HEADER HYDROLASE/HYDROLASE INHIBITOR 27-MAY-03 1PFG
TITLE STRATEGY TO DESIGN INHIBITORS: STRUCTURE OF A COMPLEX OF PROTEINASE K
TITLE 2 WITH A DESIGNED OCTAPEPTIDE INHIBITOR N-AC-PRO-ALA-PRO-PHE-DALA-ALA-
TITLE 3 ALA-ALA-NH2 AT 2.5A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEINASE K;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.21.64;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: N-AC-PAPFAAAA-NH2;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENGYODONTIUM ALBUM;
SOURCE 3 ORGANISM_TAXID: 37998;
SOURCE 4 TISSUE: LIMBER;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 OTHER_DETAILS: SOLUTION PHASE SYNTHESIS
KEYWDS PROTEINASE K, OCTAPEPTIDE, INHIBITOR, COMPLEX, HYDROLASE, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.K.SAXENA,T.P.SINGH,K.PETERS,S.FITTKAU,C.BETZEL
REVDAT 5 25-OCT-23 1PFG 1 REMARK
REVDAT 4 06-NOV-19 1PFG 1 JRNL SEQADV LINK
REVDAT 3 13-JUL-11 1PFG 1 VERSN
REVDAT 2 24-FEB-09 1PFG 1 VERSN
REVDAT 1 10-JUN-03 1PFG 0
JRNL AUTH A.K.SAXENA,T.P.SINGH,K.PETERS,S.FITTKAU,C.BETZEL
JRNL TITL STRATEGY TO DESIGN PEPTIDE INHIBITORS: STRUCTURE OF A
JRNL TITL 2 COMPLEX OF PROTEINASE K WITH A DESIGNED OCTAPEPTIDE
JRNL TITL 3 INHIBITOR N-AC-PRO-ALA-PRO-PHE-DALA-ALA-ALA-ALA-NH2 AT 2.5 A
JRNL TITL 4 RESOLUTION.
JRNL REF PROTEIN SCI. V. 5 2453 1996
JRNL REFN ISSN 0961-8368
JRNL PMID 8976553
JRNL DOI 10.1002/PRO.5560051207
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 7430
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 7430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2071
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.018 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 2.600 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE DISTANCE BETWEEN (B PHE 284) AND RESIDUE (B ALA 285) IS LONGER
REMARK 3 THAN
REMARK 3 THE PEPTIDE BOND DISTANCE AS THE PEPTIDE IS HYDOLYSED AT THIS
REMARK 3 POINT.
REMARK 4
REMARK 4 1PFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019293.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-OCT-95
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : CONVENTIONAL CU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : GRAPHITE MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, TRUNCATE
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7647
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 <I/SIGMA(I)> 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: AMORE
REMARK 200 STARTING MODEL: 1PEK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS, 1MM CACL2, 1M NAHNO3, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.85000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.77500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.92500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.77500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.92500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.85000
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: DIMERIC
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 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 GLN A 103 CG CD OE1 NE2
REMARK 470 ARG A 167 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 278 CG CD OE1 NE2
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 457 O HOH A 457 7465 0.69
REMARK 500 O HOH A 476 O HOH A 543 6455 0.81
REMARK 500 OD1 ASP A 112 O HOH A 339 7465 1.77
REMARK 500 CB SER A 216 O HOH A 511 6555 1.80
REMARK 500 OG SER A 150 O HOH A 423 7465 1.93
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 238 CG MET A 238 SD -0.159
REMARK 500 ALA B 285 N ALA B 285 CA -0.342
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 THR A 58 CB - CA - C ANGL. DEV. = -19.6 DEGREES
REMARK 500 SER A 63 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG A 80 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH1 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 VAL A 85 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 LEU A 90 CB - CG - CD1 ANGL. DEV. = -11.3 DEGREES
REMARK 500 LEU A 90 CB - CG - CD2 ANGL. DEV. = 13.9 DEGREES
REMARK 500 VAL A 93 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 THR A 106 N - CA - CB ANGL. DEV. = 12.5 DEGREES
REMARK 500 ASP A 112 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 117 CB - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 ASP A 117 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG A 121 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 LYS A 125 CB - CA - C ANGL. DEV. = -14.8 DEGREES
REMARK 500 LEU A 133 CA - CB - CG ANGL. DEV. = 19.6 DEGREES
REMARK 500 LEU A 133 CB - CG - CD2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 VAL A 157 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 PRO A 171 C - N - CA ANGL. DEV. = 51.6 DEGREES
REMARK 500 PRO A 171 C - N - CD ANGL. DEV. = -44.0 DEGREES
REMARK 500 PRO A 171 CA - N - CD ANGL. DEV. = -24.5 DEGREES
REMARK 500 PRO A 171 N - CA - CB ANGL. DEV. = 14.8 DEGREES
REMARK 500 PRO A 171 N - CD - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 GLU A 174 N - CA - C ANGL. DEV. = -19.3 DEGREES
REMARK 500 PRO A 175 N - CD - CG ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 188 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 218 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 SER A 224 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 SER A 224 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 VAL A 230 CB - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 LEU A 240 CA - CB - CG ANGL. DEV. = 16.9 DEGREES
REMARK 500 PHE B 284 CB - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ALA B 285 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 ALA B 288 N - CA - C ANGL. DEV. = 17.2 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 ASN A 5 46.97 34.69
REMARK 500 ALA A 29 49.90 39.95
REMARK 500 ASP A 39 -144.54 -167.28
REMARK 500 ILE A 42 115.12 -168.68
REMARK 500 GLU A 43 79.15 -64.74
REMARK 500 GLU A 50 27.53 35.99
REMARK 500 GLN A 54 137.59 -176.82
REMARK 500 LYS A 57 134.77 -173.83
REMARK 500 ALA A 164 -168.42 -115.96
REMARK 500 ALA A 166 2.22 -57.91
REMARK 500 PRO A 171 -41.39 132.90
REMARK 500 SER A 207 70.93 52.97
REMARK 500 SER A 216 -159.40 -106.16
REMARK 500 ARG A 218 141.36 -170.29
REMARK 500 ASN A 263 0.81 84.93
REMARK 500 ASN A 270 74.83 -114.73
REMARK 500 ALA B 282 -73.15 -149.81
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 CHAIN B OF N-AC-PAPFAAAA-NH2
DBREF 1PFG A 1 279 UNP P06873 PRTK_TRIAL 106 384
DBREF 1PFG B 280 289 PDB 1PFG 1PFG 280 289
SEQADV 1PFG VAL A 85 UNP P06873 ALA 190 CONFLICT
SEQRES 1 A 279 ALA ALA GLN THR ASN ALA PRO TRP GLY LEU ALA ARG ILE
SEQRES 2 A 279 SER SER THR SER PRO GLY THR SER THR TYR TYR TYR ASP
SEQRES 3 A 279 GLU SER ALA GLY GLN GLY SER CYS VAL TYR VAL ILE ASP
SEQRES 4 A 279 THR GLY ILE GLU ALA SER HIS PRO GLU PHE GLU GLY ARG
SEQRES 5 A 279 ALA GLN MET VAL LYS THR TYR TYR TYR SER SER ARG ASP
SEQRES 6 A 279 GLY ASN GLY HIS GLY THR HIS CYS ALA GLY THR VAL GLY
SEQRES 7 A 279 SER ARG THR TYR GLY VAL VAL LYS LYS THR GLN LEU PHE
SEQRES 8 A 279 GLY VAL LYS VAL LEU ASP ASP ASN GLY SER GLY GLN TYR
SEQRES 9 A 279 SER THR ILE ILE ALA GLY MET ASP PHE VAL ALA SER ASP
SEQRES 10 A 279 LYS ASN ASN ARG ASN CYS PRO LYS GLY VAL VAL ALA SER
SEQRES 11 A 279 LEU SER LEU GLY GLY GLY TYR SER SER SER VAL ASN SER
SEQRES 12 A 279 ALA ALA ALA ARG LEU GLN SER SER GLY VAL MET VAL ALA
SEQRES 13 A 279 VAL ALA ALA GLY ASN ASN ASN ALA ASP ALA ARG ASN TYR
SEQRES 14 A 279 SER PRO ALA SER GLU PRO SER VAL CYS THR VAL GLY ALA
SEQRES 15 A 279 SER ASP ARG TYR ASP ARG ARG SER SER PHE SER ASN TYR
SEQRES 16 A 279 GLY SER VAL LEU ASP ILE PHE GLY PRO GLY THR SER ILE
SEQRES 17 A 279 LEU SER THR TRP ILE GLY GLY SER THR ARG SER ILE SER
SEQRES 18 A 279 GLY THR SER MET ALA THR PRO HIS VAL ALA GLY LEU ALA
SEQRES 19 A 279 ALA TYR LEU MET THR LEU GLY LYS THR THR ALA ALA SER
SEQRES 20 A 279 ALA CYS ARG TYR ILE ALA ASP THR ALA ASN LYS GLY ASP
SEQRES 21 A 279 LEU SER ASN ILE PRO PHE GLY THR VAL ASN LEU LEU ALA
SEQRES 22 A 279 TYR ASN ASN TYR GLN ALA
SEQRES 1 B 10 ACE PRO ALA PRO PHE ALA ALA ALA ALA NH2
HET ACE B 280 3
HET NH2 B 289 1
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 2 ACE C2 H4 O
FORMUL 2 NH2 H2 N
FORMUL 3 HOH *206(H2 O)
HELIX 1 1 PRO A 7 SER A 14 1 8
HELIX 2 2 HIS A 46 GLU A 50 5 5
HELIX 3 3 GLY A 68 SER A 79 1 12
HELIX 4 4 GLN A 103 LYS A 118 1 16
HELIX 5 5 ASN A 119 ARG A 121 5 3
HELIX 6 6 SER A 138 SER A 151 1 14
HELIX 7 7 ASP A 165 ARG A 167 5 3
HELIX 8 8 ILE A 213 GLY A 215 5 3
HELIX 9 9 ALA A 226 LEU A 240 1 15
HELIX 10 10 SER A 247 THR A 255 1 9
SHEET 1 A 2 ALA A 2 GLN A 3 0
SHEET 2 A 2 TYR A 23 TYR A 24 -1 O TYR A 23 N GLN A 3
SHEET 1 B 7 ALA A 53 THR A 58 0
SHEET 2 B 7 GLN A 89 LYS A 94 1 O LYS A 94 N LYS A 57
SHEET 3 B 7 CYS A 34 ASP A 39 1 N VAL A 35 O GLN A 89
SHEET 4 B 7 VAL A 127 LEU A 131 1 O SER A 130 N TYR A 36
SHEET 5 B 7 MET A 154 ALA A 158 1 O MET A 154 N ALA A 129
SHEET 6 B 7 CYS A 178 SER A 183 1 O VAL A 180 N VAL A 157
SHEET 7 B 7 ILE A 201 PRO A 204 1 O ILE A 201 N GLY A 181
SHEET 1 C 2 GLY A 135 GLY A 136 0
SHEET 2 C 2 TYR A 169 SER A 170 -1 O SER A 170 N GLY A 135
SHEET 1 D 2 ILE A 208 TRP A 212 0
SHEET 2 D 2 SER A 216 ILE A 220 -1 O ILE A 220 N ILE A 208
SHEET 1 E 2 ASN A 257 LYS A 258 0
SHEET 2 E 2 LEU A 271 LEU A 272 -1 O LEU A 272 N ASN A 257
SSBOND 1 CYS A 34 CYS A 123 1555 1555 2.02
SSBOND 2 CYS A 178 CYS A 249 1555 1555 2.00
LINK C ACE B 280 N PRO B 281 1555 1555 1.35
LINK C ALA B 288 N NH2 B 289 1555 1555 1.33
SITE 1 AC1 23 ASN A 67 HIS A 69 GLY A 100 LEU A 133
SITE 2 AC1 23 GLY A 134 GLY A 135 ALA A 158 ASN A 161
SITE 3 AC1 23 TRP A 212 ILE A 220 SER A 221 THR A 223
SITE 4 AC1 23 SER A 224 MET A 225 HOH A 530 HOH A 532
SITE 5 AC1 23 HOH A 601 HOH B 506 HOH B 514 HOH B 542
SITE 6 AC1 23 HOH B 547 HOH B 600 HOH B 602
CRYST1 68.000 68.000 107.700 90.00 90.00 90.00 P 43 21 2 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 0.014706 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009285 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
