spacer
spacer

PDBsum entry 3pdo

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Immune system PDB id
3pdo
Jmol
Contents
Protein chains
185 a.a.
191 a.a.
17 a.a.
Ligands
GOL ×2
FMT
Waters ×320
HEADER    IMMUNE SYSTEM                           23-OCT-10   3PDO
TITLE     CRYSTAL STRUCTURE OF HLA-DR1 WITH CLIP102-120
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND   9 CHAIN: B;
COMPND  10 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND  11 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN;
COMPND  15 CHAIN: C;
COMPND  16 SYNONYM: HLA-DR ANTIGENS-ASSOCIATED INVARIANT CHAIN, IA ANTIGEN-
COMPND  17 ASSOCIATED INVARIANT CHAIN, II, P33;
COMPND  18 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DRA, HLA-DRA1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE  11 MOL_ID: 2;
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  13 ORGANISM_COMMON: HUMAN;
SOURCE  14 ORGANISM_TAXID: 9606;
SOURCE  15 GENE: HLA-DRB1;
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET24D;
SOURCE  21 MOL_ID: 3;
SOURCE  22 SYNTHETIC: YES;
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  24 ORGANISM_COMMON: HUMAN;
SOURCE  25 ORGANISM_TAXID: 9606
KEYWDS    MHC CLASS II, MHC II, SELF ANTIGEN, INVARIANT CHAIN, CLIP, IMMUNE
KEYWDS   2 SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.GUNTHER,A.SCHLUNDT,J.STICHT,Y.ROSKE,U.HEINEMANN,K.-H.WIESMULLER,
AUTHOR   2 G.JUNG,K.FALK,O.ROTZSCHKE,C.FREUND
REVDAT   2   05-JAN-11 3PDO    1       JRNL
REVDAT   1   08-DEC-10 3PDO    0
JRNL        AUTH   S.GUNTHER,A.SCHLUNDT,J.STICHT,Y.ROSKE,U.HEINEMANN,
JRNL        AUTH 2 K.H.WIESMULLER,G.JUNG,K.FALK,O.ROTZSCHKE,C.FREUND
JRNL        TITL   BIDIRECTIONAL BINDING OF INVARIANT CHAIN PEPTIDES TO AN MHC
JRNL        TITL 2 CLASS II MOLECULE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 22219 2010
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   21115828
JRNL        DOI    10.1073/PNAS.1014708107
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.26
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 32809
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) : 0.194
REMARK   3   R VALUE            (WORKING SET) : 0.191
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1641
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) : 1.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2245
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450
REMARK   3   BIN FREE R VALUE SET COUNT          : 118
REMARK   3   BIN FREE R VALUE                    : 0.3120
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3200
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 15
REMARK   3   SOLVENT ATOMS            : 320
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 30.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.29
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 3.24000
REMARK   3    B22 (A**2) : -1.73000
REMARK   3    B33 (A**2) : -1.51000
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): 0.161
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.340
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3311 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4502 ; 1.536 ; 1.944
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   392 ; 6.545 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   168 ;32.788 ;23.571
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   536 ;15.397 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;17.403 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   485 ; 0.107 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2562 ; 0.008 ; 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):  1976 ; 1.333 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3223 ; 2.236 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1335 ; 3.271 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1279 ; 5.019 ; 4.500
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 U VALUES: REFINED INDIVIDUALLY
REMARK   4
REMARK   4 3PDO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BESSY
REMARK 200  BEAMLINE                       : 14.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841
REMARK 200  MONOCHROMATOR                  : SI-111 CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32810
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.6200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.54600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, NACITRATE, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 298K
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       22.72500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.52600
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.81350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.52600
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.72500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.81350
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 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: 8740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 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     PRO A   185
REMARK 465     LEU A   186
REMARK 465     PRO A   187
REMARK 465     GLU A   188
REMARK 465     THR A   189
REMARK 465     THR A   190
REMARK 465     GLU A   191
REMARK 465     ASN A   192
REMARK 465     ARG B   191
REMARK 465     SER B   192
REMARK 465     GLU B   193
REMARK 465     SER B   194
REMARK 465     ALA B   195
REMARK 465     GLN B   196
REMARK 465     SER B   197
REMARK 465     LYS B   198
REMARK 465     LYS C   102
REMARK 465     MET C   120
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     GLU A  46    CG   CD   OE1  OE2
REMARK 470     LYS B  65    CG   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    ASP A   159     O    HOH A   262              2.14
REMARK 500   OD2  ASP B    43     O    HOH B   217              2.16
REMARK 500   O    HOH A   280     O    HOH A   324              2.17
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    VAL A 136     -179.24    -67.66
REMARK 500    ASP B   2       84.10     58.24
REMARK 500    THR B  90      -79.82   -128.02
REMARK 500    LEU B 109      -58.57     91.58
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 GOL A 193
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PGC   RELATED DB: PDB
REMARK 900 RELATED ID: 3PGD   RELATED DB: PDB
DBREF  3PDO A    1   192  UNP    P01903   DRA_HUMAN       26    217
DBREF  3PDO B    1   198  UNP    P04229   2B11_HUMAN      30    227
DBREF  3PDO C  102   120  UNP    P04233   HG2A_HUMAN     102    120
SEQADV 3PDO MET A    0  UNP  P01903              EXPRESSION TAG
SEQADV 3PDO MET B    0  UNP  P04229              EXPRESSION TAG
SEQRES   1 A  193  MET ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE
SEQRES   2 A  193  TYR LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP
SEQRES   3 A  193  PHE ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS
SEQRES   4 A  193  LYS GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE
SEQRES   5 A  193  ALA SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA
SEQRES   6 A  193  VAL ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER
SEQRES   7 A  193  ASN TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR
SEQRES   8 A  193  VAL LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN
SEQRES   9 A  193  VAL LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL
SEQRES  10 A  193  VAL ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR
SEQRES  11 A  193  THR GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP
SEQRES  12 A  193  HIS LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO
SEQRES  13 A  193  SER THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP
SEQRES  14 A  193  GLY LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES  15 A  193  ALA PRO SER PRO LEU PRO GLU THR THR GLU ASN
SEQRES   1 B  199  MET GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS
SEQRES   2 B  199  PHE GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG
SEQRES   3 B  199  LEU LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL
SEQRES   4 B  199  ARG PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR
SEQRES   5 B  199  GLU LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN
SEQRES   6 B  199  LYS ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR
SEQRES   7 B  199  TYR CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR
SEQRES   8 B  199  VAL GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO
SEQRES   9 B  199  SER LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL
SEQRES  10 B  199  CYS SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL
SEQRES  11 B  199  ARG TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL
SEQRES  12 B  199  VAL SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE
SEQRES  13 B  199  GLN THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY
SEQRES  14 B  199  GLU VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR
SEQRES  15 B  199  SER PRO LEU THR VAL GLU TRP ARG ALA ARG SER GLU SER
SEQRES  16 B  199  ALA GLN SER LYS
SEQRES   1 C   19  LYS PRO VAL SER LYS MET ARG MET ALA THR PRO LEU LEU
SEQRES   2 C   19  MET GLN ALA LEU PRO MET
HET    GOL  A 193       6
HET    GOL  B 199       6
HET    FMT  B 200       3
HETNAM     GOL GLYCEROL
HETNAM     FMT FORMIC ACID
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   4  GOL    2(C3 H8 O3)
FORMUL   6  FMT    C H2 O2
FORMUL   7  HOH   *320(H2 O)
HELIX    1   1 LEU A   45  ARG A   50  5                                   6
HELIX    2   2 GLU A   55  SER A   77  1                                  23
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  TYR B   78  1                                  15
HELIX    6   6 TYR B   78  GLU B   87  1                                  10
HELIX    7   7 SER B   88  THR B   90  5                                   3
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  ASP A  35   O  GLU A  40
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29
SHEET    4   A 8 GLU A   4  ASN A  15 -1  N  ILE A   8   O  ASP A  25
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  ARG B  25   N  HIS B  16
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  PHE B  40   N  GLU B  28
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 2 ALA A  52  SER A  53  0
SHEET    2   B 2 SER C 105  LYS C 106  1  O  SER C 105   N  SER A  53
SHEET    1   C 4 GLU A  88  THR A  93  0
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  PHE A 108   N  THR A  90
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107
SHEET    4   C 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   D 4 GLU A  88  THR A  93  0
SHEET    2   D 4 ASN A 103  PHE A 112 -1  O  PHE A 108   N  THR A  90
SHEET    3   D 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107
SHEET    4   D 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   E 4 LYS A 126  VAL A 128  0
SHEET    2   E 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   E 4 TYR A 161  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4   E 4 LEU A 174  TRP A 178 -1  O  LEU A 174   N  VAL A 165
SHEET    1   F 4 LYS B  98  SER B 104  0
SHEET    2   F 4 LEU B 114  PHE B 122 -1  O  SER B 120   N  LYS B  98
SHEET    3   F 4 PHE B 155  GLU B 162 -1  O  THR B 157   N  VAL B 119
SHEET    4   F 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   G 4 LYS B  98  SER B 104  0
SHEET    2   G 4 LEU B 114  PHE B 122 -1  O  SER B 120   N  LYS B  98
SHEET    3   G 4 PHE B 155  GLU B 162 -1  O  THR B 157   N  VAL B 119
SHEET    4   G 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   H 4 GLN B 136  GLU B 138  0
SHEET    2   H 4 GLU B 128  ARG B 133 -1  N  TRP B 131   O  GLU B 138
SHEET    3   H 4 TYR B 171  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   H 4 LEU B 184  TRP B 188 -1  O  LEU B 184   N  VAL B 175
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.11
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.13
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.05
CISPEP   1 ASN A   15    PRO A   16          0         0.38
CISPEP   2 THR A  113    PRO A  114          0         1.36
CISPEP   3 TYR B  123    PRO B  124          0         3.79
SITE     1 AC1  8 ARG A  44  VAL A 104  TYR A 150  HOH A 257
SITE     2 AC1  8 HOH A 272  HOH A 308  HOH A 335  ASP B 152
SITE     1 AC2  5 ARG B  25  ARG B  39  GLU B  87  HOH B 221
SITE     2 AC2  5 HOH B 303
SITE     1 AC3  4 ARG B  48  ALA B  49  ALA B  58  ARG B  94
CRYST1   45.450   97.627   99.052  90.00  90.00  90.00 P 21 21 21    4
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      0.022002  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010243  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010096        0.00000
      
PROCHECK
Go to PROCHECK summary
 References