HEADER IMMUNE SYSTEM 11-JUL-01 1JK8
TITLE CRYSTAL STRUCTURE OF A HUMAN INSULIN PEPTIDE-HLA-DQ8 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS II HLA-DQ8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA CHAIN (DQA1*0301);
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MHC CLASS II HLA-DQ8;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: BETA CHAIN (DQB1*0302);
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: INSULIN B PEPTIDE;
COMPND 13 CHAIN: C;
COMPND 14 FRAGMENT: PEPTIDE (9-SHLVEALYLVCGERG-23);
COMPND 15 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_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 17 MOL_ID: 3;
SOURCE 18 SYNTHETIC: YES;
SOURCE 19 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 20 OF THIS PEPTIDE OCCURS NATURALLY IN HUMANS (HOMO SAPIENS).
KEYWDS HLA-DQ8, INSULIN B PEPTIDE, TYPE 1 DIABETES, AUTOIMMUNITY, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.H.LEE,K.W.WUCHERPFENNIG,D.C.WILEY
REVDAT 5 29-JUL-20 1JK8 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE
REVDAT 4 31-JAN-18 1JK8 1 REMARK
REVDAT 3 13-JUL-11 1JK8 1 VERSN
REVDAT 2 24-FEB-09 1JK8 1 VERSN
REVDAT 1 22-AUG-01 1JK8 0
JRNL AUTH K.H.LEE,K.W.WUCHERPFENNIG,D.C.WILEY
JRNL TITL STRUCTURE OF A HUMAN INSULIN PEPTIDE-HLA-DQ8 COMPLEX AND
JRNL TITL 2 SUSCEPTIBILITY TO TYPE 1 DIABETES.
JRNL REF NAT.IMMUNOL. V. 2 501 2001
JRNL REFN ISSN 1529-2908
JRNL PMID 11376336
JRNL DOI 10.1038/88694
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1016975.090
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 17854
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 SET) : 0.224
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1765
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2396
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 257
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 70
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 4.63000
REMARK 3 B33 (A**2) : -5.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.39
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.370 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.840 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.320 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.530 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 24.65
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 1JK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013871.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18183
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10300
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) : 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, MAGNESIUM ACETATE, PH 3.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 18K, TEMPERATURE
REMARK 280 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 21.43100
REMARK 290 SMTRY3 2 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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 ARG B 105 CG CD NE CZ NH1 NH2
REMARK 470 THR B 106 OG1 CG2
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 LEU B 109 CG CD1 CD2
REMARK 470 ASN B 110 CG OD1 ND2
REMARK 470 HIS B 111 CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 112 CG ND1 CD2 CE1 NE2
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 B 105
REMARK 475 THR B 106
REMARK 475 GLU B 107
REMARK 475 ALA B 108
REMARK 475 LEU B 109
REMARK 475 ASN B 110
REMARK 475 HIS B 111
REMARK 475 HIS B 112
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 GLU A 37 CG GLU A 37 CD -0.342
REMARK 500 GLU A 88 CG GLU A 88 CD 0.252
REMARK 500 GLN A 101 CG GLN A 101 CD -0.140
REMARK 500 ASP A 157 CG ASP A 157 OD1 0.174
REMARK 500 ASP A 157 CG ASP A 157 OD2 -0.220
REMARK 500 ASP A 171 CG ASP A 171 OD1 0.455
REMARK 500 PRO A 180 C GLU A 181 N -0.217
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 GLU A 88 CB - CG - CD ANGL. DEV. = -20.3 DEGREES
REMARK 500 ASP A 157 CB - CG - OD1 ANGL. DEV. = -15.9 DEGREES
REMARK 500 ASP A 157 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP A 171 OD1 - CG - OD2 ANGL. DEV. = -29.0 DEGREES
REMARK 500 ASP A 171 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 171 CB - CG - OD2 ANGL. DEV. = 24.7 DEGREES
REMARK 500 PRO A 180 O - C - N ANGL. DEV. = -10.2 DEGREES
REMARK 500 SER B 104 O - C - N ANGL. DEV. = -18.5 DEGREES
REMARK 500 ARG B 105 C - N - CA ANGL. DEV. = 16.4 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 PHE A 113 128.46 -178.08
REMARK 500 HIS A 143 9.17 80.21
REMARK 500 PRO A 180 78.10 -51.64
REMARK 500 ASN B 19 73.21 59.65
REMARK 500 ASN B 33 -99.58 68.23
REMARK 500 PRO B 52 2.26 -67.32
REMARK 500 CYS B 79 -70.56 -53.73
REMARK 500 THR B 89 -94.97 -128.77
REMARK 500 ARG B 105 -83.86 104.67
REMARK 500 THR B 106 -146.27 -162.80
REMARK 500 ALA B 108 116.62 64.98
REMARK 500 ASN B 110 55.51 101.03
REMARK 500 HIS B 111 4.90 58.29
REMARK 500 ASN B 113 167.24 -33.90
REMARK 500 TYR B 123 138.27 -170.07
REMARK 500 PRO B 124 -175.03 -67.34
REMARK 500 ASN B 134 -112.75 62.06
REMARK 500 GLN B 191 72.66 70.24
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 ASP A 171 0.11 SIDE CHAIN
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 SER B 104 17.44
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JK8 A 2 181 UNP P04225 HA24_HUMAN 27 207
DBREF 1JK8 B 3 192 UNP P01920 HB24_HUMAN 35 224
DBREF 1JK8 C 1 14 GB 3776078 CAA08766 35 48
SEQADV 1JK8 GLY C 14 GB 3776078 GLU 48 CONFLICT
SEQRES 1 A 181 VAL ALA ASP HIS VAL ALA SER TYR GLY VAL ASN LEU TYR
SEQRES 2 A 181 GLN SER TYR GLY PRO SER GLY GLN TYR SER HIS GLU PHE
SEQRES 3 A 181 ASP GLY ASP GLU GLU PHE TYR VAL ASP LEU GLU ARG LYS
SEQRES 4 A 181 GLU THR VAL TRP GLN LEU PRO LEU PHE ARG ARG PHE ARG
SEQRES 5 A 181 ARG PHE ASP PRO GLN PHE ALA LEU THR ASN ILE ALA VAL
SEQRES 6 A 181 LEU LYS HIS ASN LEU ASN ILE VAL ILE LYS ARG SER ASN
SEQRES 7 A 181 SER THR ALA ALA THR ASN GLU VAL PRO GLU VAL THR VAL
SEQRES 8 A 181 PHE SER LYS SER PRO VAL THR LEU GLY GLN PRO ASN THR
SEQRES 9 A 181 LEU ILE CYS LEU VAL ASP ASN ILE PHE PRO PRO VAL VAL
SEQRES 10 A 181 ASN ILE THR TRP LEU SER ASN GLY HIS SER VAL THR GLU
SEQRES 11 A 181 GLY VAL SER GLU THR SER PHE LEU SER LYS SER ASP HIS
SEQRES 12 A 181 SER PHE PHE LYS ILE SER TYR LEU THR PHE LEU PRO SER
SEQRES 13 A 181 ASP ASP GLU ILE TYR ASP CYS LYS VAL GLU HIS TRP GLY
SEQRES 14 A 181 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PRO GLU
SEQRES 1 B 190 SER PRO GLU ASP PHE VAL TYR GLN PHE LYS GLY MET CYS
SEQRES 2 B 190 TYR PHE THR ASN GLY THR GLU ARG VAL ARG LEU VAL THR
SEQRES 3 B 190 ARG TYR ILE TYR ASN ARG GLU GLU TYR ALA ARG PHE ASP
SEQRES 4 B 190 SER ASP VAL GLY VAL TYR ARG ALA VAL THR PRO LEU GLY
SEQRES 5 B 190 PRO PRO ALA ALA GLU TYR TRP ASN SER GLN LYS GLU VAL
SEQRES 6 B 190 LEU GLU ARG THR ARG ALA GLU LEU ASP THR VAL CYS ARG
SEQRES 7 B 190 HIS ASN TYR GLN LEU GLU LEU ARG THR THR LEU GLN ARG
SEQRES 8 B 190 ARG VAL GLU PRO THR VAL THR ILE SER PRO SER ARG THR
SEQRES 9 B 190 GLU ALA LEU ASN HIS HIS ASN LEU LEU VAL CYS SER VAL
SEQRES 10 B 190 THR ASP PHE TYR PRO ALA GLN ILE LYS VAL ARG TRP PHE
SEQRES 11 B 190 ARG ASN ASP GLN GLU GLU THR THR GLY VAL VAL SER THR
SEQRES 12 B 190 PRO LEU ILE ARG ASN GLY ASP TRP THR PHE GLN ILE LEU
SEQRES 13 B 190 VAL MET LEU GLU MET THR PRO GLN ARG GLY ASP VAL TYR
SEQRES 14 B 190 THR CYS HIS VAL GLU HIS PRO SER LEU GLN ASN PRO ILE
SEQRES 15 B 190 ILE VAL GLU TRP ARG ALA GLN SER
SEQRES 1 C 14 LEU VAL GLU ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY
SEQRES 2 C 14 GLY
MODRES 1JK8 ASN A 78 ASN GLYCOSYLATION SITE
HET NAG A 401 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
FORMUL 4 NAG C8 H15 N O6
FORMUL 5 HOH *70(H2 O)
HELIX 1 1 LEU A 45 ARG A 52 1 8
HELIX 2 2 ASP A 55 SER A 77 1 23
HELIX 3 3 GLY B 54 SER B 63 1 10
HELIX 4 4 GLN B 64 VAL B 78 1 15
HELIX 5 5 VAL B 78 ARG B 88 1 11
HELIX 6 6 THR B 89 ARG B 93 5 5
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 O TYR A 33 N VAL A 42
SHEET 3 A 8 SER A 19 PHE A 26 -1 O TYR A 22 N VAL A 34
SHEET 4 A 8 HIS A 5 GLN A 14 -1 N SER A 8 O GLU A 25
SHEET 5 A 8 VAL B 8 THR B 18 -1 N TYR B 9 O TYR A 13
SHEET 6 A 8 ARG B 23 TYR B 32 -1 O ARG B 23 N THR B 18
SHEET 7 A 8 GLU B 35 ASP B 41 -1 O GLU B 35 N TYR B 32
SHEET 8 A 8 TYR B 47 ALA B 49 -1 N ARG B 48 O ARG B 39
SHEET 1 B 4 GLU A 88 SER A 93 0
SHEET 2 B 4 ASN A 103 ILE A 112 -1 N ILE A 106 O PHE A 92
SHEET 3 B 4 PHE A 145 PHE A 153 -1 O PHE A 145 N ILE A 112
SHEET 4 B 4 VAL A 132 GLU A 134 -1 O SER A 133 N TYR A 150
SHEET 1 C 4 GLU A 88 SER A 93 0
SHEET 2 C 4 ASN A 103 ILE A 112 -1 N ILE A 106 O PHE A 92
SHEET 3 C 4 PHE A 145 PHE A 153 -1 O PHE A 145 N ILE A 112
SHEET 4 C 4 LEU A 138 SER A 139 -1 N LEU A 138 O PHE A 146
SHEET 1 D 4 HIS A 126 VAL A 128 0
SHEET 2 D 4 ASN A 118 SER A 123 -1 O TRP A 121 N VAL A 128
SHEET 3 D 4 TYR A 161 GLU A 166 -1 O ASP A 162 N LEU A 122
SHEET 4 D 4 LEU A 174 TRP A 178 -1 N LEU A 174 O VAL A 165
SHEET 1 E 4 THR B 98 PRO B 103 0
SHEET 2 E 4 LEU B 114 PHE B 122 -1 N VAL B 116 O SER B 102
SHEET 3 E 4 PHE B 155 GLU B 162 -1 N PHE B 155 O PHE B 122
SHEET 4 E 4 VAL B 142 SER B 144 -1 O VAL B 143 N MET B 160
SHEET 1 F 4 THR B 98 PRO B 103 0
SHEET 2 F 4 LEU B 114 PHE B 122 -1 N VAL B 116 O SER B 102
SHEET 3 F 4 PHE B 155 GLU B 162 -1 N PHE B 155 O PHE B 122
SHEET 4 F 4 ILE B 148 ARG B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 G 4 GLN B 136 GLU B 138 0
SHEET 2 G 4 LYS B 128 ARG B 133 -1 O TRP B 131 N GLU B 138
SHEET 3 G 4 VAL B 170 GLU B 176 -1 O THR B 172 N PHE B 132
SHEET 4 G 4 ILE B 184 ARG B 189 -1 O ILE B 184 N VAL B 175
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.03
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.03
LINK ND2 ASN A 78 C1 NAG A 401 1555 1555 1.45
CISPEP 1 GLY A 17 PRO A 18 0 -0.35
CISPEP 2 PHE A 113 PRO A 114 0 -0.03
CISPEP 3 TYR B 123 PRO B 124 0 -0.50
CRYST1 66.034 42.862 87.467 90.00 102.48 90.00 P 1 21 1 2
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 0.015144 0.000000 0.003352 0.00000
SCALE2 0.000000 0.023331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END