIS HIS HIS HIS HIS HIS HIS HIS
MODRES 3GRO MSE A 41 MET SELENOMETHIONINE
MODRES 3GRO MSE A 51 MET SELENOMETHIONINE
MODRES 3GRO MSE A 57 MET SELENOMETHIONINE
MODRES 3GRO MSE A 77 MET SELENOMETHIONINE
MODRES 3GRO MSE A 112 MET SELENOMETHIONINE
MODRES 3GRO MSE A 133 MET SELENOMETHIONINE
MODRES 3GRO MSE A 220 MET SELENOMETHIONINE
MODRES 3GRO MSE A 227 MET SELENOMETHIONINE
MODRES 3GRO MSE A 274 MET SELENOMETHIONINE
MODRES 3GRO MSE B 41 MET SELENOMETHIONINE
MODRES 3GRO MSE B 51 MET SELENOMETHIONINE
MODRES 3GRO MSE B 57 MET SELENOMETHIONINE
MODRES 3GRO MSE B 77 MET SELENOMETHIONINE
MODRES 3GRO MSE B 112 MET SELENOMETHIONINE
MODRES 3GRO MSE B 133 MET SELENOMETHIONINE
MODRES 3GRO MSE B 220 MET SELENOMETHIONINE
MODRES 3GRO MSE B 227 MET SELENOMETHIONINE
MODRES 3GRO MSE B 274 MET SELENOMETHIONINE
HET MSE A 41 8
HET MSE A 51 8
HET MSE A 57 8
HET MSE A 77 8
HET MSE A 112 8
HET MSE A 133 8
HET MSE A 220 8
HET MSE A 227 8
HET MSE A 274 8
HET MSE B 41 8
HET MSE B 51 8
HET MSE B 57 8
HET MSE B 77 8
HET MSE B 112 8
HET MSE B 133 8
HET MSE B 220 8
HET MSE B 227 8
HET MSE B 274 8
HET UNX A 3 1
HET UNX A 4 1
HET UNX B 1 1
HET UNX B 2 1
HETNAM MSE SELENOMETHIONINE
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 3 UNX 4(X)
FORMUL 7 HOH *24(H2 O)
HELIX 1 1 SER A 50 ILE A 62 1 13
HELIX 2 2 THR A 75 LEU A 86 1 12
HELIX 3 3 ASN A 87 ASP A 102 1 16
HELIX 4 4 PRO A 103 GLN A 106 5 4
HELIX 5 5 SER A 115 CYS A 128 1 14
HELIX 6 6 SER A 156 ALA A 171 1 16
HELIX 7 7 SER A 173 GLU A 178 1 6
HELIX 8 8 LEU A 180 TRP A 186 5 7
HELIX 9 9 LYS A 191 SER A 199 1 9
HELIX 10 10 PHE A 201 ASN A 206 1 6
HELIX 11 11 ASN A 212 ALA A 221 1 10
HELIX 12 12 PRO A 238 PHE A 244 5 7
HELIX 13 13 PRO A 257 GLU A 260 5 4
HELIX 14 14 THR A 261 GLN A 266 1 6
HELIX 15 15 GLY A 270 ALA A 277 1 8
HELIX 16 16 SER A 293 ILE A 301 1 9
HELIX 17 17 ILE A 302 GLY A 306 5 5
HELIX 18 18 SER B 50 ILE B 62 1 13
HELIX 19 19 THR B 75 LEU B 86 1 12
HELIX 20 20 ASN B 87 ASP B 102 1 16
HELIX 21 21 PRO B 103 GLN B 106 5 4
HELIX 22 22 GLN B 116 CYS B 128 1 13
HELIX 23 23 SER B 156 ALA B 171 1 16
HELIX 24 24 SER B 173 GLU B 178 1 6
HELIX 25 25 LEU B 180 TYR B 185 1 6
HELIX 26 26 LYS B 191 SER B 199 1 9
HELIX 27 27 PHE B 201 ASN B 206 1 6
HELIX 28 28 ASN B 212 MSE B 220 1 9
HELIX 29 29 PRO B 238 PHE B 244 5 7
HELIX 30 30 PRO B 257 GLU B 260 5 4
HELIX 31 31 THR B 261 GLN B 266 1 6
HELIX 32 32 GLY B 270 ALA B 277 1 8
HELIX 33 33 SER B 293 ILE B 301 1 9
HELIX 34 34 ILE B 302 LEU B 305 5 4
SHEET 1 A 6 VAL A 67 SER A 69 0
SHEET 2 A 6 LEU A 35 TRP A 38 1 N ILE A 37 O LEU A 68
SHEET 3 A 6 TYR A 109 PHE A 114 1 O ASN A 110 N VAL A 36
SHEET 4 A 6 MSE A 133 VAL A 139 1 O VAL A 139 N GLY A 113
SHEET 5 A 6 LYS A 224 PHE A 230 1 O VAL A 226 N SER A 138
SHEET 6 A 6 LEU A 280 THR A 285 1 O VAL A 281 N MSE A 227
SHEET 1 B 2 PHE A 246 TYR A 247 0
SHEET 2 B 2 THR A 255 ILE A 256 -1 O ILE A 256 N PHE A 246
SHEET 1 C 6 VAL B 67 SER B 69 0
SHEET 2 C 6 LEU B 35 TRP B 38 1 N ILE B 37 O LEU B 68
SHEET 3 C 6 TYR B 109 PHE B 114 1 O MSE B 112 N VAL B 36
SHEET 4 C 6 MSE B 133 VAL B 139 1 O VAL B 139 N GLY B 113
SHEET 5 C 6 LYS B 224 PHE B 230 1 O VAL B 226 N SER B 138
SHEET 6 C 6 LEU B 280 THR B 285 1 O VAL B 281 N MSE B 227
SHEET 1 D 2 PHE B 246 TYR B 247 0
SHEET 2 D 2 THR B 255 ILE B 256 -1 O ILE B 256 N PHE B 246
SSBOND 1 CYS A 45 CYS A 46 1555 1555 2.09
SSBOND 2 CYS A 96 CYS A 128 1555 1555 2.04
SSBOND 3 CYS A 152 CYS A 160 1555 1555 2.04
SSBOND 4 CYS B 45 CYS B 46 1555 1555 2.08
SSBOND 5 CYS B 96 CYS B 128 1555 1555 2.02
SSBOND 6 CYS B 152 CYS B 160 1555 1555 2.07
LINK C GLY A 40 N MSE A 41 1555 1555 1.32
LINK C MSE A 41 N GLY A 42 1555 1555 1.33
LINK C SER A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N GLY A 52 1555 1555 1.34
LINK C LYS A 56 N MSE A 57 1555 1555 1.33
LINK C MSE A 57 N VAL A 58 1555 1555 1.33
LINK C LEU A 76 N MSE A 77 1555 1555 1.33
LINK C MSE A 77 N GLU A 78 1555 1555 1.34
LINK C ALA A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N GLY A 113 1555 1555 1.33
LINK C PRO A 132 N MSE A 133 1555 1555 1.32
LINK C MSE A 133 N ILE A 134 1555 1555 1.34
LINK C LEU A 219 N MSE A 220 1555 1555 1.33
LINK C MSE A 220 N ALA A 221 1555 1555 1.34
LINK C VAL A 226 N MSE A 227 1555 1555 1.33
LINK C MSE A 227 N VAL A 228 1555 1555 1.33
LINK C GLU A 273 N MSE A 274 1555 1555 1.33
LINK C MSE A 274 N ASP A 275 1555 1555 1.33
LINK C GLY B 40 N MSE B 41 1555 1555 1.32
LINK C MSE B 41 N GLY B 42 1555 1555 1.33
LINK C SER B 50 N MSE B 51 1555 1555 1.34
LINK C MSE B 51 N GLY B 52 1555 1555 1.33
LINK C LYS B 56 N MSE B 57 1555 1555 1.33
LINK C MSE B 57 N VAL B 58 1555 1555 1.33
LINK C LEU B 76 N MSE B 77 1555 1555 1.33
LINK C MSE B 77 N GLU B 78 1555 1555 1.33
LINK C ALA B 111 N MSE B 112 1555 1555 1.34
LINK C MSE B 112 N GLY B 113 1555 1555 1.33
LINK C PRO B 132 N MSE B 133 1555 1555 1.33
LINK C MSE B 133 N ILE B 134 1555 1555 1.33
LINK C LEU B 219 N MSE B 220 1555 1555 1.34
LINK C MSE B 220 N ALA B 221 1555 1555 1.34
LINK C VAL B 226 N MSE B 227 1555 1555 1.33
LINK C MSE B 227 N VAL B 228 1555 1555 1.33
LINK C GLU B 273 N MSE B 274 1555 1555 1.33
LINK C MSE B 274 N ASP B 275 1555 1555 1.33
CISPEP 1 SER A 130 PRO A 131 0 3.33
CISPEP 2 ASP A 237 PRO A 238 0 0.34
CISPEP 3 SER B 130 PRO B 131 0 -3.20
CISPEP 4 ASP B 237 PRO B 238 0 -4.92
CRYST1 53.710 90.642 129.165 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 0.018619 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011032 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007742 0.00000
TER 2142 GLY A 306
TER 4237 LEU B 305
MASTER 357 0 22 34 16 0 0 6 4263 2 192 46
END |