HEADER ALPHA-BETA STRUCTURE 12-MAR-99 1QAH
TITLE CRYSTAL STRUCTURE OF PERCHLORIC ACID SOLUBLE PROTEIN-A TRANSLATIONAL
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERCHLORIC ACID SOLUBLE PROTEIN;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: LIVER, KIDNEY
KEYWDS ALPHA-BETA STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.DJINOVIC CARUGO,T.OKA
REVDAT 5 14-FEB-24 1QAH 1 REMARK
REVDAT 4 28-JUL-21 1QAH 1 REMARK
REVDAT 3 13-JUL-11 1QAH 1 VERSN
REVDAT 2 24-FEB-09 1QAH 1 VERSN
REVDAT 1 09-MAR-04 1QAH 0
JRNL AUTH K.DJINOVIC CARUGO,T.OKA
JRNL TITL CRYSTAL STRUCTURE OF PERCHLORIC ACID SOLUBLE PROTEIN-A
JRNL TITL 2 TRANSLATIONAL INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22116
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1946
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.10
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.015 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.037 ; 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: NULL
REMARK 4
REMARK 4 1QAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000009305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9183
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22619
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 63.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.340
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.93
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
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: NULL
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP, PH 4.5,
REMARK 280 293K, PEG 8000, SODIUM ACETATE, AMMONIUM SULPHATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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
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 44.87150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.87150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.87150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.87150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.87150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.87150
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 44.87150
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 44.87150
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 44.87150
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 44.87150
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 44.87150
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 44.87150
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 44.87150
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 44.87150
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 44.87150
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 44.87150
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 44.87150
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 44.87150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 0.000000 1.000000 -44.87150
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 44.87150
REMARK 350 BIOMT3 2 0.000000 -1.000000 0.000000 89.74300
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 44.87150
REMARK 350 BIOMT2 3 0.000000 0.000000 -1.000000 89.74300
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 44.87150
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
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 BIOMT1 2 0.000000 0.000000 -1.000000 44.87150
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 44.87150
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 -44.87150
REMARK 350 BIOMT3 3 -1.000000 0.000000 0.000000 44.87150
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 322 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 323 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 324 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 325 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 327 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 311 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 312 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 313 LIES ON A SPECIAL POSITION.
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 THR A 133
REMARK 465 ALA A 134
REMARK 465 GLY A 135
REMARK 465 LEU A 136
REMARK 465 THR B 133
REMARK 465 ALA B 134
REMARK 465 GLY B 135
REMARK 465 LEU B 136
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 GLY A 129 CA GLY A 129 C -0.114
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 SER A 1 CA - C - O ANGL. DEV. = -13.3 DEGREES
REMARK 500 SER A 1 CA - C - N ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 5 N - CA - CB ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG A 5 CA - CB - CG ANGL. DEV. = 23.9 DEGREES
REMARK 500 ASP A 27 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 TYR A 31 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 GLU A 52 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 PHE A 72 CB - CG - CD2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 PHE A 72 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR A 109 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 TYR A 109 CG - CD1 - CE1 ANGL. DEV. = -14.8 DEGREES
REMARK 500 TYR A 109 CD1 - CE1 - CZ ANGL. DEV. = 22.9 DEGREES
REMARK 500 TYR A 109 CE1 - CZ - CE2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 ARG A 119 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLU A 121 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLY A 129 N - CA - C ANGL. DEV. = 46.3 DEGREES
REMARK 500 PRO A 130 N - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 ARG B 5 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 28 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 28 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 28 NE - CZ - NH2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 TYR B 95 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR B 109 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TYR B 109 CB - CG - CD1 ANGL. DEV. = 5.4 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 ASP A 27 -103.29 60.80
REMARK 500 ASN A 102 99.25 -62.88
REMARK 500 ILE B 17 106.72 -48.33
REMARK 500 ALA B 19 -175.26 -65.09
REMARK 500 TYR B 20 149.48 58.28
REMARK 500 ASP B 27 -108.76 65.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 108 12.03
REMARK 500 LEU B 58 -10.36
REMARK 500 GLN B 128 -13.65
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QAH A 1 136 UNP P52759 UK14_RAT 1 136
DBREF 1QAH B 1 136 UNP P52759 UK14_RAT 1 136
SEQRES 1 A 136 SER SER ILE ILE ARG LYS VAL ILE SER THR SER LYS ALA
SEQRES 2 A 136 PRO ALA ALA ILE GLY ALA TYR SER GLN ALA VAL LEU VAL
SEQRES 3 A 136 ASP ARG THR ILE TYR VAL SER GLY GLN ILE GLY MET ASP
SEQRES 4 A 136 PRO SER SER GLY GLN LEU VAL PRO GLY GLY VAL ALA GLU
SEQRES 5 A 136 GLU ALA LYS GLN ALA LEU LYS ASN LEU GLY GLU ILE LEU
SEQRES 6 A 136 LYS ALA ALA GLY CYS ASP PHE THR ASN VAL VAL LYS THR
SEQRES 7 A 136 THR VAL LEU LEU ALA ASP ILE ASN ASP PHE GLY THR VAL
SEQRES 8 A 136 ASN GLU ILE TYR LYS THR TYR PHE GLN GLY ASN LEU PRO
SEQRES 9 A 136 ALA ARG ALA ALA TYR GLN VAL ALA ALA LEU PRO LYS GLY
SEQRES 10 A 136 SER ARG ILE GLU ILE GLU ALA ILE ALA VAL GLN GLY PRO
SEQRES 11 A 136 PHE THR THR ALA GLY LEU
SEQRES 1 B 136 SER SER ILE ILE ARG LYS VAL ILE SER THR SER LYS ALA
SEQRES 2 B 136 PRO ALA ALA ILE GLY ALA TYR SER GLN ALA VAL LEU VAL
SEQRES 3 B 136 ASP ARG THR ILE TYR VAL SER GLY GLN ILE GLY MET ASP
SEQRES 4 B 136 PRO SER SER GLY GLN LEU VAL PRO GLY GLY VAL ALA GLU
SEQRES 5 B 136 GLU ALA LYS GLN ALA LEU LYS ASN LEU GLY GLU ILE LEU
SEQRES 6 B 136 LYS ALA ALA GLY CYS ASP PHE THR ASN VAL VAL LYS THR
SEQRES 7 B 136 THR VAL LEU LEU ALA ASP ILE ASN ASP PHE GLY THR VAL
SEQRES 8 B 136 ASN GLU ILE TYR LYS THR TYR PHE GLN GLY ASN LEU PRO
SEQRES 9 B 136 ALA ARG ALA ALA TYR GLN VAL ALA ALA LEU PRO LYS GLY
SEQRES 10 B 136 SER ARG ILE GLU ILE GLU ALA ILE ALA VAL GLN GLY PRO
SEQRES 11 B 136 PHE THR THR ALA GLY LEU
FORMUL 3 HOH *379(H2 O)
HELIX 1 1 VAL A 50 ALA A 67 1 18
HELIX 2 2 PHE A 72 ASN A 74 5 3
HELIX 3 3 ILE A 85 ASP A 87 5 3
HELIX 4 4 PHE A 88 LYS A 96 1 9
HELIX 5 5 PRO A 115 GLY A 117 5 3
HELIX 6 6 VAL B 50 ALA B 67 1 18
HELIX 7 7 PHE B 72 ASN B 74 5 3
HELIX 8 8 ILE B 85 ASP B 87 5 3
HELIX 9 9 PHE B 88 LYS B 96 1 9
HELIX 10 10 PRO B 115 GLY B 117 5 3
SHEET 1 A 6 ARG A 5 ILE A 8 0
SHEET 2 A 6 ALA A 23 VAL A 26 -1 O LEU A 25 N LYS A 6
SHEET 3 A 6 THR A 29 GLN A 35 -1 O THR A 29 N VAL A 26
SHEET 4 A 6 ILE A 120 VAL A 127 -1 O ALA A 126 N ILE A 30
SHEET 5 A 6 VAL A 75 LEU A 82 -1 N LEU A 81 O GLU A 121
SHEET 6 A 6 ALA A 105 GLN A 110 1 O ALA A 107 N VAL A 80
SHEET 1 B 6 ARG B 5 ILE B 8 0
SHEET 2 B 6 ALA B 23 VAL B 26 -1 O LEU B 25 N LYS B 6
SHEET 3 B 6 THR B 29 ILE B 36 -1 O THR B 29 N VAL B 26
SHEET 4 B 6 ILE B 120 VAL B 127 -1 O ALA B 126 N ILE B 30
SHEET 5 B 6 VAL B 75 LEU B 82 -1 N LEU B 81 O GLU B 121
SHEET 6 B 6 ALA B 105 GLN B 110 1 O ALA B 107 N VAL B 80
CRYST1 89.743 89.743 89.743 90.00 90.00 90.00 P 21 3 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 0.011140 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011140 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011140 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
