HEADER TRANSFERASE, PROTEIN BINDING 26-MAR-12 4ECC
TITLE CHIMERIC GST CONTAINING INSERTS OF KININOGEN PEPTIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHIMERIC PROTEIN BETWEEN GSHKT10 AND DOMAIN 5 OF KININOGEN-
COMPND 3 1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 1-49, KINONOGEN 498-510, 50-228;
COMPND 6 SYNONYM: GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, GST 26,
COMPND 7 SJ26 ANTIGEN, SJGST/ALPHA-2-THIOL PROTEINASE INHIBITOR, FITZGERALD
COMPND 8 FACTOR, HIGH MOLECULAR WEIGHT, KININOGEN, DOMAIN 5 OF HUMAN HIGH
COMPND 9 MOLECULAR WEIGHT KININOGEN;
COMPND 10 EC: 2.5.1.18;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHISTOSOMA JAPONICUM, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: BLOOD FLUKE, HUMAN;
SOURCE 4 ORGANISM_TAXID: 6182, 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS GST, DOMAIN 5 OF HUMAN HIGH MOLECULAR WEIGHT KININOGEN, BIOSYNTHETIC
KEYWDS 2 PROTEIN, TRANSFERASE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.AMBER,M.M.SERGEI,P.YI,R.RITA,Q.XIAOPING,P.-C.MARIANNE,
AUTHOR 2 C.M.WILLIAM,Y.VIVIEN,R.M.KEITH,A.K.ANTON
REVDAT 4 13-SEP-23 4ECC 1 REMARK
REVDAT 3 09-AUG-17 4ECC 1 SOURCE REMARK
REVDAT 2 19-SEP-12 4ECC 1 JRNL
REVDAT 1 16-MAY-12 4ECC 0
JRNL AUTH A.A.BENTLEY,S.M.MERKULOV,Y.PENG,R.ROZMARYNOWYCZ,X.QI,
JRNL AUTH 2 M.PUSZTAI-CAREY,W.C.MERRICK,V.C.YEE,K.R.MCCRAE,A.A.KOMAR
JRNL TITL CHIMERIC GLUTATHIONE S-TRANSFERASES CONTAINING INSERTS OF
JRNL TITL 2 KININOGEN PEPTIDES: POTENTIAL NOVEL PROTEIN THERAPEUTICS.
JRNL REF J.BIOL.CHEM. V. 287 22142 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22577144
JRNL DOI 10.1074/JBC.M112.372854
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 12158
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 626
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 884
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1682
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : -0.41000
REMARK 3 B33 (A**2) : 0.82000
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): 0.291
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.232
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.159
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.113
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1727 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2333 ; 1.363 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 5.437 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 79 ;35.727 ;24.051
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 312 ;13.957 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;21.447 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 246 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1302 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1027 ; 0.970 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1656 ; 1.820 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 700 ; 2.580 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 677 ; 4.135 ; 4.500
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4ECC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071438.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-08
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 : 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) : 0.97857
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR.
REMARK 200 LN2 COOLED FIRST CRYSTAL,
REMARK 200 SAGITTAL FOCUSING 2ND CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12806
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1M99
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (1)0.2 M AMMONIUM SULFATE, 0.1 M
REMARK 280 HEPES, 25% PEG 3350 (2)0.2 M LITHIUM SULFATE, 25% PEG 3350, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 29.04350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 46.26000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 46.26000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.56525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 46.26000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 46.26000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.52175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 46.26000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.26000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 43.56525
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 46.26000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.26000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 14.52175
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 29.04350
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -29.04350
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 371 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 MET A 1
REMARK 465 LYS A 40
REMARK 465 TRP A 41
REMARK 465 ARG A 42
REMARK 465 ASN A 43
REMARK 465 LYS A 44
REMARK 465 LYS A 45
REMARK 465 PHE A 46
REMARK 465 GLU A 47
REMARK 465 LEU A 48
REMARK 465 GLY A 49
REMARK 465 LYS A 50
REMARK 465 HIS A 51
REMARK 465 GLY A 52
REMARK 465 HIS A 53
REMARK 465 GLY A 54
REMARK 465 HIS A 55
REMARK 465 GLY A 56
REMARK 465 LYS A 57
REMARK 465 HIS A 58
REMARK 465 LYS A 59
REMARK 465 ASN A 60
REMARK 465 LYS A 61
REMARK 465 PRO A 230
REMARK 465 LYS A 231
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 18 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = 3.3 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 LYS A 11 -72.71 -62.91
REMARK 500 GLU A 37 35.17 -83.71
REMARK 500 PRO A 66 122.83 -34.30
REMARK 500 GLN A 80 112.94 73.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ECB RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CRYSTALLIZED SEQUENCE REPRESENTS A CHIMERIC CONSTRUCT.
REMARK 999 GLUTATHIONE S-TRANSFERASE CONTAINS A LINKER CORRESPONDING TO DOMAIN
REMARK 999 OF A HUMAN KININOGEN-1
DBREF 4ECC A 1 49 UNP P08515 GST26_SCHJA 1 49
DBREF 4ECC A 50 62 UNP P01042 KNG1_HUMAN 498 510
DBREF 4ECC A 63 228 UNP P08515 GST26_SCHJA 50 215
SEQRES 1 A 231 MET SER PRO ILE LEU GLY TYR TRP LYS ILE LYS GLY LEU
SEQRES 2 A 231 VAL GLN PRO THR ARG LEU LEU LEU GLU TYR LEU GLU GLU
SEQRES 3 A 231 LYS TYR GLU GLU HIS LEU TYR GLU ARG ASP GLU GLY ASP
SEQRES 4 A 231 LYS TRP ARG ASN LYS LYS PHE GLU LEU GLY LYS HIS GLY
SEQRES 5 A 231 HIS GLY HIS GLY LYS HIS LYS ASN LYS GLY LEU GLU PHE
SEQRES 6 A 231 PRO ASN LEU PRO TYR TYR ILE ASP GLY ASP VAL LYS LEU
SEQRES 7 A 231 THR GLN SER MET ALA ILE ILE ARG TYR ILE ALA ASP LYS
SEQRES 8 A 231 HIS ASN MET LEU GLY GLY CYS PRO LYS GLU ARG ALA GLU
SEQRES 9 A 231 ILE SER MET LEU GLU GLY ALA VAL LEU ASP ILE ARG TYR
SEQRES 10 A 231 GLY VAL SER ARG ILE ALA TYR SER LYS ASP PHE GLU THR
SEQRES 11 A 231 LEU LYS VAL ASP PHE LEU SER LYS LEU PRO GLU MET LEU
SEQRES 12 A 231 LYS MET PHE GLU ASP ARG LEU CYS HIS LYS THR TYR LEU
SEQRES 13 A 231 ASN GLY ASP HIS VAL THR HIS PRO ASP PHE MET LEU TYR
SEQRES 14 A 231 ASP ALA LEU ASP VAL VAL LEU TYR MET ASP PRO MET CYS
SEQRES 15 A 231 LEU ASP ALA PHE PRO LYS LEU VAL CYS PHE LYS LYS ARG
SEQRES 16 A 231 ILE GLU ALA ILE PRO GLN ILE ASP LYS TYR LEU LYS SER
SEQRES 17 A 231 SER LYS TYR ILE ALA TRP PRO LEU GLN GLY TRP GLN ALA
SEQRES 18 A 231 THR PHE GLY GLY GLY ASP HIS PRO PRO LYS
FORMUL 2 HOH *71(H2 O)
HELIX 1 1 LYS A 11 LEU A 13 5 3
HELIX 2 2 VAL A 14 LEU A 24 1 11
HELIX 3 3 GLN A 80 HIS A 92 1 13
HELIX 4 4 CYS A 98 TYR A 124 1 27
HELIX 5 5 ASP A 127 LEU A 150 1 24
HELIX 6 6 THR A 162 ASP A 179 1 18
HELIX 7 7 PHE A 186 ILE A 199 1 14
HELIX 8 8 ILE A 199 SER A 208 1 10
SHEET 1 A 4 GLU A 29 TYR A 33 0
SHEET 2 A 4 ILE A 4 TRP A 8 1 N TYR A 7 O HIS A 31
SHEET 3 A 4 TYR A 70 ASP A 73 -1 O TYR A 70 N GLY A 6
SHEET 4 A 4 VAL A 76 THR A 79 -1 O LEU A 78 N TYR A 71
CISPEP 1 LEU A 68 PRO A 69 0 -2.44
CISPEP 2 TRP A 214 PRO A 215 0 0.37
CRYST1 92.520 92.520 58.087 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 0.010808 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
