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PDBsum entry 1n7d

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Lipid transport PDB id
1n7d
Jmol
Contents
Protein chain
639 a.a. *
Ligands
NAG-NAG-BMA-MAN-
MAN
NAG-NAG-BMA-MAN
KEG ×3
Metals
_CA ×8
* Residue conservation analysis
HEADER    LIPID TRANSPORT                         13-NOV-02   1N7D
TITLE     EXTRACELLULAR DOMAIN OF THE LDL RECEPTOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 1-699;
COMPND   5 SYNONYM: LDL RECEPTOR;
COMPND   6 ENGINEERED: YES;
COMPND   7 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: LDLR;
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS    LDL-RECEPTOR, FAMILIAL HYPERCHOLESTEROLEMIA, LDL, CHOLESTEROL
KEYWDS   2 METABOLISM, LIPID TRANSPORT
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.RUDENKO,L.HENRY,K.HENDERSON,K.ICHTCHENKO,M.S.BROWN,J.L.GOLDSTEIN,
AUTHOR   2 J.DEISENHOFER
REVDAT   3   13-JUL-11 1N7D    1       VERSN
REVDAT   2   24-FEB-09 1N7D    1       VERSN
REVDAT   1   21-JAN-03 1N7D    0
JRNL        AUTH   G.RUDENKO,L.HENRY,K.HENDERSON,K.ICHTCHENKO,M.S.BROWN,
JRNL        AUTH 2 J.L.GOLDSTEIN,J.DEISENHOFER
JRNL        TITL   STRUCTURE OF THE LDL RECEPTOR EXTRACELLULAR DOMAIN AT
JRNL        TITL 2 ENDOSOMAL PH
JRNL        REF    SCIENCE                       V. 298  2353 2002
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   12459547
JRNL        DOI    10.1126/SCIENCE.1078124
REMARK   2
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.8
REMARK   3   NUMBER OF REFLECTIONS             : 16008
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) : 0.381
REMARK   3   FREE R VALUE                     : 0.382
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1119
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.87
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 36.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 757
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4550
REMARK   3   BIN FREE R VALUE                    : 0.5120
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 68
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.062
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4702
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 254
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 74.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 124.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 20.49000
REMARK   3    B22 (A**2) : 20.49000
REMARK   3    B33 (A**2) : -40.98000
REMARK   3    B12 (A**2) : 9.97000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 1.10
REMARK   3   ESD FROM SIGMAA              (A) : 1.05
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 50.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 1.19
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.11
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.031
REMARK   3   BOND ANGLES            (DEGREES) : 4.90
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.52
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : OVERALL
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  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.16
REMARK   3   BSOL        : 10.00
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : KEG_18JAN02.PAR
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : ION.TOP
REMARK   3  TOPOLOGY FILE  3   : KEG_12JUL02.TOP
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  5   : WATER.TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  THE SUGARS HAVE NOT BEEN REFINED, JUST MANUALLY PLACED
REMARK   3  IN THE DENSITY. THE EXACT IDENTITY OF THE SUGARS
REMARK   3  IN THESE N-LINKED GLYCOSYLATION
REMARK   3  SITES IS NOT KNOWN.
REMARK   3  AT THIS RESOLUTION POSITIONAL
REMARK   3  REFINEMENT IS OF LIMITED USE.
REMARK   3  HARMONIC RESTRAINTS WERE USED
REMARK   3  ON MOST CORE RESIDUES. NO SIMULATED
REMARK   3  ANNEALING WAS USED.
REMARK   3
REMARK   3
REMARK   3  THE RESOLUTION OF THE MAD DATA USED IN THE STRUCTURE DETERMINATION
REMARK   3  IS 3.7 ANG AND THE B-FACTORS WERE HIGH.
REMARK   3  THIS MEANS THAT THE POSITIONS OF THE SIDE CHAINS
REMARK   3  ARE NOT WELL DETERMINED IN THE MODEL.
REMARK   3  THE AUTHORS URGE
REMARK   3  USERS TO EXERCIZE CAUTION AND RESTRAINT INTERPRETING THIS MODEL.
REMARK   3  THE AUTHORS ARE AVAILABLE FOR QUESTIONS.
REMARK   3
REMARK   3
REMARK   3  THE CLUSTERS WERE INCLUDED IN THE POSITIONAL REFINEMENT
REMARK   3  (REGULARIZATION OF THE MODEL).
REMARK   3  THE CARBOHYDRATES WERE NOT INCLUDED IN THE POSITIONAL
REMARK   3  REFINEMENT (REGULARIZATION OF THE MODEL) BUT FITTED MANUALLY.
REMARK   3  THE CARBOHYDRATES WERE MODELLED AS THE N-LINKED HIGH MANNOSE TYPE.
REMARK   4
REMARK   4 1N7D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-02.
REMARK 100 THE RCSB ID CODE IS RCSB017610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-01; NULL; NULL
REMARK 200  TEMPERATURE           (KELVIN) : 110; NULL; NULL
REMARK 200  PH                             : 5.3
REMARK 200  NUMBER OF CRYSTALS USED        : 8
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y
REMARK 200  RADIATION SOURCE               : ALS; ALS; APS
REMARK 200  BEAMLINE                       : 5.0.2; 8.2.1; 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.21363, 1.21423, 1.10696,
REMARK 200                                   1.23985; NULL; NULL
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL
REMARK 200  OPTICS                         : NULL; NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD; CCD; NULL
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; ADSC QUANTUM
REMARK 200                                   210; NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17303
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.300
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.83
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.44900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; NULL; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: PDB ENTRIES: 1AJJ, 1D2J, 1I0U, 1IJQ, 1FX5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ACETATE BUFFER PH 5.3, 1,2-HEXANEDIOL,
REMARK 280  0.5 MM CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       28.39533
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.79067
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.79067
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       28.39533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 THE AUTHORS BELIEVE THE BIOLOGICAL UNIT IS A MONOMER.
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 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 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 O1   KEG A6003  LIES ON A SPECIAL POSITION.
REMARK 375 W1   KEG A6003  LIES ON A SPECIAL POSITION.
REMARK 375 P1   KEG A6003  LIES ON A SPECIAL POSITION.
REMARK 375 W2   KEG A6003  LIES ON A SPECIAL POSITION.
REMARK 375 O2   KEG A6003  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     ALA A     1
REMARK 465     VAL A     2
REMARK 465     GLY A     3
REMARK 465     ASP A     4
REMARK 465     ARG A     5
REMARK 465     CYS A     6
REMARK 465     GLU A     7
REMARK 465     ARG A     8
REMARK 465     ASN A     9
REMARK 465     GLU A    10
REMARK 465     PHE A    11
REMARK 465     GLN A    12
REMARK 465     CYS A    13
REMARK 465     GLN A    14
REMARK 465     ASP A    15
REMARK 465     GLY A    16
REMARK 465     LYS A    17
REMARK 465     CYS A    18
REMARK 465     ILE A    19
REMARK 465     SER A    20
REMARK 465     TYR A    21
REMARK 465     LYS A    22
REMARK 465     TRP A    23
REMARK 465     VAL A    24
REMARK 465     CYS A    25
REMARK 465     ASP A    26
REMARK 465     GLY A    27
REMARK 465     SER A    28
REMARK 465     ALA A    29
REMARK 465     GLU A    30
REMARK 465     CYS A    31
REMARK 465     GLN A    32
REMARK 465     ASP A    33
REMARK 465     GLY A    34
REMARK 465     SER A    35
REMARK 465     ASP A    36
REMARK 465     GLU A    37
REMARK 465     SER A    38
REMARK 465     GLN A    39
REMARK 465     GLU A    40
REMARK 465     THR A    41
REMARK 465     CYS A    42
REMARK 465     LEU A    43
REMARK 465     ARG A    57
REMARK 465     VAL A    58
REMARK 465     ASP A    75
REMARK 465     LYS A    99
REMARK 465     CYS A   100
REMARK 465     ILE A   101
REMARK 465     SER A   102
REMARK 465     VAL A   388
REMARK 465     VAL A   441
REMARK 465     GLN A   453
REMARK 465     ALA A   454
REMARK 465     ALA A   694
REMARK 465     GLU A   695
REMARK 465     ALA A   696
REMARK 465     ALA A   697
REMARK 465     VAL A   698
REMARK 465     ALA A   699
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     SER A  44    OG
REMARK 470     ASN A  59    CG   OD1
REMARK 470     GLN A  64    CG   CD   OE1  NE2
REMARK 470     GLN A  71    CG   CD   OE1  NE2
REMARK 470     VAL A  72    CG1  CG2
REMARK 470     GLN A  81    CG   CD   OE1  NE2
REMARK 470     SER A  89    OG
REMARK 470     GLN A  90    CG   CD   OE1  NE2
REMARK 470     ASP A  91    CG   OD1  OD2
REMARK 470     GLU A  92    CG   CD   OE1  OE2
REMARK 470     PHE A  93    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     ARG A  94    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 142    CG   CD   OE1  NE2
REMARK 470     GLN A 161    CG   CD   OE1  NE2
REMARK 470     ARG A 162    CG   CD   NE   CZ   NH1  NH2
REMARK 470     PHE A 181    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LEU A 184    CG   CD1  CD2
REMARK 470     ARG A 194    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A 224    CG   OD1  OD2
REMARK 470     ILE A 228    CG1  CG2  CD1
REMARK 470     GLN A 233    CG   CD   OE1  NE2
REMARK 470     ARG A 236    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 241    CG   CD   CE   NZ
REMARK 470     LYS A 262    CG   CD   CE   NZ
REMARK 470     ASP A 272    CG   OD1  OD2
REMARK 470     ARG A 282    CG   CD   NE   CZ   NH1  NH2
REMARK 470     TRP A 284    CG   CD1  CD2  NE1  CE2  CE3  CZ2
REMARK 470     TRP A 284    CZ3  CH2
REMARK 470     LYS A 312    CG   CD   CE   NZ
REMARK 470     LYS A 355    CG   CD   CE   NZ
REMARK 470     LYS A 369    CG   CD   CE   NZ
REMARK 470     LYS A 372    CG   CD   CE   NZ
REMARK 470     ARG A 385    CG   CD   NE   CZ   NH1  NH2
REMARK 470     HIS A 386    CG   ND1  CD2  CE1  NE2
REMARK 470     THR A 399    CB   OG1  CG2
REMARK 470     SER A 400    CB   OG
REMARK 470     LEU A 401    CB   CG   CD1  CD2
REMARK 470     ILE A 402    CB   CG1  CG2  CD1
REMARK 470     LEU A 405    CG   CD1  CD2
REMARK 470     ARG A 406    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 419    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 428    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 437    CG   CD   NE   CZ   NH1  NH2
REMARK 470     HIS A 439    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG A 450    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 488    CG   CD   CE   NZ
REMARK 470     LYS A 520    CG   CD   CE   NZ
REMARK 470     LYS A 522    CG   CD   CE   NZ
REMARK 470     LYS A 523    CG   CD   CE   NZ
REMARK 470     LEU A 554    CG   CD1  CD2
REMARK 470     TYR A 555    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG A 574    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 575    CG   CD   CE   NZ
REMARK 470     GLU A 579    CG   CD   OE1  OE2
REMARK 470     ARG A 583    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A 626    CG   CD1  CD2
REMARK 470     LYS A 672    CG   CD   CE   NZ
REMARK 470     ARG A 685    CG   CD   NE   CZ   NH1  NH2
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   CG   ASN A   251     N2   NAG A  3030              1.75
REMARK 500   CB   ASN A   251     N2   NAG A  3030              1.78
REMARK 500   O    CYS A   152     N    ASP A   154              1.88
REMARK 500   O    CYS A   134     N    SER A   136              1.90
REMARK 500   O    ASP A    73     OD1  ASP A    79              1.93
REMARK 500   OD1  ASN A   527     OG1  THR A   674              1.95
REMARK 500   N    LEU A   554     O    ILE A   567              1.95
REMARK 500   O    PRO A   141     N    LEU A   143              1.96
REMARK 500   ND2  ASN A   543     OG   SER A   559              1.96
REMARK 500   O    GLN A   133     C8   NAG A  2030              1.96
REMARK 500   ND2  ASN A   135     O5   NAG A  2030              1.98
REMARK 500   CB   ASN A   251     C8   NAG A  3030              2.00
REMARK 500   OH   TYR A   468     CD2  LEU A   526              2.01
REMARK 500   O    SER A   192     N    ARG A   194              2.02
REMARK 500   OH   TYR A   468     CD1  LEU A   526              2.02
REMARK 500   NH2  ARG A   499     O    GLU A   629              2.04
REMARK 500   OD2  ASP A   451     NH1  ARG A   487              2.04
REMARK 500   O    LEU A   613     N    GLY A   615              2.04
REMARK 500   CG   ASN A   135     C1   NAG A  2030              2.04
REMARK 500   O    LYS A    48     N    GLY A    50              2.05
REMARK 500   O    PHE A   105     N    CYS A   107              2.06
REMARK 500   O    CYS A   176     N    ALA A   178              2.07
REMARK 500   CA   ASN A   251     C8   NAG A  3030              2.07
REMARK 500   O    GLN A   427     N    MET A   429              2.09
REMARK 500   N    LYS A   390     O    THR A   399              2.09
REMARK 500   O    LEU A   325     CB   CYS A   331              2.10
REMARK 500   CB   ASN A   611     O    GLY A   615              2.10
REMARK 500   CB   ASN A   251     C7   NAG A  3030              2.11
REMARK 500   O    GLN A    71     OE1  GLU A    80              2.12
REMARK 500   O    HIS A   464     N    ASN A   466              2.12
REMARK 500   OD1  ASP A   147     OD2  ASP A   157              2.13
REMARK 500   O    ASN A   604     N    ALA A   606              2.13
REMARK 500   N    ASP A   280     OD2  ASP A   286              2.13
REMARK 500   O    SER A   566     N    LYS A   575              2.13
REMARK 500   O    ASP A   147     OE2  GLU A   158              2.14
REMARK 500   OD1  ASP A   149     NE2  HIS A   586              2.15
REMARK 500   O    ASP A   206     N    GLU A   208              2.16
REMARK 500   O    TRP A    66     O    ASP A    79              2.16
REMARK 500   O    PHE A   261     O    GLU A   267              2.16
REMARK 500   O    HIS A   507     N    PHE A   509              2.17
REMARK 500   O    ASN A   300     N    GLY A   303              2.17
REMARK 500   O    ILE A   467     CA   VAL A   479              2.17
REMARK 500   O    GLY A   293     OE2  GLU A   296              2.18
REMARK 500   SG   CYS A   152     N    GLY A   155              2.18
REMARK 500   C    CYS A   337     OG1  THR A   342              2.19
REMARK 500   O    LEU A   554     CA   SER A   566              2.19
REMARK 500   O    ASP A   115     N    SER A   117              2.19
REMARK 500   O    LYS A   262     N    HIS A   264              2.19
REMARK 500   CD   GLU A   180     O    ILE A   189              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   P1   KEG A  6003     O17  KEG A  6003     4556     1.52
REMARK 500   P1   KEG A  6003     O18  KEG A  6003     4556     1.52
REMARK 500   W1   KEG A  6003     O1   KEG A  6003     4556     1.62
REMARK 500   W2   KEG A  6003     O2   KEG A  6003     4556     1.63
REMARK 500   O18  KEG A  6003     O18  KEG A  6003     4556     1.70
REMARK 500   O17  KEG A  6003     O17  KEG A  6003     4556     1.72
REMARK 500   W2   KEG A  6003     O28  KEG A  6003     4556     1.83
REMARK 500   W1   KEG A  6003     O27  KEG A  6003     4556     1.85
REMARK 500   W2   KEG A  6003     O24  KEG A  6003     4556     1.85
REMARK 500   W6   KEG A  6003     O38  KEG A  6003     4556     1.86
REMARK 500   W5   KEG A  6003     O37  KEG A  6003     4556     1.86
REMARK 500   W1   KEG A  6003     O23  KEG A  6003     4556     1.89
REMARK 500   O    PHE A   673     OD1  ASP A   218     3564     1.95
REMARK 500   ND2  ASN A   570     O    ASN A   251     3564     1.97
REMARK 500   ND2  ASN A   404     OE1  GLN A   427     4556     2.14
REMARK 500   O    ARG A   574     CD   GLU A   267     3564     2.17
REMARK 500
REMARK 500 REMARK: NULL
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    CYS A 139   CB    CYS A 139   SG      0.107
REMARK 500    CYS A 343   CB    CYS A 343   SG     -0.142
REMARK 500    CYS A 356   CB    CYS A 356   SG     -0.101
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    THR A  46   N   -  CA  -  C   ANGL. DEV. = -23.9 DEGREES
REMARK 500    LYS A  48   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES
REMARK 500    PHE A  52   N   -  CA  -  C   ANGL. DEV. =  20.9 DEGREES
REMARK 500    PRO A  63   C   -  N   -  CA  ANGL. DEV. =  14.1 DEGREES
REMARK 500    TRP A  66   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES
REMARK 500    CYS A  68   CA  -  CB  -  SG  ANGL. DEV. = -21.8 DEGREES
REMARK 500    GLY A  77   N   -  CA  -  C   ANGL. DEV. = -17.5 DEGREES
REMARK 500    SER A  78   N   -  CA  -  C   ANGL. DEV. =  18.4 DEGREES
REMARK 500    GLU A  80   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES
REMARK 500    GLY A  82   N   -  CA  -  C   ANGL. DEV. = -21.1 DEGREES
REMARK 500    CYS A  83   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES
REMARK 500    PRO A  84   C   -  N   -  CA  ANGL. DEV. =  17.1 DEGREES
REMARK 500    PRO A  84   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES
REMARK 500    ARG A  94   N   -  CA  -  C   ANGL. DEV. = -20.5 DEGREES
REMARK 500    CYS A  95   CA  -  CB  -  SG  ANGL. DEV. =  16.6 DEGREES
REMARK 500    CYS A  95   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES
REMARK 500    CYS A 113   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES
REMARK 500    ASP A 118   N   -  CA  -  C   ANGL. DEV. = -22.3 DEGREES
REMARK 500    SER A 121   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES
REMARK 500    PRO A 123   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES
REMARK 500    SER A 131   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES
REMARK 500    SER A 131   C   -  N   -  CA  ANGL. DEV. = -15.9 DEGREES
REMARK 500    CYS A 134   CA  -  CB  -  SG  ANGL. DEV. =  13.0 DEGREES
REMARK 500    CYS A 134   N   -  CA  -  C   ANGL. DEV. = -29.3 DEGREES
REMARK 500    TRP A 144   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES
REMARK 500    ASP A 154   N   -  CA  -  C   ANGL. DEV. =  26.8 DEGREES
REMARK 500    ASP A 154   C   -  N   -  CA  ANGL. DEV. =  19.9 DEGREES
REMARK 500    GLN A 161   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES
REMARK 500    CYS A 163   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES
REMARK 500    LEU A 166   N   -  CA  -  C   ANGL. DEV. =  18.3 DEGREES
REMARK 500    VAL A 168   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES
REMARK 500    GLN A 170   N   -  CA  -  C   ANGL. DEV. =  18.7 DEGREES
REMARK 500    PHE A 179   N   -  CA  -  C   ANGL. DEV. = -28.4 DEGREES
REMARK 500    GLU A 180   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES
REMARK 500    CYS A 188   N   -  CA  -  C   ANGL. DEV. =  21.6 DEGREES
REMARK 500    ILE A 189   N   -  CA  -  C   ANGL. DEV. =  18.0 DEGREES
REMARK 500    PRO A 199   C   -  N   -  CA  ANGL. DEV. =  12.4 DEGREES
REMARK 500    ASP A 200   N   -  CA  -  C   ANGL. DEV. =  16.4 DEGREES
REMARK 500    CYS A 201   N   -  CA  -  C   ANGL. DEV. = -25.0 DEGREES
REMARK 500    ALA A 213   N   -  CA  -  C   ANGL. DEV. =  17.8 DEGREES
REMARK 500    PRO A 217   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES
REMARK 500    PRO A 217   C   -  N   -  CA  ANGL. DEV. =  14.6 DEGREES
REMARK 500    CYS A 222   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES
REMARK 500    HIS A 229   N   -  CA  -  C   ANGL. DEV. =  19.5 DEGREES
REMARK 500    GLY A 230   N   -  CA  -  C   ANGL. DEV. = -20.6 DEGREES
REMARK 500    SER A 231   C   -  N   -  CA  ANGL. DEV. = -19.5 DEGREES
REMARK 500    GLN A 233   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES
REMARK 500    CYS A 240   CA  -  CB  -  SG  ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP A 245   N   -  CA  -  C   ANGL. DEV. = -24.7 DEGREES
REMARK 500    CYS A 263   CA  -  CB  -  SG  ANGL. DEV. =   9.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     123 ANGLE DEVIATIONS.
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    THR A  46       41.73    172.82
REMARK 500    CYS A  47      153.72    -27.87
REMARK 500    SER A  49       87.11    -45.81
REMARK 500    ASP A  51       42.15   -104.43
REMARK 500    PHE A  52      113.39    177.76
REMARK 500    CYS A  54     -134.66   -114.64
REMARK 500    CYS A  61       76.89     78.51
REMARK 500    PRO A  63       19.41    -33.58
REMARK 500    GLN A  64       -1.27     49.32
REMARK 500    CYS A  68       34.83     34.01
REMARK 500    GLN A  71       97.27    167.06
REMARK 500    VAL A  72       94.61    -42.87
REMARK 500    ASP A  79       30.13     21.68
REMARK 500    GLU A  80        3.72    164.89
REMARK 500    GLN A  81       11.57   -160.29
REMARK 500    PRO A  84     -119.49    -38.74
REMARK 500    PRO A  85      105.75    -29.26
REMARK 500    CYS A  88       61.79     29.73
REMARK 500    GLN A  90       78.86     57.18
REMARK 500    ASP A  91       92.29    153.55
REMARK 500    GLU A  92       71.22    -66.85
REMARK 500    CYS A  95     -167.71    -58.19
REMARK 500    HIS A  96       19.71    -64.22
REMARK 500    ASP A  97      -99.35   -165.45
REMARK 500    PHE A 105       67.57   -100.93
REMARK 500    VAL A 106       46.97    -21.60
REMARK 500    CYS A 107       78.76     46.27
REMARK 500    ASP A 108       47.57    -90.66
REMARK 500    ARG A 111       76.96    -39.91
REMARK 500    ASP A 112       69.02   -111.92
REMARK 500    CYS A 113       21.98    169.98
REMARK 500    ASP A 118       90.11     74.31
REMARK 500    GLU A 119       45.99    104.82
REMARK 500    ALA A 120       40.46   -159.20
REMARK 500    SER A 121       48.57   -172.83
REMARK 500    VAL A 124      113.73   -161.49
REMARK 500    CYS A 127       96.44    -58.39
REMARK 500    PRO A 129       32.92    -51.45
REMARK 500    ALA A 130       78.07   -156.70
REMARK 500    ASN A 135       17.85    -51.52
REMARK 500    SER A 137       71.19     72.09
REMARK 500    ILE A 140      144.21   -173.48
REMARK 500    GLN A 142       65.97    -47.69
REMARK 500    LEU A 143        5.02   -154.56
REMARK 500    ALA A 145      105.48    -52.03
REMARK 500    ASN A 148       22.40    -78.84
REMARK 500    ASP A 151       27.50   -166.83
REMARK 500    GLU A 153       72.07    -60.25
REMARK 500    ASP A 154       88.08     56.39
REMARK 500    SER A 156       20.03   -147.33
REMARK 500
REMARK 500 THIS ENTRY HAS     225 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 167         0.07    SIDE CHAIN
REMARK 500    TYR A 468         0.09    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A  52        24.4      L          L   OUTSIDE RANGE
REMARK 500    SER A  53        24.4      L          L   OUTSIDE RANGE
REMARK 500    CYS A  61        24.0      L          L   OUTSIDE RANGE
REMARK 500    SER A  78        23.7      L          L   OUTSIDE RANGE
REMARK 500    ASP A  79        24.2      L          L   OUTSIDE RANGE
REMARK 500    CYS A  83        22.5      L          L   OUTSIDE RANGE
REMARK 500    THR A  87        24.2      L          L   OUTSIDE RANGE
REMARK 500    SER A 131        21.4      L          L   OUTSIDE RANGE
REMARK 500    CYS A 134        52.9      L          L   OUTSIDE RANGE
REMARK 500    TRP A 144        45.7      L          L   OUTSIDE RANGE
REMARK 500    ASP A 154        16.4      L          L   OUTSIDE RANGE
REMARK 500    LEU A 166        22.1      L          L   OUTSIDE RANGE
REMARK 500    TYR A 167        21.8      L          L   OUTSIDE RANGE
REMARK 500    VAL A 168        22.4      L          L   OUTSIDE RANGE
REMARK 500    PHE A 169        24.4      L          L   OUTSIDE RANGE
REMARK 500    GLN A 170        22.3      L          L   OUTSIDE RANGE
REMARK 500    SER A 174        24.5      L          L   OUTSIDE RANGE
REMARK 500    ALA A 178        23.4      L          L   OUTSIDE RANGE
REMARK 500    PHE A 179        48.1      L          L   OUTSIDE RANGE
REMARK 500    GLU A 180        23.1      L          L   OUTSIDE RANGE
REMARK 500    CYS A 188        19.3      L          L   OUTSIDE RANGE
REMARK 500    ASP A 200        21.7      L          L   OUTSIDE RANGE
REMARK 500    ALA A 213        23.0      L          L   OUTSIDE RANGE
REMARK 500    HIS A 229        24.0      L          L   OUTSIDE RANGE
REMARK 500    GLN A 233        22.2      L          L   OUTSIDE RANGE
REMARK 500    ASP A 245        46.8      L          L   OUTSIDE RANGE
REMARK 500    THR A 253        23.9      L          L   OUTSIDE RANGE
REMARK 500    ASP A 299        47.1      L          L   OUTSIDE RANGE
REMARK 500    VAL A 307        17.6      L          L   OUTSIDE RANGE
REMARK 500    ILE A 313        18.3      L          L   OUTSIDE RANGE
REMARK 500    LEU A 318        22.6      L          L   OUTSIDE RANGE
REMARK 500    GLN A 324        23.7      L          L   OUTSIDE RANGE
REMARK 500    VAL A 326        24.0      L          L   OUTSIDE RANGE
REMARK 500    ARG A 330        23.1      L          L   OUTSIDE RANGE
REMARK 500    CYS A 331        22.7      L          L   OUTSIDE RANGE
REMARK 500    ASP A 339        20.5      L          L   OUTSIDE RANGE
REMARK 500    ASP A 341        49.0      L          L   OUTSIDE RANGE
REMARK 500    LEU A 346        21.0      L          L   OUTSIDE RANGE
REMARK 500    PRO A 366        24.8      L          L   OUTSIDE RANGE
REMARK 500    ASP A 394        22.1      L          L   OUTSIDE RANGE
REMARK 500    ARG A 395        49.2      L          L   OUTSIDE RANGE
REMARK 500    SER A 396        24.3      L          L   OUTSIDE RANGE
REMARK 500    VAL A 409        22.2      L          L   OUTSIDE RANGE
REMARK 500    LEU A 411        20.6      L          L   OUTSIDE RANGE
REMARK 500    GLU A 414        23.8      L          L   OUTSIDE RANGE
REMARK 500    SER A 417        50.0      L          L   OUTSIDE RANGE
REMARK 500    SER A 443        22.2      L          L   OUTSIDE RANGE
REMARK 500    ASP A 445        19.2      L          L   OUTSIDE RANGE
REMARK 500    THR A 446        21.9      L          L   OUTSIDE RANGE
REMARK 500    ILE A 467        24.3      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS      68 CHIRALITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE ATOMS W1 AND W2 OF THE LIGAND
REMARK 600 KEG 6003 ARE ON A TWO-FOLD
REMARK 600 AXIS.  COORDINATES FOR THE HALF OF
REMARK 600 THE CLUSTER KEG 6003 IN THE ASYMMETRIC
REMARK 600 UNIT ARE INCLUDED IN THIS ENTRY. THE
REMARK 600 SECOND HALF OF THE CLUSTER CAN BE
REMARK 600 GENERATED USING SYMMETRY OPERATION
REMARK 600 Y,X,1-Z.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     KEG A 6003
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1008  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A  66   O
REMARK 620 2 GLN A  71   O   140.3
REMARK 620 3 ASP A  79   O    49.0  98.3
REMARK 620 4 ASP A  79   OD2  66.3  86.4  76.2
REMARK 620 5 GLU A  80   OE1  96.4  45.4  53.9  69.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1007  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 108   OD1
REMARK 620 2 ASP A 112   OD2 110.2
REMARK 620 3 ASP A 118   OD1  97.7 131.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1006  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 147   OD1
REMARK 620 2 ASP A 147   OD2  53.0
REMARK 620 3 ASP A 149   O    98.4 113.1
REMARK 620 4 ASP A 157   OD2  47.9 100.0  88.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1003  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 196   OD1
REMARK 620 2 GLY A 198   O    83.9
REMARK 620 3 ASP A 200   OD1 155.9 119.7
REMARK 620 4 ASP A 206   OD2 122.4  72.7  66.0
REMARK 620 5 GLU A 207   OE1  61.5  68.2 120.1  61.0
REMARK 620 6 LYS A 582   NZ   74.6 108.7  99.9 162.7 136.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1004  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 232   O
REMARK 620 2 GLN A 233   O    88.1
REMARK 620 3 GLU A 237   O   104.8 121.1
REMARK 620 4 GLU A 246   OE1 164.1 104.2  60.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1005  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 273   O
REMARK 620 2 ASN A 276   OD1  81.9
REMARK 620 3 ASP A 280   OD2 129.5  89.7
REMARK 620 4 ASP A 286   OD1 108.2 117.0 119.7
REMARK 620 5 GLU A 287   OE2  99.8  54.3 115.1  62.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1001  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 294   OG1
REMARK 620 2 ASN A 295   N    71.5
REMARK 620 3 GLU A 296   OE2 102.9  62.9
REMARK 620 4 ASP A 310   OD1 137.4 100.1 109.9
REMARK 620 5 LEU A 311   O    92.6 128.3 163.7  59.2
REMARK 620 6 ILE A 313   N    74.6 146.1 128.0 103.7  51.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A1002  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 333   OD1
REMARK 620 2 ASP A 333   OD2  44.0
REMARK 620 3 ILE A 334   O    65.3  77.2
REMARK 620 4 GLU A 336   OE1 134.0  96.2  87.1
REMARK 620 5 GLU A 336   OE2  88.1  58.0  56.8  46.1
REMARK 620 6 ASN A 349   OD1 131.9 173.9  97.0  85.1 120.3
REMARK 620 7 LEU A 350   O    68.2  94.2 120.1 152.4 152.1  87.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 2031
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 2032
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2033
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 2035
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 3031
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 3032
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 3033
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEG A 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEG A 6002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KEG A 6003
DBREF  1N7D A    1   699  UNP    P01130   LDLR_HUMAN      22    720
SEQADV 1N7D GLN A  494  UNP  P01130    ASN   515 ENGINEERED
SEQADV 1N7D GLN A  636  UNP  P01130    ASN   657 ENGINEERED
SEQRES   1 A  699  ALA VAL GLY ASP ARG CYS GLU ARG ASN GLU PHE GLN CYS
SEQRES   2 A  699  GLN ASP GLY LYS CYS ILE SER TYR LYS TRP VAL CYS ASP
SEQRES   3 A  699  GLY SER ALA GLU CYS GLN ASP GLY SER ASP GLU SER GLN
SEQRES   4 A  699  GLU THR CYS LEU SER VAL THR CYS LYS SER GLY ASP PHE
SEQRES   5 A  699  SER CYS GLY GLY ARG VAL ASN ARG CYS ILE PRO GLN PHE
SEQRES   6 A  699  TRP ARG CYS ASP GLY GLN VAL ASP CYS ASP ASN GLY SER
SEQRES   7 A  699  ASP GLU GLN GLY CYS PRO PRO LYS THR CYS SER GLN ASP
SEQRES   8 A  699  GLU PHE ARG CYS HIS ASP GLY LYS CYS ILE SER ARG GLN
SEQRES   9 A  699  PHE VAL CYS ASP SER ASP ARG ASP CYS LEU ASP GLY SER
SEQRES  10 A  699  ASP GLU ALA SER CYS PRO VAL LEU THR CYS GLY PRO ALA
SEQRES  11 A  699  SER PHE GLN CYS ASN SER SER THR CYS ILE PRO GLN LEU
SEQRES  12 A  699  TRP ALA CYS ASP ASN ASP PRO ASP CYS GLU ASP GLY SER
SEQRES  13 A  699  ASP GLU TRP PRO GLN ARG CYS ARG GLY LEU TYR VAL PHE
SEQRES  14 A  699  GLN GLY ASP SER SER PRO CYS SER ALA PHE GLU PHE HIS
SEQRES  15 A  699  CYS LEU SER GLY GLU CYS ILE HIS SER SER TRP ARG CYS
SEQRES  16 A  699  ASP GLY GLY PRO ASP CYS LYS ASP LYS SER ASP GLU GLU
SEQRES  17 A  699  ASN CYS ALA VAL ALA THR CYS ARG PRO ASP GLU PHE GLN
SEQRES  18 A  699  CYS SER ASP GLY ASN CYS ILE HIS GLY SER ARG GLN CYS
SEQRES  19 A  699  ASP ARG GLU TYR ASP CYS LYS ASP MET SER ASP GLU VAL
SEQRES  20 A  699  GLY CYS VAL ASN VAL THR LEU CYS GLU GLY PRO ASN LYS
SEQRES  21 A  699  PHE LYS CYS HIS SER GLY GLU CYS ILE THR LEU ASP LYS
SEQRES  22 A  699  VAL CYS ASN MET ALA ARG ASP CYS ARG ASP TRP SER ASP
SEQRES  23 A  699  GLU PRO ILE LYS GLU CYS GLY THR ASN GLU CYS LEU ASP
SEQRES  24 A  699  ASN ASN GLY GLY CYS SER HIS VAL CYS ASN ASP LEU LYS
SEQRES  25 A  699  ILE GLY TYR GLU CYS LEU CYS PRO ASP GLY PHE GLN LEU
SEQRES  26 A  699  VAL ALA GLN ARG ARG CYS GLU ASP ILE ASP GLU CYS GLN
SEQRES  27 A  699  ASP PRO ASP THR CYS SER GLN LEU CYS VAL ASN LEU GLU
SEQRES  28 A  699  GLY GLY TYR LYS CYS GLN CYS GLU GLU GLY PHE GLN LEU
SEQRES  29 A  699  ASP PRO HIS THR LYS ALA CYS LYS ALA VAL GLY SER ILE
SEQRES  30 A  699  ALA TYR LEU PHE PHE THR ASN ARG HIS GLU VAL ARG LYS
SEQRES  31 A  699  MET THR LEU ASP ARG SER GLU TYR THR SER LEU ILE PRO
SEQRES  32 A  699  ASN LEU ARG ASN VAL VAL ALA LEU ASP THR GLU VAL ALA
SEQRES  33 A  699  SER ASN ARG ILE TYR TRP SER ASP LEU SER GLN ARG MET
SEQRES  34 A  699  ILE CYS SER THR GLN LEU ASP ARG ALA HIS GLY VAL SER
SEQRES  35 A  699  SER TYR ASP THR VAL ILE SER ARG ASP ILE GLN ALA PRO
SEQRES  36 A  699  ASP GLY LEU ALA VAL ASP TRP ILE HIS SER ASN ILE TYR
SEQRES  37 A  699  TRP THR ASP SER VAL LEU GLY THR VAL SER VAL ALA ASP
SEQRES  38 A  699  THR LYS GLY VAL LYS ARG LYS THR LEU PHE ARG GLU GLN
SEQRES  39 A  699  GLY SER LYS PRO ARG ALA ILE VAL VAL ASP PRO VAL HIS
SEQRES  40 A  699  GLY PHE MET TYR TRP THR ASP TRP GLY THR PRO ALA LYS
SEQRES  41 A  699  ILE LYS LYS GLY GLY LEU ASN GLY VAL ASP ILE TYR SER
SEQRES  42 A  699  LEU VAL THR GLU ASN ILE GLN TRP PRO ASN GLY ILE THR
SEQRES  43 A  699  LEU ASP LEU LEU SER GLY ARG LEU TYR TRP VAL ASP SER
SEQRES  44 A  699  LYS LEU HIS SER ILE SER SER ILE ASP VAL ASN GLY GLY
SEQRES  45 A  699  ASN ARG LYS THR ILE LEU GLU ASP GLU LYS ARG LEU ALA
SEQRES  46 A  699  HIS PRO PHE SER LEU ALA VAL PHE GLU ASP LYS VAL PHE
SEQRES  47 A  699  TRP THR ASP ILE ILE ASN GLU ALA ILE PHE SER ALA ASN
SEQRES  48 A  699  ARG LEU THR GLY SER ASP VAL ASN LEU LEU ALA GLU ASN
SEQRES  49 A  699  LEU LEU SER PRO GLU ASP MET VAL LEU PHE HIS GLN LEU
SEQRES  50 A  699  THR GLN PRO ARG GLY VAL ASN TRP CYS GLU ARG THR THR
SEQRES  51 A  699  LEU SER ASN GLY GLY CYS GLN TYR LEU CYS LEU PRO ALA
SEQRES  52 A  699  PRO GLN ILE ASN PRO HIS SER PRO LYS PHE THR CYS ALA
SEQRES  53 A  699  CYS PRO ASP GLY MET LEU LEU ALA ARG ASP MET ARG SER
SEQRES  54 A  699  CYS LEU THR GLU ALA GLU ALA ALA VAL ALA
MODRES 1N7D ASN A  251  ASN  GLYCOSYLATION SITE
MODRES 1N7D ASN A  135  ASN  GLYCOSYLATION SITE
HET    NAG  A2030      14
HET    NAG  A2031      14
HET    BMA  A2032      11
HET    MAN  A2033      11
HET    MAN  A2035      11
HET    NAG  A3030      14
HET    NAG  A3031      14
HET    BMA  A3032      11
HET    MAN  A3033      11
HET     CA  A1001       1
HET     CA  A1002       1
HET     CA  A1003       1
HET     CA  A1004       1
HET     CA  A1005       1
HET     CA  A1006       1
HET     CA  A1007       1
HET     CA  A1008       1
HET    KEG  A6001      53
HET    KEG  A6002      53
HET    KEG  A6003      29
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     KEG 12-TUNGSTOPHOSPHATE
FORMUL   2  NAG    4(C8 H15 N O6)
FORMUL   2  BMA    2(C6 H12 O6)
FORMUL   2  MAN    3(C6 H12 O6)
FORMUL   4   CA    8(CA 2+)
FORMUL  12  KEG    3(O40 P W12)
SHEET    1   A 2 GLU A 219  GLN A 221  0
SHEET    2   A 2 CYS A 227  HIS A 229 -1  O  ILE A 228   N  PHE A 220
SHEET    1   B 2 LYS A 390  MET A 391  0
SHEET    2   B 2 TYR A 398  THR A 399 -1  O  THR A 399   N  LYS A 390
SHEET    1   C 3 ASP A 412  GLU A 414  0
SHEET    2   C 3 ARG A 419  TRP A 422 -1  O  ARG A 419   N  GLU A 414
SHEET    3   C 3 CYS A 431  GLN A 434 -1  O  CYS A 431   N  TRP A 422
SHEET    1   D 2 LEU A 458  ALA A 459  0
SHEET    2   D 2 TYR A 468  TRP A 469 -1  O  TYR A 468   N  ALA A 459
SHEET    1   E 2 VAL A 477  ALA A 480  0
SHEET    2   E 2 ARG A 487  LEU A 490 -1  O  LEU A 490   N  VAL A 477
SHEET    1   F 2 ILE A 501  VAL A 502  0
SHEET    2   F 2 TYR A 511  TRP A 512 -1  O  TYR A 511   N  VAL A 502
SHEET    1   G 2 ILE A 521  LYS A 522  0
SHEET    2   G 2 SER A 533  LEU A 534 -1  O  LEU A 534   N  ILE A 521
SHEET    1   H 4 ILE A 545  LEU A 547  0
SHEET    2   H 4 LEU A 554  ASP A 558 -1  O  TYR A 555   N  THR A 546
SHEET    3   H 4 SER A 563  ILE A 567 -1  O  ILE A 567   N  LEU A 554
SHEET    4   H 4 LYS A 575  ILE A 577 -1  O  LYS A 575   N  SER A 566
SHEET    1   I 4 ALA A 591  PHE A 593  0
SHEET    2   I 4 LYS A 596  THR A 600 -1  O  PHE A 598   N  ALA A 591
SHEET    3   I 4 ILE A 607  ASN A 611 -1  O  ALA A 610   N  VAL A 597
SHEET    4   I 4 GLY A 615  ASN A 619 -1  O  GLY A 615   N  ASN A 611
SHEET    1   J 2 LEU A 682  LEU A 683  0
SHEET    2   J 2 CYS A 690  LEU A 691 -1  N  LEU A 691   O  LEU A 682
SSBOND   1 CYS A   47    CYS A   61                          1555   1555  2.03
SSBOND   2 CYS A   54    CYS A   74                          1555   1555  2.03
SSBOND   3 CYS A   68    CYS A   83                          1555   1555  2.03
SSBOND   4 CYS A   95    CYS A  113                          1555   1555  2.05
SSBOND   5 CYS A  107    CYS A  122                          1555   1555  2.03
SSBOND   6 CYS A  127    CYS A  139                          1555   1555  2.10
SSBOND   7 CYS A  134    CYS A  152                          1555   1555  2.10
SSBOND   8 CYS A  146    CYS A  163                          1555   1555  2.04
SSBOND   9 CYS A  176    CYS A  188                          1555   1555  2.07
SSBOND  10 CYS A  183    CYS A  201                          1555   1555  2.02
SSBOND  11 CYS A  195    CYS A  210                          1555   1555  2.05
SSBOND  12 CYS A  215    CYS A  227                          1555   1555  2.01
SSBOND  13 CYS A  222    CYS A  240                          1555   1555  2.04
SSBOND  14 CYS A  234    CYS A  249                          1555   1555  2.03
SSBOND  15 CYS A  255    CYS A  268                          1555   1555  2.04
SSBOND  16 CYS A  263    CYS A  281                          1555   1555  2.03
SSBOND  17 CYS A  275    CYS A  292                          1555   1555  2.03
SSBOND  18 CYS A  297    CYS A  308                          1555   1555  2.04
SSBOND  19 CYS A  304    CYS A  317                          1555   1555  2.02
SSBOND  20 CYS A  319    CYS A  331                          1555   1555  2.02
SSBOND  21 CYS A  337    CYS A  347                          1555   1555  2.06
SSBOND  22 CYS A  343    CYS A  356                          1555   1555  2.01
SSBOND  23 CYS A  358    CYS A  371                          1555   1555  2.04
SSBOND  24 CYS A  646    CYS A  660                          1555   1555  2.06
SSBOND  25 CYS A  656    CYS A  675                          1555   1555  2.02
SSBOND  26 CYS A  677    CYS A  690                          1555   1555  2.03
LINK         ND2 ASN A 251                 C1  NAG A3030     1555   1555  1.83
LINK         C1  MAN A2033                 O6  BMA A2032     1555   1555  1.41
LINK         O3  BMA A2032                 C1  MAN A2035     1555   1555  1.40
LINK         O4  NAG A3030                 C1  NAG A3031     1555   1555  1.40
LINK         O4  NAG A3031                 C1  BMA A3032     1555   1555  1.39
LINK         O6  BMA A3032                 C1  MAN A3033     1555   1555  1.41
LINK         ND2 ASN A 135                 C1  NAG A2030     1555   1555  1.73
LINK         O4  NAG A2030                 C1  NAG A2031     1555   1555  1.40
LINK         O4  NAG A2031                 C1  BMA A2032     1555   1555  1.39
LINK         O   TRP A  66                CA    CA A1008     1555   1555  2.17
LINK         O   GLN A  71                CA    CA A1008     1555   1555  2.86
LINK         O   ASP A  79                CA    CA A1008     1555   1555  2.83
LINK         OD2 ASP A  79                CA    CA A1008     1555   1555  2.62
LINK         OE1 GLU A  80                CA    CA A1008     1555   1555  2.57
LINK         OD1 ASP A 108                CA    CA A1007     1555   1555  2.60
LINK         OD2 ASP A 112                CA    CA A1007     1555   1555  2.05
LINK         OD1 ASP A 118                CA    CA A1007     1555   1555  2.89
LINK         OD1 ASP A 147                CA    CA A1006     1555   1555  2.36
LINK         OD2 ASP A 147                CA    CA A1006     1555   1555  2.54
LINK         O   ASP A 149                CA    CA A1006     1555   1555  2.10
LINK         OD2 ASP A 157                CA    CA A1006     1555   1555  2.79
LINK         OD1 ASP A 196                CA    CA A1003     1555   1555  2.50
LINK         O   GLY A 198                CA    CA A1003     1555   1555  2.16
LINK         OD1 ASP A 200                CA    CA A1003     1555   1555  2.13
LINK         OD2 ASP A 206                CA    CA A1003     1555   1555  2.94
LINK         OE1 GLU A 207                CA    CA A1003     1555   1555  2.43
LINK         O   ARG A 232                CA    CA A1004     1555   1555  2.24
LINK         O   GLN A 233                CA    CA A1004     1555   1555  2.78
LINK         O   GLU A 237                CA    CA A1004     1555   1555  2.75
LINK         OE1 GLU A 246                CA    CA A1004     1555   1555  2.79
LINK         O   LYS A 273                CA    CA A1005     1555   1555  2.57
LINK         OD1 ASN A 276                CA    CA A1005     1555   1555  2.98
LINK         OD2 ASP A 280                CA    CA A1005     1555   1555  2.74
LINK         OD1 ASP A 286                CA    CA A1005     1555   1555  2.55
LINK         OE2 GLU A 287                CA    CA A1005     1555   1555  2.69
LINK         OG1 THR A 294                CA    CA A1001     1555   1555  2.91
LINK         N   ASN A 295                CA    CA A1001     1555   1555  2.51
LINK         OE2 GLU A 296                CA    CA A1001     1555   1555  2.78
LINK         OD1 ASP A 310                CA    CA A1001     1555   1555  2.43
LINK         O   LEU A 311                CA    CA A1001     1555   1555  2.05
LINK         N   ILE A 313                CA    CA A1001     1555   1555  2.86
LINK         OD1 ASP A 333                CA    CA A1002     1555   1555  2.99
LINK         OD2 ASP A 333                CA    CA A1002     1555   1555  2.90
LINK         O   ILE A 334                CA    CA A1002     1555   1555  2.35
LINK         OE1 GLU A 336                CA    CA A1002     1555   1555  2.79
LINK         OE2 GLU A 336                CA    CA A1002     1555   1555  2.82
LINK         OD1 ASN A 349                CA    CA A1002     1555   1555  2.23
LINK         O   LEU A 350                CA    CA A1002     1555   1555  2.10
LINK         NZ  LYS A 582                CA    CA A1003     1555   1555  2.99
CISPEP   1 ASP A  339    PRO A  340          0         2.60
SITE     1 AC1  6 PHE A 132  GLN A 133  ASN A 135  GLY A 155
SITE     2 AC1  6 GLN A 161  NAG A2031
SITE     1 AC2  2 NAG A2030  BMA A2032
SITE     1 AC3  3 NAG A2031  MAN A2033  MAN A2035
SITE     1 AC4  1 BMA A2032
SITE     1 AC5  1 BMA A2032
SITE     1 AC6  4 ASN A 251  VAL A 252  ASN A 570  NAG A3031
SITE     1 AC7  3 ASN A 667  NAG A3030  BMA A3032
SITE     1 AC8  2 NAG A3031  MAN A3033
SITE     1 AC9  1 BMA A3032
SITE     1 BC1  8 THR A 294  ASN A 295  GLU A 296  ASP A 310
SITE     2 BC1  8 LEU A 311  LYS A 312  ILE A 313  TYR A 315
SITE     1 BC2  5 ASP A 333  ILE A 334  GLU A 336  ASN A 349
SITE     2 BC2  5 LEU A 350
SITE     1 BC3  7 TRP A 193  ASP A 196  GLY A 198  ASP A 200
SITE     2 BC3  7 ASP A 206  GLU A 207  LYS A 582
SITE     1 BC4  8 ARG A 232  GLN A 233  CYS A 234  ASP A 235
SITE     2 BC4  8 GLU A 237  ASP A 239  ASP A 245  GLU A 246
SITE     1 BC5  5 LYS A 273  ASN A 276  ASP A 280  ASP A 286
SITE     2 BC5  5 GLU A 287
SITE     1 BC6  4 ASP A 147  ASP A 149  ASP A 151  ASP A 157
SITE     1 BC7  6 PHE A 105  ASP A 108  ASP A 110  ASP A 112
SITE     2 BC7  6 ASP A 118  GLU A 119
SITE     1 BC8  6 TRP A  66  ASP A  69  GLN A  71  ASP A  73
SITE     2 BC8  6 ASP A  79  GLU A  80
SITE     1 BC9  1 GLY A  55
SITE     1 CC1  4 ARG A 103  GLN A 104  SER A 449  ARG A 450
SITE     1 CC2  2 ARG A 385  ASN A 407
CRYST1  185.290  185.290   85.186  90.00  90.00 120.00 P 31 2 1      6
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      0.005397  0.003116  0.000000        0.00000
SCALE2      0.000000  0.006232  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011739        0.00000
      
PROCHECK
Go to PROCHECK summary
 References