HEADER HYDROLASE 03-SEP-00 1FQ3
TITLE CRYSTAL STRUCTURE OF HUMAN GRANZYME B
CAVEAT 1FQ3 NAG C 1 HAS WRONG CHIRALITY AT ATOM C1 NAG D 1 HAS WRONG
CAVEAT 2 1FQ3 CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRANZYME B;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.79;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS SYSTEM
KEYWDS CHYMOTRYPSIN-LIKE SERINE PROTEINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.ESTEBANEZ-PERPINA,P.FUENTES-PRIOR,D.BELORGEY,H.RUBIN,W.BODE
REVDAT 4 29-JUL-20 1FQ3 1 CAVEAT COMPND REMARK HET
REVDAT 4 2 1 HETNAM FORMUL LINK SITE
REVDAT 4 3 1 ATOM
REVDAT 3 13-JUL-11 1FQ3 1 VERSN
REVDAT 2 24-FEB-09 1FQ3 1 VERSN
REVDAT 1 31-JAN-01 1FQ3 0
JRNL AUTH E.ESTEBANEZ-PERPINA,P.FUENTES-PRIOR,D.BELORGEY,M.BRAUN,
JRNL AUTH 2 R.KIEFERSAUER,K.MASKOS,R.HUBER,H.RUBIN,W.BODE
JRNL TITL CRYSTAL STRUCTURE OF THE CASPASE ACTIVATOR HUMAN GRANZYME B,
JRNL TITL 2 A PROTEINASE HIGHLY SPECIFIC FOR AN ASP-P1 RESIDUE.
JRNL REF BIOL.CHEM. V. 381 1203 2000
JRNL REFN ISSN 1431-6730
JRNL PMID 11209755
JRNL DOI 10.1515/BC.2000.148
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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 SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 32.500
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3582
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 0
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.511
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011806.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-00
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11275
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.19900
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) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 15.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.19900
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: CATHEPSIN G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 20.87000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.76000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.15500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.76000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.87000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.15500
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 300 REMARK: DIMER CONSTRUCTED FROM CHAIN A AND CHAIN B NOT RELATED BY A
REMARK 300 TWO-FOLD SYMMETRY
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, C, D
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ARG A 244
REMARK 475 TYR A 245
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 23 CG CD CE NZ
REMARK 480 HIS A 25 CG ND1 CD2 CE1 NE2
REMARK 480 MET A 34 CG SD CE
REMARK 480 TRP A 36 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 480 TRP A 36 CZ3 CH2
REMARK 480 GLN A 37A CG CD OE1 NE2
REMARK 480 LYS A 37B CG CD CE NZ
REMARK 480 LYS A 40 CG CD CE NZ
REMARK 480 LYS A 86 CE NZ
REMARK 480 ARG A 114 CD NE CZ NH1 NH2
REMARK 480 ARG A 116 CZ NH1 NH2
REMARK 480 ASN A 126 CB CG OD1 ND2
REMARK 480 LYS A 127 CB CG CD CE NZ
REMARK 480 LYS A 131 CD CE NZ
REMARK 480 HIS A 151 CG ND1 CD2 CE1 NE2
REMARK 480 GLU A 164 CB CG CD OE1 OE2
REMARK 480 ARG A 166 CD NE CZ NH1 NH2
REMARK 480 LYS A 167 CD CE NZ
REMARK 480 ASP A 170A CB CG OD1 OD2
REMARK 480 LEU A 171 CA
REMARK 480 ARG A 172 CB CG CD NE CZ NH1 NH2
REMARK 480 HIS A 173 CG ND1 CD2 CE1 NE2
REMARK 480 SER A 177 OG
REMARK 480 GLU A 186 CG CD OE1 OE2
REMARK 480 LYS A 188 CG CD CE NZ
REMARK 480 LYS A 188A CD CE NZ
REMARK 480 LYS A 192 CG CD CE NZ
REMARK 480 LYS A 203 CG CD CE NZ
REMARK 480 ARG A 217 CG CD NE CZ NH1 NH2
REMARK 480 CYS A 228 SG
REMARK 480 LYS A 230 NZ
REMARK 480 LYS A 239 CG CD CE NZ
REMARK 480 LYS A 243 CD CE NZ
REMARK 480 LYS B 23 CE NZ
REMARK 480 ASP B 37 CG OD1 OD2
REMARK 480 GLN B 37A CG CD OE1 NE2
REMARK 480 LYS B 37B CB CG CD CE NZ
REMARK 480 LYS B 40 CG CD CE NZ
REMARK 480 GLU B 75 CG CD OE1 OE2
REMARK 480 GLN B 76 CD OE1 NE2
REMARK 480 LYS B 111 CD CE NZ
REMARK 480 LYS B 113 CD CE NZ
REMARK 480 HIS B 151 CG ND1 CD2 CE1 NE2
REMARK 480 LYS B 159 CE NZ
REMARK 480 GLU B 164 CB CG CD OE1 OE2
REMARK 480 ARG B 166 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 167 CG CD CE NZ
REMARK 480 ARG B 172 CB CG CD NE CZ NH1 NH2
REMARK 480 HIS B 173 CB CG ND1 CD2 CE1 NE2
REMARK 480 LYS B 188 CG CD CE NZ
REMARK 480 LYS B 192 CG CD CE NZ
REMARK 480 LYS B 203 CG CD CE NZ
REMARK 480 LYS B 239 CD CE NZ
REMARK 480 LYS B 240 CG CD CE NZ
REMARK 480 LYS B 243 CD CE NZ
REMARK 480 ARG B 244 NE CZ NH1 NH2
REMARK 480 TYR B 245 C O CB CG CD1 CD2 CE1
REMARK 480 TYR B 245 CE2 CZ OH OXT
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 38 N - CA - C ANGL. DEV. = 17.9 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 HIS A 25 49.23 36.72
REMARK 500 MET A 34 109.61 -166.68
REMARK 500 GLN A 37A 155.72 73.89
REMARK 500 LYS A 37B -42.35 -12.07
REMARK 500 GLN A 48 137.65 -175.45
REMARK 500 ASP A 49 -37.16 -27.31
REMARK 500 HIS A 57 8.28 -68.77
REMARK 500 PRO A 96 -174.81 -53.77
REMARK 500 LYS A 97 17.99 52.55
REMARK 500 ASN A 98 -28.43 -168.24
REMARK 500 SER A 100 -115.64 -42.19
REMARK 500 ASP A 102 82.02 -65.47
REMARK 500 LEU A 105 95.84 -165.33
REMARK 500 SER A 125 139.55 62.70
REMARK 500 ASN A 126 -157.66 75.91
REMARK 500 ALA A 145 156.27 63.41
REMARK 500 LYS A 149 130.81 -176.70
REMARK 500 HIS A 151 95.39 -22.71
REMARK 500 LEU A 155 -176.27 -60.24
REMARK 500 GLN A 156 109.64 -168.64
REMARK 500 VAL A 158 144.66 -179.59
REMARK 500 VAL A 162 84.72 -66.13
REMARK 500 GLN A 163 174.46 -55.04
REMARK 500 GLU A 169 -16.92 -47.34
REMARK 500 ASP A 170A -37.86 76.67
REMARK 500 LEU A 171 44.51 -76.79
REMARK 500 ARG A 172 -60.75 -16.63
REMARK 500 THR A 178 -24.83 -34.24
REMARK 500 LYS A 203 56.15 88.02
REMARK 500 GLN A 210 -12.68 52.14
REMARK 500 SER A 214 -88.15 -104.92
REMARK 500 ARG A 217 140.01 -29.94
REMARK 500 MET A 242 13.54 -54.44
REMARK 500 LYS A 243 -76.22 -152.43
REMARK 500 HIS B 25 50.12 37.06
REMARK 500 GLN B 37A 132.73 49.49
REMARK 500 LYS B 37B 56.35 21.52
REMARK 500 SER B 38 133.14 161.71
REMARK 500 GLN B 48 138.41 -176.81
REMARK 500 ASP B 49 -41.60 -23.75
REMARK 500 HIS B 57 10.28 -68.71
REMARK 500 HIS B 71 -50.97 -120.29
REMARK 500 ASN B 72 79.52 -116.58
REMARK 500 ILE B 73 5.58 -53.32
REMARK 500 GLN B 76 95.44 -46.58
REMARK 500 LYS B 97 -38.81 76.94
REMARK 500 PHE B 99 23.57 41.15
REMARK 500 ASP B 102 75.67 -69.16
REMARK 500 LEU B 105 94.30 -168.94
REMARK 500 PRO B 124 84.73 -64.72
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 32 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FQ3 A 16 245 UNP P10144 GRAB_HUMAN 21 247
DBREF 1FQ3 B 16 245 UNP P10144 GRAB_HUMAN 21 247
SEQRES 1 A 227 ILE ILE GLY GLY HIS GLU ALA LYS PRO HIS SER ARG PRO
SEQRES 2 A 227 TYR MET ALA TYR LEU MET ILE TRP ASP GLN LYS SER LEU
SEQRES 3 A 227 LYS ARG CYS GLY GLY PHE LEU ILE GLN ASP ASP PHE VAL
SEQRES 4 A 227 LEU THR ALA ALA HIS CYS TRP GLY SER SER ILE ASN VAL
SEQRES 5 A 227 THR LEU GLY ALA HIS ASN ILE LYS GLU GLN GLU PRO THR
SEQRES 6 A 227 GLN GLN PHE ILE PRO VAL LYS ARG PRO ILE PRO HIS PRO
SEQRES 7 A 227 ALA TYR ASN PRO LYS ASN PHE SER ASN ASP ILE MET LEU
SEQRES 8 A 227 LEU GLN LEU GLU ARG LYS ALA LYS ARG THR ARG ALA VAL
SEQRES 9 A 227 GLN PRO LEU ARG LEU PRO SER ASN LYS ALA GLN VAL LYS
SEQRES 10 A 227 PRO GLY GLN THR CYS SER VAL ALA GLY TRP GLY GLN THR
SEQRES 11 A 227 ALA PRO LEU GLY LYS HIS SER HIS THR LEU GLN GLU VAL
SEQRES 12 A 227 LYS MET THR VAL GLN GLU ASP ARG LYS CYS GLU SER ASP
SEQRES 13 A 227 LEU ARG HIS TYR TYR ASP SER THR ILE GLU LEU CYS VAL
SEQRES 14 A 227 GLY ASP PRO GLU ILE LYS LYS THR SER PHE LYS GLY ASP
SEQRES 15 A 227 SER GLY GLY PRO LEU VAL CYS ASN LYS VAL ALA GLN GLY
SEQRES 16 A 227 ILE VAL SER TYR GLY ARG ASN ASN GLY MET PRO PRO ARG
SEQRES 17 A 227 ALA CYS THR LYS VAL SER SER PHE VAL HIS TRP ILE LYS
SEQRES 18 A 227 LYS THR MET LYS ARG TYR
SEQRES 1 B 227 ILE ILE GLY GLY HIS GLU ALA LYS PRO HIS SER ARG PRO
SEQRES 2 B 227 TYR MET ALA TYR LEU MET ILE TRP ASP GLN LYS SER LEU
SEQRES 3 B 227 LYS ARG CYS GLY GLY PHE LEU ILE GLN ASP ASP PHE VAL
SEQRES 4 B 227 LEU THR ALA ALA HIS CYS TRP GLY SER SER ILE ASN VAL
SEQRES 5 B 227 THR LEU GLY ALA HIS ASN ILE LYS GLU GLN GLU PRO THR
SEQRES 6 B 227 GLN GLN PHE ILE PRO VAL LYS ARG PRO ILE PRO HIS PRO
SEQRES 7 B 227 ALA TYR ASN PRO LYS ASN PHE SER ASN ASP ILE MET LEU
SEQRES 8 B 227 LEU GLN LEU GLU ARG LYS ALA LYS ARG THR ARG ALA VAL
SEQRES 9 B 227 GLN PRO LEU ARG LEU PRO SER ASN LYS ALA GLN VAL LYS
SEQRES 10 B 227 PRO GLY GLN THR CYS SER VAL ALA GLY TRP GLY GLN THR
SEQRES 11 B 227 ALA PRO LEU GLY LYS HIS SER HIS THR LEU GLN GLU VAL
SEQRES 12 B 227 LYS MET THR VAL GLN GLU ASP ARG LYS CYS GLU SER ASP
SEQRES 13 B 227 LEU ARG HIS TYR TYR ASP SER THR ILE GLU LEU CYS VAL
SEQRES 14 B 227 GLY ASP PRO GLU ILE LYS LYS THR SER PHE LYS GLY ASP
SEQRES 15 B 227 SER GLY GLY PRO LEU VAL CYS ASN LYS VAL ALA GLN GLY
SEQRES 16 B 227 ILE VAL SER TYR GLY ARG ASN ASN GLY MET PRO PRO ARG
SEQRES 17 B 227 ALA CYS THR LYS VAL SER SER PHE VAL HIS TRP ILE LYS
SEQRES 18 B 227 LYS THR MET LYS ARG TYR
MODRES 1FQ3 ASN B 65 ASN GLYCOSYLATION SITE
MODRES 1FQ3 ASN A 65 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET SO4 A 800 5
HET SO4 B 900 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM SO4 SULFATE ION
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 BMA 2(C6 H12 O6)
FORMUL 5 SO4 2(O4 S 2-)
HELIX 1 1 ALA A 55 TRP A 59 5 5
HELIX 2 2 GLU A 164 GLU A 169 1 6
HELIX 3 3 LYS A 230 MET A 242 1 13
HELIX 4 4 ALA B 55 TRP B 59 5 5
HELIX 5 5 GLU B 164 LEU B 171 1 9
HELIX 6 6 LYS B 230 MET B 242 1 13
SHEET 1 A 9 SER A 38 LYS A 40 0
SHEET 2 A 9 ILE A 35 ASP A 37 -1 N ILE A 35 O LYS A 40
SHEET 3 A 9 SER A 63 LEU A 68 -1 N SER A 63 O TRP A 36
SHEET 4 A 9 MET A 30 TYR A 32 -1 O TYR A 32 N THR A 67
SHEET 5 A 9 GLY A 43 GLN A 48 -1 O GLY A 44 N ALA A 31
SHEET 6 A 9 PHE A 51 THR A 54 -1 N PHE A 51 O GLN A 48
SHEET 7 A 9 MET A 104 LEU A 108 -1 N MET A 104 O THR A 54
SHEET 8 A 9 GLN A 81 PRO A 88 -1 N LYS A 86 O GLN A 107
SHEET 9 A 9 SER A 63 LEU A 68 -1 O ILE A 64 N VAL A 85
SHEET 1 B 2 THR A 135 SER A 137 0
SHEET 2 B 2 LYS A 159 THR A 161 -1 N MET A 160 O CYS A 136
SHEET 1 C 3 GLU A 180 LEU A 181 0
SHEET 2 C 3 CYS A 228 THR A 229 -1 N CYS A 228 O LEU A 181
SHEET 3 C 3 ILE A 212 VAL A 213 -1 N ILE A 212 O THR A 229
SHEET 1 D 7 MET B 104 LEU B 108 0
SHEET 2 D 7 GLN B 81 PRO B 88 -1 N LYS B 86 O GLN B 107
SHEET 3 D 7 ILE B 64 LEU B 68 -1 O ILE B 64 N VAL B 85
SHEET 4 D 7 MET B 30 TRP B 36 -1 N TYR B 32 O THR B 67
SHEET 5 D 7 LEU B 39 GLN B 48 -1 O LYS B 40 N ILE B 35
SHEET 6 D 7 PHE B 51 THR B 54 -1 O PHE B 51 N GLN B 48
SHEET 7 D 7 MET B 104 LEU B 108 -1 N MET B 104 O THR B 54
SHEET 1 E 6 LYS B 159 THR B 161 0
SHEET 2 E 6 THR B 135 VAL B 138 -1 O CYS B 136 N MET B 160
SHEET 3 E 6 PRO B 198 VAL B 200 -1 O VAL B 200 N SER B 137
SHEET 4 E 6 ALA B 209 TYR B 215 -1 N GLN B 210 O LEU B 199
SHEET 5 E 6 ALA B 227 THR B 229 -1 O ALA B 227 N SER B 214
SHEET 6 E 6 GLU B 180 LEU B 181 -1 O LEU B 181 N CYS B 228
SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.02
SSBOND 4 CYS B 42 CYS B 58 1555 1555 2.03
SSBOND 5 CYS B 136 CYS B 201 1555 1555 2.02
SSBOND 6 CYS B 168 CYS B 182 1555 1555 2.02
LINK ND2 ASN A 65 C1 NAG C 1 1555 1555 1.57
LINK ND2 ASN B 65 C1 NAG D 1 1555 1555 1.56
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.47
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.41
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45
CISPEP 1 PRO A 224A PRO A 225 0 -0.12
CISPEP 2 PRO B 224A PRO B 225 0 -0.45
CRYST1 41.740 114.310 135.520 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 0.023958 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008748 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007379 0.00000
(ATOM LINES ARE NOT SHOWN.)
END