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PDBsum entry 2c6f

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2c6f
Jmol
Contents
Protein chain
612 a.a.
Ligands
NAG ×9
NAG-NAG ×2
ACT ×3
GOL ×2
Metals
_ZN ×2
_CL ×2
Waters ×24
HEADER    HYDROLASE                               09-NOV-05   2C6F
TITLE     STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME
TITLE    2 N DOMAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: N DOMAIN, RESIDUES 30-641;
COMPND   5 SYNONYM: SOMATIC ANGIOTENSIN-I CONVERTING ENZYME N DOMAIN,
COMPND   6  DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143
COMPND   7  ANTIGEN;
COMPND   8 EC: 3.4.15.1;
COMPND   9 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PEE14
KEYWDS    HYDROLASE, ANGIOTENSIN-I CONVERTING ENZYME, N DOMAIN, ZINC
KEYWDS   2 METALLOPEPTIDASE, METALLOPROTEASE, ANGIOTENSIN,
KEYWDS   3 LISINOPRIL, ALTERNATIVE SPLICING, CARBOXYPEPTIDASE,
KEYWDS   4 GLYCOPROTEIN, METAL-BINDING, PHOSPHORYLATION, PROTEASE,
KEYWDS   5 TRANSMEMBRANE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.R.CORRADI,S.L.U.SCHWAGER,A.NICHINDA,E.D.STURROCK,
AUTHOR   2 K.R.ACHARYA
REVDAT   2   24-FEB-09 2C6F    1       VERSN
REVDAT   1   08-NOV-06 2C6F    0
JRNL        AUTH   H.R.CORRADI,S.L.U.SCHWAGER,A.T.NCHINDA,
JRNL        AUTH 2 E.D.STURROCK,K.R.ACHARYA
JRNL        TITL   CRYSTAL STRUCTURE OF THE N DOMAIN OF HUMAN SOMATIC
JRNL        TITL 2 ANGIOTENSIN I-CONVERTING ENZYME PROVIDES A
JRNL        TITL 3 STRUCTURAL BASIS FOR DOMAIN-SPECIFIC INHIBITOR
JRNL        TITL 4 DESIGN.
JRNL        REF    J.MOL.BIOL.                   V. 357   964 2006
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   16476442
JRNL        DOI    10.1016/J.JMB.2006.01.048
REMARK   2
REMARK   2 RESOLUTION.    3.01 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 : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.91
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1705344.90
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7
REMARK   3   NUMBER OF REFLECTIONS             : 35643
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.224
REMARK   3   FREE R VALUE                     : 0.273
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 1441
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.6
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5410
REMARK   3   BIN R VALUE           (WORKING SET) : 0.318
REMARK   3   BIN FREE R VALUE                    : 0.408
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.2
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 237
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9736
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 210
REMARK   3   SOLVENT ATOMS            : 24
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 41
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.1
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00
REMARK   3    B22 (A**2) : 0.00
REMARK   3    B33 (A**2) : 0.00
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37
REMARK   3   ESD FROM SIGMAA              (A) : 0.49
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.47
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 1.7
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.6
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.56
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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        : 0.337654
REMARK   3   BSOL        : 25.6359
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  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2C6F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-05.
REMARK 100 THE PDBE ID CODE IS EBI-26315.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-05
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 4.90
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX14.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36858
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 4.900
REMARK 200  R MERGE                    (I) : 0.14000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.59000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1O8A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 63.6
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.4
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULPHATE, 0.1M
REMARK 280  SODIUM ACETATE, PH 4.9, 10UM ZINC SULPHATE, 15%
REMARK 280  POLYETHYLENE GLYCOL 4000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.63500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.63500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       50.56000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      105.66000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.56000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      105.66000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.63500
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.56000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      105.66000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.63500
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.56000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      105.66000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMOLECULE:  2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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      HOH Z   7  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     LEU B     1
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     LEU A   1    CG   CD1  CD2
REMARK 470     GLN A  22    CG   CD   OE1  NE2
REMARK 470     SER A  26    OG
REMARK 470     GLU A  56    CG   CD   OE1  OE2
REMARK 470     GLN A  70    CG   CD   OE1  NE2
REMARK 470     GLU A  74    CG   CD   OE1  OE2
REMARK 470     ASN A 131    CG   OD1  ND2
REMARK 470     LYS A 132    CG   CD   CE   NZ
REMARK 470     THR A 133    OG1  CG2
REMARK 470     THR A 135    OG1  CG2
REMARK 470     ASP A 140    CG   OD1  OD2
REMARK 470     GLN A 188    CG   CD   OE1  NE2
REMARK 470     ARG A 240    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A 273    CG   OD1  OD2
REMARK 470     ASP A 278    CG   OD1  OD2
REMARK 470     GLU A 305    CG   CD   OE1  OE2
REMARK 470     GLU A 315    CG   CD   OE1  OE2
REMARK 470     ASP A 324    CG   OD1  OD2
REMARK 470     GLU A 403    CG   CD   OE1  OE2
REMARK 470     LYS A 407    CG   CD   CE   NZ
REMARK 470     ASP A 412    CG   OD1  OD2
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL A 414    CG1  CG2
REMARK 470     THR A 415    OG1  CG2
REMARK 470     ASN A 416    CG   OD1  ND2
REMARK 470     LYS A 535    CG   CD   CE   NZ
REMARK 470     LYS A 542    CG   CD   CE   NZ
REMARK 470     GLU A 609    CG   CD   OE1  OE2
REMARK 470     ILE A 611    CG1  CG2  CD1
REMARK 470     ASP A 612    CG   OD1  OD2
REMARK 470     ASP B   2    CG   OD1  OD2
REMARK 470     ASN B   9    CG   OD1  ND2
REMARK 470     SER B  11    OG
REMARK 470     ASP B  13    CG   OD1  OD2
REMARK 470     LEU B  19    CG   CD1  CD2
REMARK 470     GLN B  22    CG   CD   OE1  NE2
REMARK 470     SER B  23    OG
REMARK 470     GLN B  34    CG   CD   OE1  NE2
REMARK 470     ARG B  52    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  53    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B  56    CG   CD   OE1  OE2
REMARK 470     GLN B  70    CG   CD   OE1  NE2
REMARK 470     GLU B  74    CG   CD   OE1  OE2
REMARK 470     ILE B  79    CG1  CG2  CD1
REMARK 470     THR B  84    OG1  CG2
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 132    CG   CD   CE   NZ
REMARK 470     THR B 133    OG1  CG2
REMARK 470     THR B 135    OG1  CG2
REMARK 470     ASN B 276    CG   OD1  ND2
REMARK 470     LEU B 277    CG   CD1  CD2
REMARK 470     ASP B 278    CG   OD1  OD2
REMARK 470     GLU B 315    CG   CD   OE1  OE2
REMARK 470     LYS B 341    CG   CD   CE   NZ
REMARK 470     ARG B 350    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B 403    CG   CD   OE1  OE2
REMARK 470     LEU B 410    CG   CD1  CD2
REMARK 470     ASP B 412    CG   OD1  OD2
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B 522    CG   CD   OE1  OE2
REMARK 470     ILE B 530    CD1
REMARK 470     LYS B 535    CG   CD   CE   NZ
REMARK 470     GLN B 568    CG   CD   OE1  NE2
REMARK 470     GLU B 609    CG   CD   OE1  OE2
REMARK 470     ILE B 611    CG1  CG2  CD1
REMARK 470     ASP B 612    CG   OD1  OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480   M RES CSSEQI  ATOMS
REMARK 480     ILE A  92   CD1
REMARK 480     LYS A 126    CD   CE   NZ
REMARK 480     LYS A 274    CE   NZ
REMARK 480     GLU B  77    CD  OE1  OE2
REMARK 480     LYS B 126    CD   CE
REMARK 480     LYS B 274    CD   CE   NZ
REMARK 480     GLN B 285    CD  OE1  NE2
REMARK 480     ILE B 408   CD1
REMARK 480     LYS B 542    CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   CD   PRO B     3  -  NE2  GLN B     6              2.13
REMARK 500   CG2  THR B   282  -  CB   LEU B   410              2.18
REMARK 500
REMARK 500 REMARK: NULL
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    TYR B 607   CB  -  CG  -  CD1 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TYR B 607   CB  -  CG  -  CD2 ANGL. DEV. =   4.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 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    ASN A   9      135.60   -173.83
REMARK 500    ALA A  12       36.25    -77.00
REMARK 500    ASN A  45      116.38   -173.45
REMARK 500    GLN A  81       -1.63     84.21
REMARK 500    TYR A 111      -73.46    -46.97
REMARK 500    PRO A 130      -70.90    -46.12
REMARK 500    THR A 135      120.36    -28.73
REMARK 500    ASN A 203       71.34     42.98
REMARK 500    ALA A 250      -10.86    -44.58
REMARK 500    MET A 256      -32.54    -38.83
REMARK 500    VAL A 269      118.00    -39.87
REMARK 500    PRO A 272     -165.16    -77.12
REMARK 500    LEU A 277       37.82    -86.71
REMARK 500    THR A 280      -28.67    -35.48
REMARK 500    PRO A 322      171.00    -50.25
REMARK 500    ARG A 340        8.58     52.42
REMARK 500    LYS A 341      -51.73   -122.35
REMARK 500    VAL A 351       85.97    -62.12
REMARK 500    ASP A 374       45.14    -97.40
REMARK 500    ARG A 413     -161.74   -128.96
REMARK 500    VAL A 414      101.45   -161.33
REMARK 500    PHE A 484       66.48   -152.08
REMARK 500    PHE A 490      -34.17    -36.87
REMARK 500    VAL A 495       68.66     30.91
REMARK 500    ILE A 499       -5.23    -53.14
REMARK 500    ARG A 532       17.16     51.13
REMARK 500    GLN A 545        4.17    -56.37
REMARK 500    GLU A 596       48.40    -89.86
REMARK 500    GLN A 598      -11.33     83.68
REMARK 500    PRO A 608       56.05   -141.55
REMARK 500    LEU B   5        9.37    -69.87
REMARK 500    ALA B  12       71.74   -101.35
REMARK 500    ASP B  13     -162.00   -126.67
REMARK 500    ASN B  45       88.88   -166.61
REMARK 500    THR B  47     -151.88   -123.36
REMARK 500    ILE B  79     -139.14   -119.95
REMARK 500    TRP B  80      -50.32     73.45
REMARK 500    PRO B 130       -6.61    -40.96
REMARK 500    ALA B 134      117.74     -8.89
REMARK 500    THR B 135       56.45   -173.95
REMARK 500    ALA B 185      -72.72    -47.53
REMARK 500    ASN B 203       74.15     36.53
REMARK 500    ASP B 266        1.35    -61.32
REMARK 500    VAL B 269      115.09    -38.47
REMARK 500    GLN B 285        1.18    -66.09
REMARK 500    GLU B 327      143.19    -36.27
REMARK 500    PHE B 337       10.69    -67.19
REMARK 500    ARG B 340        7.02     56.86
REMARK 500    GLN B 347      116.06   -169.81
REMARK 500    ARG B 350     -158.54   -125.15
REMARK 500    ASP B 417     -167.44   -101.96
REMARK 500    VAL B 495       59.05     38.21
REMARK 500    PRO B 497      156.00    -45.85
REMARK 500    ARG B 532       -7.75     68.22
REMARK 500    TYR B 597       -9.39    -51.14
REMARK 500    PRO B 604      130.30    -36.46
REMARK 500    PRO B 608      179.34     52.89
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 TYR A  607     PRO A  608                   36.08
REMARK 500 PRO B  275     ASN B  276                 -134.62
REMARK 500 GLY B  409     LEU B  410                 -122.16
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 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    ILE B  79       -32.6      L          D   WRONG HAND
REMARK 500    LEU B 410       -42.5      L          D   WRONG HAND
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
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                              ZN A 701  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 365   NE2
REMARK 620 2 HIS A 361   NE2 101.3
REMARK 620 3 GLU A 389   OE1  92.1 103.4
REMARK 620 4 HOH A2011   O   119.9 111.1 125.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 701  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 361   NE2
REMARK 620 2 HIS B 365   NE2  97.8
REMARK 620 3 GLU B 389   OE1  98.7  92.8
REMARK 620 N                    1     2
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 691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 692
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 697
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 696
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 692
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 693
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 694
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2434
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B2433
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C6N   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I
REMARK 900  CONVERTING ENZYME N DOMAIN WITH LISINOPRIL
DBREF  2C6F A    1   612  UNP    P12821   ACE_HUMAN       30    641
DBREF  2C6F B    1   612  UNP    P12821   ACE_HUMAN       30    641
SEQRES   1 A  612  LEU ASP PRO GLY LEU GLN PRO GLY ASN PHE SER ALA ASP
SEQRES   2 A  612  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR ASN SER
SEQRES   3 A  612  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES   4 A  612  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES   5 A  612  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES   6 A  612  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES   7 A  612  ILE TRP GLN ASN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES   8 A  612  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES   9 A  612  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER ASN
SEQRES  10 A  612  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES  11 A  612  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES  12 A  612  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES  13 A  612  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES  14 A  612  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES  15 A  612  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES  16 A  612  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES  17 A  612  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES  18 A  612  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES  19 A  612  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES  20 A  612  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES  21 A  612  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES  22 A  612  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES  23 A  612  GLY TRP ASN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES  24 A  612  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES  25 A  612  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES  26 A  612  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES  27 A  612  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES  28 A  612  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES  29 A  612  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES  30 A  612  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES  31 A  612  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES  32 A  612  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES  33 A  612  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES  34 A  612  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES  35 A  612  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES  36 A  612  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES  37 A  612  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES  38 A  612  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES  39 A  612  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES  40 A  612  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES  41 A  612  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES  42 A  612  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU GLN ALA
SEQRES  43 A  612  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES  44 A  612  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES  45 A  612  TYR PHE GLN PRO VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES  46 A  612  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES  47 A  612  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES  48 A  612  ASP
SEQRES   1 B  612  LEU ASP PRO GLY LEU GLN PRO GLY ASN PHE SER ALA ASP
SEQRES   2 B  612  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR ASN SER
SEQRES   3 B  612  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES   4 B  612  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES   5 B  612  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES   6 B  612  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES   7 B  612  ILE TRP GLN ASN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES   8 B  612  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES   9 B  612  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER ASN
SEQRES  10 B  612  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES  11 B  612  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES  12 B  612  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES  13 B  612  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES  14 B  612  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES  15 B  612  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES  16 B  612  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES  17 B  612  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES  18 B  612  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES  19 B  612  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES  20 B  612  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES  21 B  612  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES  22 B  612  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES  23 B  612  GLY TRP ASN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES  24 B  612  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES  25 B  612  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES  26 B  612  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES  27 B  612  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES  28 B  612  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES  29 B  612  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES  30 B  612  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES  31 B  612  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES  32 B  612  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES  33 B  612  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES  34 B  612  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES  35 B  612  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES  36 B  612  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES  37 B  612  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES  38 B  612  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES  39 B  612  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES  40 B  612  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES  41 B  612  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES  42 B  612  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU GLN ALA
SEQRES  43 B  612  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES  44 B  612  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES  45 B  612  TYR PHE GLN PRO VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES  46 B  612  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES  47 B  612  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE
SEQRES  48 B  612  ASP
HET    NAG  A 691      14
HET    NAG  A 696      14
HET    NAG  A 692      14
HET    NAG  A 693      14
HET    NAG  A 694      14
HET    NAG  A 695      14
HET    NAG  A 697      14
HET    NAG  B 691      14
HET    NAG  B 696      14
HET    NAG  B 692      14
HET    NAG  B 693      14
HET    NAG  B 694      14
HET    NAG  B 695      14
HET     ZN  A 701       1
HET     CL  A 702       1
HET    ACT  A 800       4
HET    ACT  A 801       4
HET     ZN  B 701       1
HET     CL  B 703       1
HET    ACT  B 801       4
HET    GOL  A2434       6
HET    GOL  B2433       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
HETNAM     ACT ACETATE ION
HETNAM     GOL GLYCEROL
HETSYN     NAG NAG
FORMUL   3  NAG    13(C8 H15 N O6)
FORMUL  12   ZN    2(ZN 2+)
FORMUL  13   CL    2(CL 1-)
FORMUL  14  ACT    3(C2 H3 O2 1-)
FORMUL  19  GOL    2(C3 H8 O3)
FORMUL  21  HOH   *24(H2 O1)
HELIX    1   1 ASP A    2  GLN A    6  5                                   5
HELIX    2   2 ASP A   13  THR A   44  1                                  32
HELIX    3   3 THR A   47  GLU A   77  1                                  31
HELIX    4   4 ASP A   85  ARG A   96  1                                  12
HELIX    5   5 LEU A   98  LEU A  103  5                                   6
HELIX    6   6 PRO A  104  ALA A  125  1                                  22
HELIX    7   7 PRO A  141  SER A  150  1                                  10
HELIX    8   8 SER A  152  GLN A  188  1                                  37
HELIX    9   9 ASP A  193  SER A  200  1                                   8
HELIX   10  10 TRP A  201  ASN A  203  5                                   3
HELIX   11  11 THR A  206  GLY A  238  1                                  33
HELIX   12  12 TRP A  261  ASN A  263  5                                   3
HELIX   13  13 ILE A  264  VAL A  269  1                                   6
HELIX   14  14 VAL A  279  GLY A  287  1                                   9
HELIX   15  15 ASN A  289  LEU A  304  1                                  16
HELIX   16  16 PRO A  310  SER A  317  1                                   8
HELIX   17  17 THR A  352  LYS A  373  1                                  22
HELIX   18  18 PRO A  376  ARG A  380  5                                   5
HELIX   19  19 ASN A  384  THR A  401  1                                  18
HELIX   20  20 ASP A  417  ILE A  433  1                                  17
HELIX   21  21 ALA A  434  SER A  451  1                                  18
HELIX   22  22 PRO A  455  SER A  457  5                                   3
HELIX   23  23 ARG A  458  GLY A  472  1                                  15
HELIX   24  24 PHE A  484  LYS A  489  5                                   6
HELIX   25  25 TYR A  498  GLY A  520  1                                  23
HELIX   26  26 PRO A  524  CYS A  528  5                                   5
HELIX   27  27 SER A  533  GLN A  545  1                                  13
HELIX   28  28 PRO A  551  GLY A  561  1                                  11
HELIX   29  29 ALA A  567  PHE A  574  1                                   8
HELIX   30  30 PHE A  574  ASN A  588  1                                  15
HELIX   31  31 GLU B   14  THR B   44  1                                  31
HELIX   32  32 ALA B   48  TYR B   76  1                                  29
HELIX   33  33 ASP B   85  ARG B   96  1                                  12
HELIX   34  34 LEU B   98  LEU B  103  5                                   6
HELIX   35  35 PRO B  104  SER B  123  1                                  20
HELIX   36  36 PRO B  141  SER B  150  1                                  10
HELIX   37  37 SER B  152  ILE B  169  1                                  18
HELIX   38  38 LEU B  171  GLN B  188  1                                  18
HELIX   39  39 ASP B  193  SER B  200  1                                   8
HELIX   40  40 TRP B  201  ASN B  203  5                                   3
HELIX   41  41 THR B  206  GLY B  238  1                                  33
HELIX   42  42 TRP B  261  VAL B  268  5                                   8
HELIX   43  43 VAL B  279  GLN B  285  1                                   7
HELIX   44  44 ASN B  289  LEU B  304  1                                  16
HELIX   45  45 PRO B  310  SER B  317  1                                   8
HELIX   46  46 THR B  352  TYR B  372  1                                  21
HELIX   47  47 PRO B  376  ARG B  380  5                                   5
HELIX   48  48 ASN B  384  THR B  401  1                                  18
HELIX   49  49 THR B  401  LYS B  407  1                                   7
HELIX   50  50 THR B  418  LYS B  432  1                                  15
HELIX   51  51 ALA B  434  SER B  451  1                                  18
HELIX   52  52 PRO B  455  TYR B  459  5                                   5
HELIX   53  53 ASN B  460  GLN B  471  1                                  12
HELIX   54  54 PHE B  484  LYS B  489  5                                   6
HELIX   55  55 TYR B  498  ALA B  519  1                                  22
HELIX   56  56 PRO B  524  CYS B  528  5                                   5
HELIX   57  57 SER B  533  GLN B  545  1                                  13
HELIX   58  58 PRO B  551  VAL B  560  1                                  10
HELIX   59  59 ALA B  567  GLY B  589  1                                  23
SHEET    1  AA 2 LYS A 126  VAL A 127  0
SHEET    2  AA 2 TRP A 137  SER A 138 -1  O  TRP A 137   N  VAL A 127
SHEET    1  AB 2 ILE A 248  PRO A 249  0
SHEET    2  AB 2 ILE A 473  CYS A 474  1  N  CYS A 474   O  ILE A 248
SHEET    1  AC 2 SER A 333  ASP A 336  0
SHEET    2  AC 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335
SHEET    1  BA 2 ILE B 248  PRO B 249  0
SHEET    2  BA 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248
SHEET    1  BB 2 SER B 333  ASP B 336  0
SHEET    2  BB 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  1.56
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.06
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.00
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.06
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.01
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03
LINK         ND2 ASN A  25                 C1  NAG A 693     1555   1555  1.48
LINK         ND2 ASN A  45                 C1  NAG A 692     1555   1555  1.45
LINK         ND2 ASN A  45                 O5  NAG A 692     1555   1555  2.02
LINK         ND2 ASN A 117                 C1  NAG A 695     1555   1555  1.48
LINK         ND2 ASN A 289                 C1  NAG A 697     1555   1555  1.47
LINK         ND2 ASN A 289                 O5  NAG A 697     1555   1555  1.82
LINK         ND2 ASN A 480                 C1  NAG A 691     1555   1555  1.46
LINK         OE2 GLU A 596                 O7  NAG A 691     3554   1555  2.01
LINK         O4  NAG A 691                 C1  NAG A 696     1555   1555  1.48
LINK         O4  NAG A 691                 C2  NAG A 696     1555   1555  2.02
LINK         O4  NAG A 693                 C1  NAG A 694     1555   1555  1.47
LINK        ZN    ZN A 701                 NE2 HIS A 365     1555   1555  2.30
LINK        ZN    ZN A 701                 NE2 HIS A 361     1555   1555  2.10
LINK        ZN    ZN A 701                 O   HOH A2011     1555   1555  2.64
LINK        ZN    ZN A 701                 OE1 GLU A 389     1555   1555  1.99
LINK         ND2 ASN B  25                 C1  NAG B 693     1555   1555  1.48
LINK         ND2 ASN B  25                 O5  NAG B 693     1555   1555  2.05
LINK         ND2 ASN B  45                 C1  NAG B 692     1555   1555  1.43
LINK         ND2 ASN B 117                 C1  NAG B 695     1555   1555  1.45
LINK         ND2 ASN B 480                 C1  NAG B 691     1555   1555  1.47
LINK         O4  NAG B 691                 C1  NAG B 696     1555   1555  1.43
LINK         O4  NAG B 693                 C1  NAG B 694     1555   1555  1.48
LINK        ZN    ZN B 701                 NE2 HIS B 365     1555   1555  2.17
LINK        ZN    ZN B 701                 OE1 GLU B 389     1555   1555  1.82
LINK        ZN    ZN B 701                 NE2 HIS B 361     1555   1555  2.12
CISPEP   1 ASP A  140    PRO A  141          0        10.03
CISPEP   2 ASP B  140    PRO B  141          0        -5.83
SITE     1 AC1  6 ARG A 245  ASN A 480  THR A 482  HIS A 483
SITE     2 AC1  6 GLU A 596  NAG A 696
SITE     1 AC2  1 NAG A 691
SITE     1 AC3  4 ASN A  45  THR A  47  ASN A  50  ARG A 326
SITE     1 AC4  4 ASN A  25  SER A  26  ARG A 340  NAG A 694
SITE     1 AC5  2 ARG A 340  NAG A 693
SITE     1 AC6  4 LEU A 114  ASN A 117  ARG A 120  LEU A 174
SITE     1 AC7  8 ASN A 289  THR A 291  HIS A 292  GLU A 320
SITE     2 AC7  8 HIS A 406  LYS A 407  ILE A 408  GLY A 409
SITE     1 AC8  4 ASN B 480  THR B 482  GLU B 596  NAG B 696
SITE     1 AC9  1 NAG B 691
SITE     1 BC1  4 ASN B  45  THR B  47  ASN B  50  ARG B 326
SITE     1 BC2  5 ASN B  25  SER B  26  GLU B  29  ARG B 340
SITE     2 BC2  5 NAG B 694
SITE     1 BC3  2 ARG B 340  NAG B 693
SITE     1 BC4  3 LEU B 114  ASN B 117  LEU B 174
SITE     1 BC5  4 HIS A 361  HIS A 365  GLU A 389  HOH A2011
SITE     1 BC6  4 TYR B 202  PRO B 385  PRO B 497  ARG B 500
SITE     1 BC7  3 ARG A 453  ASP A 462  TYR A 465
SITE     1 BC8  4 GLN A 259  LYS A 489  HIS A 491  TYR A 498
SITE     1 BC9  4 HIS B 361  HIS B 365  GLU B 389  HOH B2013
SITE     1 CC1  3 TYR A 202  PRO A 497  ARG A 500
SITE     1 CC2  4 GLN B 259  LYS B 489  HIS B 491  TYR B 498
SITE     1 CC3  6 GLU A 219  LEU A 223  ARG A 458  LYS A 469
SITE     2 CC3  6 GLY A 593  TRP A 594
SITE     1 CC4  6 GLN A 586  GLU B 219  ARG B 458  LYS B 469
SITE     2 CC4  6 GLY B 593  TRP B 594
CRYST1  101.120  211.320  171.270  90.00  90.00  90.00 C 2 2 21     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      0.009889  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004732  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005839        0.00000
MTRIX1   1  0.006620  0.999960 -0.005230       -0.61786    1
MTRIX2   1  0.999890 -0.006690 -0.013180       -0.64509    1
MTRIX3   1 -0.013220 -0.005140 -0.999900     -128.55352    1
      
PROCHECK
Go to PROCHECK summary
 References