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PDBsum entry 1nma

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Top Page protein ligands Protein-protein interface(s) links
Complex (hydrolase/immunoglobulin) PDB id
1nma
Jmol
Contents
Protein chains
378 a.a. *
109 a.a. *
122 a.a. *
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN
NAG
* Residue conservation analysis
HEADER    COMPLEX (HYDROLASE/IMMUNOGLOBULIN)      06-MAY-94   1NMA
TITLE     N9 NEURAMINIDASE COMPLEXES WITH ANTIBODIES NC41 AND NC10: EMPIRICAL
TITLE    2 FREE-ENERGY CALCULATIONS CAPTURE SPECIFICITY TRENDS OBSERVED WITH
TITLE    3 MUTANT BINDING DATA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: N9 NEURAMINIDASE;
COMPND   3 CHAIN: N;
COMPND   4 EC: 3.2.1.18;
COMPND   5 MUTATION: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: FAB NC10;
COMPND   8 CHAIN: L;
COMPND   9 OTHER_DETAILS: RESOLUTION OF 3.0 ANGSTROMS;
COMPND  10 MOL_ID: 3;
COMPND  11 MOLECULE: FAB NC10;
COMPND  12 CHAIN: H;
COMPND  13 OTHER_DETAILS: RESOLUTION OF 3.0 ANGSTROMS
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_TAXID: 11320;
SOURCE   4 MOL_ID: 2;
SOURCE   5 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   6 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   7 ORGANISM_TAXID: 10090;
SOURCE   8 OTHER_DETAILS: ISOLATED FROM MONOCLONAL MURINE ANTIBODY;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE  11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE  12 ORGANISM_TAXID: 10090;
SOURCE  13 OTHER_DETAILS: ISOLATED FROM MONOCLONAL MURINE ANTIBODY
KEYWDS    COMPLEX (HYDROLASE-IMMUNOGLOBULIN), COMPLEX (HYDROLASE-
KEYWDS   2 IMMUNOGLOBULIN) COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.R.TULIP,J.N.VARGHESE,P.M.COLMAN
REVDAT   4   13-JUL-11 1NMA    1       VERSN
REVDAT   3   24-FEB-09 1NMA    1       VERSN
REVDAT   2   01-APR-03 1NMA    1       JRNL
REVDAT   1   15-SEP-95 1NMA    0
JRNL        AUTH   W.R.TULIP,V.R.HARLEY,R.G.WEBSTER,J.NOVOTNY
JRNL        TITL   N9 NEURAMINIDASE COMPLEXES WITH ANTIBODIES NC41 AND NC10:
JRNL        TITL 2 EMPIRICAL FREE ENERGY CALCULATIONS CAPTURE SPECIFICITY
JRNL        TITL 3 TRENDS OBSERVED WITH MUTANT BINDING DATA.
JRNL        REF    BIOCHEMISTRY                  V.  33  7986 1994
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   7517697
JRNL        DOI    10.1021/BI00192A002
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   W.R.TULIP,J.N.VARGHESE,W.G.LAVER,R.G.WEBSTER,P.M.COLMAN
REMARK   1  TITL   REFINED CRYSTAL STRUCTURES OF THE INFLUENZA VIRUS N9
REMARK   1  TITL 2 NEURAMINIDASE-NC41 FAB COMPLEX
REMARK   1  REF    J.MOL.BIOL.                   V. 227   122 1992
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   P.M.COLMAN,W.R.TULIP,J.N.VARGHESE,P.A.TULLOCH,A.T.BAKER,
REMARK   1  AUTH 2 W.G.LAVER,G.M.AIR,R.G.WEBSTER
REMARK   1  TITL   THREE DIMENSIONAL STRUCTURES OF INFLUENZA VIRUS
REMARK   1  TITL 2 NEURAMINIDASE-ANTIBODY COMPLEXES
REMARK   1  REF    PHILOS.TRANS.R.SOC.LONDON,    V. 323   511 1989
REMARK   1  REF  2 SER.B
REMARK   1  REFN                   ISSN 0080-4622
REMARK   1 REFERENCE 3
REMARK   1  AUTH   W.R.TULIP,J.N.VARGHESE,R.G.WEBSTER,G.M.AIR,W.G.LAVER,
REMARK   1  AUTH 2 P.M.COLMAN
REMARK   1  TITL   CRYSTAL STRUCTURES OF NEURAMINIDASE-ANTIBODY COMPLEXES
REMARK   1  REF    COLD SPRING HARBOR            V.  54   257 1989
REMARK   1  REF  2 SYMP.QUANT.BIOL.
REMARK   1  REFN                   ISSN 0091-7451
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.200
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4777
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 86
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 3.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  NO SOLVENT ATOMS AND NO CALCIUM ATOM.  THE REFERENCE
REMARK   3  STRUCTURE FOR THE CALCIUM ATOM IS THE N9 MUTANT S370L (PDB
REMARK   3  ENTRY 2NN9).
REMARK   4
REMARK   4 1NMA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   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   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 71.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       80.10000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       80.10000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       80.10000
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       80.10000
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       80.10000
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       80.10000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       85.75000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       80.10000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       85.75000
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       85.75000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       80.10000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE COORDINATES OF THE CARBOHYDRATE 200A - 200F DO NOT
REMARK 300 REQUIRE TRANSFORMATION TO APPEAR AS PART OF THE EPITOPE.
REMARK 300 THIS CARBOHYDRATE IS COVALENTLY ATTACHED TO THE
REMARK 300 NEURAMINIDASE SUBUNIT WHICH IS NEIGHBORING TO THE ONE IN
REMARK 300 THIS FILE.
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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, L, H
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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      171.50000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      171.50000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      171.50000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      171.50000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 NEURAMINIDASE RESIDUES 458 - 468 ARE INCORRECT, ALL BEING
REMARK 400 ONE RESIDUE OUT OF REGISTER.  THEY ARE NOT PART OF ANTIBODY
REMARK 400 BINDING SITE.
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 N   459
REMARK 465     ASP N   460
REMARK 465     GLY N   461
REMARK 465     ALA N   462
REMARK 465     LYS N   463
REMARK 465     ILE N   464
REMARK 465     GLU N   465
REMARK 465     TYR N   466
REMARK 465     PHE N   467
REMARK 465     LEU N   468
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   ND2  ASN N   200     C1   NAG N   469A    3655     1.49
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    HIS N  98   NE2   HIS N  98   CD2    -0.081
REMARK 500    HIS N 144   NE2   HIS N 144   CD2    -0.067
REMARK 500    HIS N 184   NE2   HIS N 184   CD2    -0.075
REMARK 500    HIS N 274   NE2   HIS N 274   CD2    -0.071
REMARK 500    HIS N 312   NE2   HIS N 312   CD2    -0.072
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 N  88   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES
REMARK 500    TRP N  97   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TRP N  97   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES
REMARK 500    GLU N 119   CA  -  CB  -  CG  ANGL. DEV. =  13.2 DEGREES
REMARK 500    ARG N 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    TRP N 161   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP N 161   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TRP N 161   CG  -  CD2 -  CE3 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG N 172   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG N 172   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    TRP N 178   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP N 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG N 187   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG N 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    TRP N 206   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP N 206   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG N 210   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    TRP N 218   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    TRP N 218   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG N 224   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    GLN N 226   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES
REMARK 500    TYR N 256   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    TRP N 265   CD1 -  CG  -  CD2 ANGL. DEV. =   7.7 DEGREES
REMARK 500    TRP N 265   CB  -  CG  -  CD1 ANGL. DEV. =  -9.1 DEGREES
REMARK 500    TRP N 265   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    TRP N 265   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES
REMARK 500    TRP N 265   CG  -  CD2 -  CE3 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP N 295   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP N 295   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG N 300   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    TRP N 361   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    TRP N 361   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG N 364   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG N 364   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG N 371   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ARG N 371   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    THR N 401   N   -  CA  -  CB  ANGL. DEV. = -14.3 DEGREES
REMARK 500    TRP N 403   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    TRP N 403   CB  -  CG  -  CD1 ANGL. DEV. =  -8.6 DEGREES
REMARK 500    TRP N 403   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP N 403   CG  -  CD2 -  CE3 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TYR N 406   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    TRP N 412B  CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP N 412B  CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG N 430   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    TRP N 437   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    TRP N 437   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP N 438   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500    TRP N 438   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TRP N 456   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      76 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    GLU N  83      129.80   -172.46
REMARK 500    TYR N 100      -62.89   -124.64
REMARK 500    ASN N 104       38.62    -91.62
REMARK 500    ALA N 105      -51.99    -29.68
REMARK 500    ASP N 111       45.93   -148.77
REMARK 500    THR N 117     -164.49   -122.52
REMARK 500    ARG N 118      172.21    171.89
REMARK 500    GLU N 119       87.36     35.52
REMARK 500    PRO N 126        5.30    -60.02
REMARK 500    ASP N 127       11.58   -151.56
REMARK 500    ASN N 146      104.11    -57.70
REMARK 500    ARG N 152      112.09   -160.96
REMARK 500    PRO N 167       82.85    -64.30
REMARK 500    ASN N 170      -59.25    172.23
REMARK 500    THR N 181      145.94   -179.85
REMARK 500    ARG N 187      -63.83    -92.12
REMARK 500    ASN N 200       43.64   -157.97
REMARK 500    ASN N 208       71.87     60.72
REMARK 500    ARG N 209       -9.50     61.59
REMARK 500    THR N 217      104.45    -38.80
REMARK 500    ARG N 220       50.89     18.28
REMARK 500    ILE N 222       95.94     38.62
REMARK 500    THR N 225     -157.40   -127.93
REMARK 500    GLU N 227       32.54     75.30
REMARK 500    THR N 247       54.25    -91.93
REMARK 500    LYS N 264      173.06    164.99
REMARK 500    GLU N 277       98.80     55.71
REMARK 500    GLU N 283      -70.60   -138.03
REMARK 500    ALA N 285        5.77     58.42
REMARK 500    CYS N 291     -153.82   -125.22
REMARK 500    TRP N 295      -79.27    -62.14
REMARK 500    GLN N 315     -168.91   -173.42
REMARK 500    SER N 319      156.62    -49.06
REMARK 500    ASP N 330      108.26    -58.84
REMARK 500    ASN N 346       16.47     86.31
REMARK 500    ASP N 356       64.63   -118.92
REMARK 500    SER N 404     -130.83   -122.58
REMARK 500    ASP N 434        1.12    -63.81
REMARK 500    THR L   8      144.24     64.74
REMARK 500    ALA L  13      137.77   -171.99
REMARK 500    SER L  14       31.54    -87.78
REMARK 500    LEU L  15       89.78     59.09
REMARK 500    ILE L  29       34.48    -85.47
REMARK 500    SER L  30     -105.14     36.45
REMARK 500    ASN L  31       33.71   -143.50
REMARK 500    PRO L  40      -36.27    -33.61
REMARK 500    THR L  43      106.36     -8.29
REMARK 500    THR L  51      -49.04     61.29
REMARK 500    HIS L  55     -167.86    -77.73
REMARK 500    SER L  60      -22.60    -36.07
REMARK 500
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLY N  248     PRO N  249                 -145.49
REMARK 500 ARG N  327     PRO N  328                  146.03
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    ARG L 107         0.28    SIDE CHAIN
REMARK 500    ARG L 108         0.08    SIDE CHAIN
REMARK 500    TYR H  90         0.07    SIDE CHAIN
REMARK 500    ARG H 100         0.21    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    ARG N 220        24.9      L          L   OUTSIDE RANGE
REMARK 500    GLN N 226        23.6      L          L   OUTSIDE RANGE
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 NAG N 469A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 470B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA N 471C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 472D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 473E
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN N 474F
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG N 475A
DBREF  1NMA N   82   468  UNP    P05803   NRAM_IAWHM      83    470
DBREF  1NMA L    1   107  GB     501094   AAA19165       159    265
DBREF  1NMA H    2   112  GB     501094   AAA19165        24    143
SEQADV 1NMA LYS N  387  UNP  P05803    ARG   388 CONFLICT
SEQADV 1NMA ARG N  389  UNP  P05803    LYS   390 CONFLICT
SEQADV 1NMA GLN L    3  GB   501094    GLU   161 CONFLICT
SEQADV 1NMA MET L    4  GB   501094    LEU   162 CONFLICT
SEQADV 1NMA PRO H    7  GB   501094    SER    29 CONFLICT
SEQADV 1NMA LEU H  109  GB   501094    VAL   140 CONFLICT
SEQRES   1 N  388  ARG GLU PHE ASN ASN LEU THR LYS GLY LEU CYS THR ILE
SEQRES   2 N  388  ASN SER TRP HIS ILE TYR GLY LYS ASP ASN ALA VAL ARG
SEQRES   3 N  388  ILE GLY GLU ASP SER ASP VAL LEU VAL THR ARG GLU PRO
SEQRES   4 N  388  TYR VAL SER CYS ASP PRO ASP GLU CYS ARG PHE TYR ALA
SEQRES   5 N  388  LEU SER GLN GLY THR THR ILE ARG GLY LYS HIS SER ASN
SEQRES   6 N  388  GLY THR ILE HIS ASP ARG SER GLN TYR ARG ASP LEU ILE
SEQRES   7 N  388  SER TRP PRO LEU SER SER PRO PRO THR VAL TYR ASN SER
SEQRES   8 N  388  ARG VAL GLU CYS ILE GLY TRP SER SER THR SER CYS HIS
SEQRES   9 N  388  ASP GLY ARG ALA ARG MET SER ILE CYS ILE SER GLY PRO
SEQRES  10 N  388  ASN ASN ASN ALA SER ALA VAL ILE TRP TYR ASN ARG ARG
SEQRES  11 N  388  PRO VAL THR GLU ILE ASN THR TRP ALA ARG ASN ILE LEU
SEQRES  12 N  388  ARG THR GLN GLU SER GLU CYS VAL CYS GLN ASN GLY VAL
SEQRES  13 N  388  CYS PRO VAL VAL PHE THR ASP GLY SER ALA THR GLY PRO
SEQRES  14 N  388  ALA GLU THR ARG ILE TYR TYR PHE LYS GLU GLY LYS ILE
SEQRES  15 N  388  LEU LYS TRP GLU PRO LEU THR GLY THR ALA LYS HIS ILE
SEQRES  16 N  388  GLU GLU CYS SER CYS TYR GLY GLU GLN ALA GLY VAL THR
SEQRES  17 N  388  CYS THR CYS ARG ASP ASN TRP GLN GLY SER ASN ARG PRO
SEQRES  18 N  388  VAL ILE GLN ILE ASP PRO VAL ALA MET THR HIS THR SER
SEQRES  19 N  388  GLN TYR ILE CYS SER PRO VAL LEU THR ASP ASN PRO ARG
SEQRES  20 N  388  PRO ASN ASP PRO THR VAL GLY LYS CYS ASN ASP PRO TYR
SEQRES  21 N  388  PRO GLY ASN ASN ASN ASN GLY VAL LYS GLY PHE SER TYR
SEQRES  22 N  388  LEU ASP GLY GLY ASN THR TRP LEU GLY ARG THR ILE SER
SEQRES  23 N  388  ILE ALA SER ARG SER GLY TYR GLU MET LEU LYS VAL PRO
SEQRES  24 N  388  ASN ALA LEU THR ASP ASP LYS SER ARG PRO THR GLN GLY
SEQRES  25 N  388  GLN THR ILE VAL LEU ASN THR ASP TRP SER GLY TYR SER
SEQRES  26 N  388  GLY SER PHE MET ASP TYR TRP ALA GLU GLY GLU CYS TYR
SEQRES  27 N  388  ARG ALA CYS PHE TYR VAL GLU LEU ILE ARG GLY ARG PRO
SEQRES  28 N  388  LYS GLU ASP LYS VAL TRP TRP THR SER ASN SER ILE VAL
SEQRES  29 N  388  SER MET CYS SER SER THR GLU PHE LEU GLY GLN TRP ASN
SEQRES  30 N  388  TRP PRO ASP GLY ALA LYS ILE GLU TYR PHE LEU
SEQRES   1 L  109  ASP ILE GLN MET THR GLN THR THR SER SER LEU SER ALA
SEQRES   2 L  109  SER LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER
SEQRES   3 L  109  GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN ASN
SEQRES   4 L  109  PRO ASP GLY THR VAL LYS LEU LEU ILE TYR TYR THR SER
SEQRES   5 L  109  ASN LEU HIS SER GLU VAL PRO SER ARG PHE SER GLY SER
SEQRES   6 L  109  GLY SER GLY THR ASP TYR SER LEU THR ILE SER ASN LEU
SEQRES   7 L  109  GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN ASP
SEQRES   8 L  109  PHE THR LEU PRO PHE THR PHE GLY GLY GLY THR LYS LEU
SEQRES   9 L  109  GLU ILE ARG ARG ALA
SEQRES   1 H  122  GLU VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES   2 H  122  PRO GLY ALA SER VAL ARG MET SER CYS LYS ALA SER GLY
SEQRES   3 H  122  TYR THR PHE THR ASN TYR ASN MET TYR TRP VAL LYS GLN
SEQRES   4 H  122  SER PRO GLY GLN GLY LEU GLU TRP ILE GLY ILE PHE TYR
SEQRES   5 H  122  PRO GLY ASN GLY ASP THR SER TYR ASN GLN LYS PHE LYS
SEQRES   6 H  122  ASP LYS ALA THR LEU THR ALA ASP LYS SER SER ASN THR
SEQRES   7 H  122  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES   8 H  122  ALA VAL TYR TYR CYS ALA ARG SER GLY GLY SER TYR ARG
SEQRES   9 H  122  TYR ASP GLY GLY PHE ASP TYR TRP GLY GLN GLY THR THR
SEQRES  10 H  122  LEU THR VAL SER SER
MODRES 1NMA ASN N   86  ASN  GLYCOSYLATION SITE
HET    NAG  N 469A     14
HET    NAG  N 470B     14
HET    BMA  N 471C     11
HET    MAN  N 472D     11
HET    MAN  N 473E     11
HET    MAN  N 474F     11
HET    NAG  N 475A     14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
FORMUL   4  NAG    3(C8 H15 N O6)
FORMUL   4  BMA    C6 H12 O6
FORMUL   4  MAN    3(C6 H12 O6)
HELIX    1   1 ALA N  105  ASP N  111  1                                   7
HELIX    2   2 LYS N  143  SER N  145  5                                   3
HELIX    3   3 GLN L   80  ASP L   82  5                                   3
HELIX    4   4 PHE H   29  ASN H   31  5                                   3
HELIX    5   5 PHE H   63  ASP H   65  5                                   3
HELIX    6   6 LYS H   73  SER H   75  5                                   3
HELIX    7   7 SER H   84  ASP H   86  5                                   3
SHEET    1   A 4 THR N 117  ASP N 125  0
SHEET    2   A 4 GLU N 128  SER N 135 -1  N  LEU N 134   O  ARG N 118
SHEET    3   A 4 ASP N 157  PRO N 162 -1  N  TRP N 161   O  PHE N 131
SHEET    4   A 4 ARG N 172  ILE N 176 -1  N  CYS N 175   O  LEU N 158
SHEET    1   B 4 SER N 179  HIS N 184  0
SHEET    2   B 4 ARG N 189  SER N 195 -1  N  ILE N 194   O  SER N 179
SHEET    3   B 4 SER N 202  TYR N 207 -1  N  TRP N 206   O  SER N 191
SHEET    4   B 4 ARG N 210  ASN N 216 -1  N  ILE N 215   O  ALA N 203
SHEET    1   C 4 VAL N 231  GLN N 233  0
SHEET    2   C 4 VAL N 236  GLY N 244 -1  N  PRO N 238   O  VAL N 231
SHEET    3   C 4 ALA N 250  LYS N 258 -1  N  PHE N 257   O  CYS N 237
SHEET    4   C 4 LYS N 261  PRO N 267 -1  N  GLU N 266   O  ILE N 254
SHEET    1   D 4 SER N 279  GLY N 282  0
SHEET    2   D 4 VAL N 287  THR N 290 -1  N  THR N 290   O  SER N 279
SHEET    3   D 4 PRO N 301  ASP N 306 -1  N  ILE N 305   O  VAL N 287
SHEET    4   D 4 THR N 311  TYR N 316 -1  N  GLN N 315   O  VAL N 302
SHEET    1   E 4 SER N 353  ASP N 356  0
SHEET    2   E 4 ASN N 359  ARG N 364 -1  N  TRP N 361   O  TYR N 354
SHEET    3   E 4 TYR N 374  LYS N 378 -1  N  LEU N 377   O  LEU N 362
SHEET    4   E 4 GLN N 392  VAL N 398 -1  N  VAL N 398   O  TYR N 374
SHEET    1   F 4 SER N 407  MET N 411  0
SHEET    2   F 4 ALA N 420  GLY N 429 -1  N  TYR N 423   O  GLY N 408
SHEET    3   F 4 THR N 439  SER N 449 -1  N  MET N 446   O  PHE N 422
SHEET    4   F 4 SER N  96  ASP N 103 -1  N  ASP N 103   O  ILE N 443
SHEET    1   G 4 MET L   4  GLN L   6  0
SHEET    2   G 4 VAL L  19  ALA L  25 -1  N  ARG L  24   O  THR L   5
SHEET    3   G 4 ASP L  70  ILE L  75 -1  N  ILE L  75   O  VAL L  19
SHEET    4   G 4 PHE L  62  SER L  67 -1  N  SER L  67   O  ASP L  70
SHEET    1   H 3 THR L  85  GLN L  90  0
SHEET    2   H 3 LEU L  33  GLN L  38 -1  N  GLN L  38   O  THR L  85
SHEET    3   H 3 VAL L  44  ILE L  48 -1  N  ILE L  48   O  TRP L  35
SHEET    1   I 4 GLN H   3  GLN H   5  0
SHEET    2   I 4 SER H  17  SER H  25 -1  N  SER H  25   O  GLN H   3
SHEET    3   I 4 THR H  77  SER H  82A-1  N  LEU H  82   O  VAL H  18
SHEET    4   I 4 ALA H  67  ASP H  72 -1  N  ASP H  72   O  THR H  77
SHEET    1   J 2 ALA H   9  LYS H  13  0
SHEET    2   J 2 THR H 108  SER H 112  1  N  THR H 108   O  GLU H  10
SHEET    1   K 5 ASP H  56  TYR H  59  0
SHEET    2   K 5 GLU H  46  TYR H  52 -1  N  TYR H  52   O  ASP H  56
SHEET    3   K 5 ASN H  33  SER H  40 -1  N  LYS H  38   O  GLU H  46
SHEET    4   K 5 ALA H  88  SER H  95 -1  N  ALA H  93   O  TYR H  35
SHEET    5   K 5 PHE H 100E TRP H 103 -1  N  TYR H 102   O  ARG H  94
SSBOND   1 CYS N   92    CYS N  417                          1555   1555  2.00
SSBOND   2 CYS N  124    CYS N  129                          1555   1555  2.01
SSBOND   3 CYS N  175    CYS N  193                          1555   1555  1.99
SSBOND   4 CYS N  183    CYS N  230                          1555   1555  2.02
SSBOND   5 CYS N  232    CYS N  237                          1555   1555  2.01
SSBOND   6 CYS N  278    CYS N  291                          1555   1555  2.01
SSBOND   7 CYS N  280    CYS N  289                          1555   1555  2.03
SSBOND   8 CYS N  318    CYS N  337                          1555   1555  2.01
SSBOND   9 CYS N  421    CYS N  447                          1555   1555  2.03
SSBOND  10 CYS L   23    CYS L   88                          1555   1555  2.01
SSBOND  11 CYS H   22    CYS H   92                          1555   1555  2.02
LINK         ND2 ASN N  86                 C1  NAG N 475A    1555   1555  1.48
LINK         O4  NAG N 469A                C1  NAG N 470B    1555   1555  1.45
LINK         O4  NAG N 470B                C1  BMA N 471C    1555   1555  1.42
LINK         O3  BMA N 471C                C1  MAN N 472D    1555   1555  1.42
LINK         O2  MAN N 472D                C1  MAN N 473E    1555   1555  1.44
LINK         O2  MAN N 473E                C1  MAN N 474F    1555   1555  1.40
LINK         ND2 ASN N 200                 C1  NAG N 469A    4565   1555  1.49
CISPEP   1 ASN N  325    PRO N  326          0       -20.98
CISPEP   2 ARG N  430    PRO N  431          0        13.38
CISPEP   3 LEU L   94    PRO L   95          0         8.70
SITE     1 AC1  5 ASN N 200  LEU N 453  GLY N 454  GLN N 455
SITE     2 AC1  5 NAG N 470B
SITE     1 AC2  4 GLN N 392  GLY N 394  NAG N 469A BMA N 471C
SITE     1 AC3  5 LEU N 377  PRO N 390  GLY N 394  NAG N 470B
SITE     2 AC3  5 MAN N 472D
SITE     1 AC4  5 ARG N 364  GLU N 375  BMA N 471C MAN N 473E
SITE     2 AC4  5 MAN N 474F
SITE     1 AC5  5 ARG H 100  ASP N 330  ARG N 389  MAN N 472D
SITE     2 AC5  5 MAN N 474F
SITE     1 AC6  9 ARG H 100  ASP H 100B ARG N 327  ASN N 329
SITE     2 AC6  9 ASP N 330  ARG N 364  ILE N 366  MAN N 472D
SITE     3 AC6  9 MAN N 473E
SITE     1 AC7  3 PHE N  84  ASN N  86  ASN N 234
CRYST1  171.500  171.500  160.200  90.00  90.00  90.00 I 4 2 2      16
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      0.005831  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005831  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006242        0.00000
      
PROCHECK
Go to PROCHECK summary
 References