HEADER HYDROLASE 25-AUG-11 3TK9
TITLE CRYSTAL STRUCTURE OF HUMAN GRANZYME H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRANZYME H;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GZMH, CCP-X, CATHEPSIN G-LIKE 2, CTSGL2, CYTOTOXIC T-
COMPND 5 LYMPHOCYTE PROTEINASE, CYTOTOXIC SERINE PROTEASE C, CSP-C;
COMPND 6 EC: 3.4.21.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GZMH, CGL2, CTSGL2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSSETA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS SERINE PROTEASE, HYDROLASE, CYTOLYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR L.WANG,K.ZHANG,L.WU,L.TONG,F.SUN,Z.FAN
REVDAT 3 01-NOV-23 3TK9 1 REMARK SEQADV
REVDAT 2 03-JUL-13 3TK9 1 JRNL
REVDAT 1 28-DEC-11 3TK9 0
JRNL AUTH L.WANG,K.ZHANG,L.WU,S.LIU,H.ZHANG,Q.ZHOU,L.TONG,F.SUN,Z.FAN
JRNL TITL STRUCTURAL INSIGHTS INTO THE SUBSTRATE SPECIFICITY OF HUMAN
JRNL TITL 2 GRANZYME H: THE FUNCTIONAL ROLES OF A NOVEL RKR MOTIF
JRNL REF J.IMMUNOL. V. 188 765 2012
JRNL REFN ISSN 0022-1767
JRNL PMID 22156497
JRNL DOI 10.4049/JIMMUNOL.1101381
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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 (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 14758
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 776
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) : 1009
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.3710
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1769
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 41
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.84000
REMARK 3 B22 (A**2) : 2.84000
REMARK 3 B33 (A**2) : -5.69000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.168
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.771
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.015 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.761 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 6.796 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ;33.817 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;20.523 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ;20.708 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.122 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.007 ; NULL
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): NULL ; 0.790 ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 1.445 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 2.061 ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 3.345 ; NULL
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 3TK9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000067581.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : TRIANGULAR SI(111) WITH AN
REMARK 200 ASYMMETRIC ANGLE OF 7.8
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15537
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.2000
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES, PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1IAU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI2SO4, 0.1M BICINE (PH 8.5), 25%
REMARK 280 (W/V) PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 71.23200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.94250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.94250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.61600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.94250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.94250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 106.84800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.94250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.94250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.61600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.94250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.94250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 106.84800
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 71.23200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 LEU A 36 CA - CB - CG ANGL. DEV. = 20.3 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 GLN A 37 -92.59 -109.29
REMARK 500 GLU A 38 43.31 -96.18
REMARK 500 LYS A 39 -12.77 70.95
REMARK 500 THR A 56 -165.45 -161.98
REMARK 500 SER A 64 74.85 46.35
REMARK 500 HIS A 72 -53.68 -137.08
REMARK 500 SER A 127 -41.78 83.30
REMARK 500 PHE A 193 -158.08 -153.19
REMARK 500 LYS A 204 41.48 39.55
REMARK 500 LYS A 239 -101.32 -62.67
REMARK 500 ARG A 240 -75.13 -51.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 38 LYS A 39 -149.99
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 RESIDUE SO4 A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TJU RELATED DB: PDB
REMARK 900 RELATED ID: 3TJV RELATED DB: PDB
DBREF 3TK9 A 16 241 UNP P20718 GRAH_HUMAN 21 246
SEQADV 3TK9 ASN A 103 UNP P20718 ASP 108 ENGINEERED MUTATION
SEQRES 1 A 226 ILE ILE GLY GLY HIS GLU ALA LYS PRO HIS SER ARG PRO
SEQRES 2 A 226 TYR MET ALA PHE VAL GLN PHE LEU GLN GLU LYS SER ARG
SEQRES 3 A 226 LYS ARG CYS GLY GLY ILE LEU VAL ARG LYS ASP PHE VAL
SEQRES 4 A 226 LEU THR ALA ALA HIS CYS GLN GLY SER SER ILE ASN VAL
SEQRES 5 A 226 THR LEU GLY ALA HIS ASN ILE LYS GLU GLN GLU ARG THR
SEQRES 6 A 226 GLN GLN PHE ILE PRO VAL LYS ARG PRO ILE PRO HIS PRO
SEQRES 7 A 226 ALA TYR ASN PRO LYS ASN PHE SER ASN ASN ILE MET LEU
SEQRES 8 A 226 LEU GLN LEU GLU ARG LYS ALA LYS TRP THR THR ALA VAL
SEQRES 9 A 226 ARG PRO LEU ARG LEU PRO SER SER LYS ALA GLN VAL LYS
SEQRES 10 A 226 PRO GLY GLN LEU CYS SER VAL ALA GLY TRP GLY TYR VAL
SEQRES 11 A 226 SER MET SER THR LEU ALA THR THR LEU GLN GLU VAL LEU
SEQRES 12 A 226 LEU THR VAL GLN LYS ASP CYS GLN CYS GLU ARG LEU PHE
SEQRES 13 A 226 HIS GLY ASN TYR SER ARG ALA THR GLU ILE CYS VAL GLY
SEQRES 14 A 226 ASP PRO LYS LYS THR GLN THR GLY PHE LYS GLY ASP SER
SEQRES 15 A 226 GLY GLY PRO LEU VAL CYS LYS ASP VAL ALA GLN GLY ILE
SEQRES 16 A 226 LEU SER TYR GLY ASN LYS LYS GLY THR PRO PRO GLY VAL
SEQRES 17 A 226 TYR ILE LYS VAL SER HIS PHE LEU PRO TRP ILE LYS ARG
SEQRES 18 A 226 THR MET LYS ARG LEU
HET SO4 A 300 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *41(H2 O)
HELIX 1 1 LYS A 163 PHE A 171 1 9
HELIX 2 2 PHE A 230 ARG A 240 1 11
SHEET 1 A 8 HIS A 20 GLU A 21 0
SHEET 2 A 8 GLN A 155 GLN A 162 -1 O GLU A 156 N HIS A 20
SHEET 3 A 8 GLU A 180 VAL A 183 -1 O CYS A 182 N GLN A 162
SHEET 4 A 8 GLY A 222 LYS A 226 -1 O GLY A 222 N VAL A 183
SHEET 5 A 8 VAL A 206 TYR A 213 -1 N TYR A 213 O VAL A 223
SHEET 6 A 8 PRO A 200 CYS A 203 -1 N LEU A 201 O GLN A 208
SHEET 7 A 8 LEU A 136 GLY A 141 -1 N SER A 138 O VAL A 202
SHEET 8 A 8 GLN A 155 GLN A 162 -1 O LEU A 159 N CYS A 137
SHEET 1 B 7 MET A 30 LEU A 36 0
SHEET 2 B 7 ARG A 41 ARG A 50 -1 O CYS A 44 N VAL A 33
SHEET 3 B 7 PHE A 53 THR A 56 -1 O PHE A 53 N VAL A 49
SHEET 4 B 7 MET A 105 LEU A 109 -1 O LEU A 107 N VAL A 54
SHEET 5 B 7 GLN A 82 PRO A 91 -1 N LYS A 87 O GLN A 108
SHEET 6 B 7 SER A 63 LEU A 69 -1 N LEU A 69 O GLN A 82
SHEET 7 B 7 MET A 30 LEU A 36 -1 N GLN A 34 O ASN A 66
SSBOND 1 CYS A 44 CYS A 60 1555 1555 2.00
SSBOND 2 CYS A 137 CYS A 203 1555 1555 2.02
SSBOND 3 CYS A 167 CYS A 182 1555 1555 2.03
CISPEP 1 PRO A 220 PRO A 221 0 -7.43
SITE 1 AC1 3 ARG A 41 ARG A 43 LYS A 75
CRYST1 63.885 63.885 142.464 90.00 90.00 90.00 P 41 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 0.015653 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007019 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
