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PDBsum entry 2c6n

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Hydrolase/hydrolase inhibitor PDB id
2c6n
Jmol
Contents
Protein chain
612 a.a.
Ligands
NAG-NAG ×2
NAG ×3
LPR ×2
GOL ×2
NDG
ACT
Metals
_ZN ×2
_CL ×2
Waters ×19
HEADER    HYDROLASE/HYDROLASE INHIBITOR           10-NOV-05   2C6N
TITLE     STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME N DOMAIN
TITLE    2 WITH LISINOPRIL
CAVEAT     2C6N    CHIRALITY ERROR AT THE CB CENTER OF ILE 530 B
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME, SOMATIC ISOFORM;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: N DOMAIN, RESIDUES 38-649;
COMPND   5 SYNONYM: SOMATIC ANGIOTENSIN-I CONVERTING ENZYME N DOMAIN,
COMPND   6  DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143 ANTIGEN;
COMPND   7 EC: 3.4.15.1;
COMPND   8 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: HOMO SAPIENS;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;
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, LISINOPRIL,
KEYWDS   3 CARBOXYPEPTIDASE, GLYCOPROTEIN, METAL-BINDING, PHOSPHORYLATION,
KEYWDS   4 PROTEASE, TRANSMEMBRANE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.R.CORRADI,S.L.U.SCHWAGER,A.T.NICHINDA,E.D.STURROCK,K.R.ACHARYA
REVDAT   4   13-JUL-11 2C6N    1       VERSN
REVDAT   3   24-FEB-09 2C6N    1       VERSN
REVDAT   2   22-MAR-06 2C6N    1       SOURCE JRNL
REVDAT   1   15-MAR-06 2C6N    0
JRNL        AUTH   H.R.CORRADI,S.L.U.SCHWAGER,A.T.NCHINDA,
JRNL        AUTH 2 E.D.STURROCKK.R.ACHARYA
JRNL        TITL   CRYSTAL STRUCTURE OF THE N DOMAIN OF HUMAN SOMATIC
JRNL        TITL 2 ANGIOTENSIN I-CONVERTING ENZYME PROVIDES A STRUCTURAL BASIS
JRNL        TITL 3 FOR DOMAIN-SPECIFIC INHIBITOR 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.    3.00 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) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.76
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2443102.530
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.1
REMARK   3   NUMBER OF REFLECTIONS             : 35238
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) : 0.294
REMARK   3   FREE R VALUE                     : 0.308
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 903
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010
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) (%) : 86.10
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5119
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3750
REMARK   3   BIN FREE R VALUE                    : 0.3560
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.50
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 130
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9412
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 190
REMARK   3   SOLVENT ATOMS            : 19
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 50.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.20
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.50
REMARK   3   ESD FROM SIGMAA              (A) : 0.61
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) : 0.54
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 2.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.95
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        : 0.35
REMARK   3   BSOL        : 39.17
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2C6N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-05.
REMARK 100 THE PDBE ID CODE IS EBI-26323.
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 : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36858
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.12000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.2000
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) : 3.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 63.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULPHATE, 0.1M SODIUM
REMARK 280  ACETATE, PH 4.9, 10UM ZINC SULPHATE, 18% 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       85.50000
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       85.50000
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       50.65000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      105.45000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.65000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      105.45000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.50000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.65000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      105.45000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.50000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.65000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      105.45000
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 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
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 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 465     ASN B   276
REMARK 465     ASP B   612
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  18    CG   CD   OE1  NE2
REMARK 470     GLN A  22    CG   CD   OE1  NE2
REMARK 470     SER A  23    OG
REMARK 470     TYR A  24    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     SER A  26    OG
REMARK 470     GLN A  30    CG   CD   OE1  NE2
REMARK 470     GLU A  49    CG   CD   OE1  OE2
REMARK 470     GLU A  56    CG   CD   OE1  OE2
REMARK 470     LEU A  60    CG   CD1  CD2
REMARK 470     GLN A  70    CG   CD   OE1  NE2
REMARK 470     LYS A  71    CG   CD   CE   NZ
REMARK 470     GLU A  74    CG   CD   OE1  OE2
REMARK 470     ILE A  79    CG1  CG2  CD1
REMARK 470     TRP A  80    CG   CD1  CD2  NE1  CE2  CE3  CZ2
REMARK 470     TRP A  80    CZ3  CH2
REMARK 470     GLN A  81    CG   CD   OE1  NE2
REMARK 470     LEU A  88    CG   CD1  CD2
REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A  98    CG   CD1  CD2
REMARK 470     LEU A 105    CG   CD1  CD2
REMARK 470     ASN A 131    CG   OD1
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     GLN A 188    CG   CD   OE1  NE2
REMARK 470     ASN A 203    CG   OD1
REMARK 470     ARG A 240    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A 273    CG   OD1  OD2
REMARK 470     ASN A 276    CG   OD1
REMARK 470     ASP A 278    CG   OD1  OD2
REMARK 470     THR A 280    OG1  CG2
REMARK 470     SER A 281    OG
REMARK 470     GLN A 285    CG   CD   OE1  NE2
REMARK 470     ASN A 289    CG   OD1
REMARK 470     THR A 291    OG1  CG2
REMARK 470     HIS A 292    CG   ND1  CD2  CE1  NE2
REMARK 470     VAL A 296    CG1  CG2
REMARK 470     SER A 303    OG
REMARK 470     GLU A 305    CG   CD   OE1  OE2
REMARK 470     GLU A 315    CG   CD   OE1  OE2
REMARK 470     LYS A 321    CG   CD   CE   NZ
REMARK 470     ASP A 324    CG   OD1  OD2
REMARK 470     GLU A 327    CG   CD   OE1  OE2
REMARK 470     ARG A 340    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 341    CG   CD   CE   NZ
REMARK 470     ARG A 344    CG   CD   NE   CZ   NH1  NH2
REMARK 470     MET A 353    CG   SD   CE
REMARK 470     SER A 357    OG
REMARK 470     LEU A 375    CG   CD1  CD2
REMARK 470     VAL A 377    CG1  CG2
REMARK 470     ARG A 380    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 403    CG   CD   OE1  OE2
REMARK 470     LYS A 407    CG   CD   CE   NZ
REMARK 470     LEU A 410    CG   CD1  CD2
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
REMARK 470     LEU A 515    CG   CD1  CD2
REMARK 470     LYS A 542    CG   CD   CE   NZ
REMARK 470     GLN A 545    CG   CD   OE1  NE2
REMARK 470     SER A 548    OG
REMARK 470     GLN A 568    CG   CD   OE1  NE2
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     GLN B   6    CG   CD   OE1  NE2
REMARK 470     ASN B   9    CG   OD1
REMARK 470     SER B  11    OG
REMARK 470     ASP B  13    CG   OD1  OD2
REMARK 470     GLU B  14    CG   CD   OE1  OE2
REMARK 470     GLN B  18    CG   CD   OE1  NE2
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     TYR B  24    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     SER B  26    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     LYS B  71    CG   CD   CE   NZ
REMARK 470     LYS B  73    CG   CD   CE   NZ
REMARK 470     GLU B  74    CG   CD   OE1  OE2
REMARK 470     ILE B  79    CG1  CG2  CD1
REMARK 470     GLN B  81    CG   CD   OE1  NE2
REMARK 470     PHE B  83    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     THR B  84    OG1  CG2
REMARK 470     LEU B  88    CG   CD1  CD2
REMARK 470     ARG B  89    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU B 105    CG   CD1  CD2
REMARK 470     LYS B 126    CG   CD   CE   NZ
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     GLU B 184    CG   CD   OE1  OE2
REMARK 470     LYS B 187    CG   CD   CE   NZ
REMARK 470     SER B 200    OG
REMARK 470     ASN B 203    CG   OD1
REMARK 470     SER B 204    OG
REMARK 470     GLU B 262    CG   CD   OE1  OE2
REMARK 470     VAL B 269    CG1  CG2
REMARK 470     LYS B 274    CG   CD   CE   NZ
REMARK 470     LEU B 277    CG   CD1  CD2
REMARK 470     LEU B 284    CG   CD1  CD2
REMARK 470     GLN B 285    CG   CD   OE1  NE2
REMARK 470     HIS B 292    CG   ND1  CD2  CE1  NE2
REMARK 470     ARG B 295    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU B 299    CG   CD   OE1  OE2
REMARK 470     LEU B 306    CG   CD1  CD2
REMARK 470     GLU B 312    CG   CD   OE1  OE2
REMARK 470     GLU B 315    CG   CD   OE1  OE2
REMARK 470     SER B 317    OG
REMARK 470     SER B 333    OG
REMARK 470     LYS B 341    CG   CD   CE   NZ
REMARK 470     ARG B 344    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE B 345    CG1  CG2  CD1
REMARK 470     ARG B 350    CG   CD   NE   CZ   NH1  NH2
REMARK 470     MET B 353    CG   SD   CE
REMARK 470     ASP B 354    CG   OD1  OD2
REMARK 470     GLN B 355    CG   CD   OE1  NE2
REMARK 470     LEU B 356    CG   CD1  CD2
REMARK 470     ASP B 374    CG   OD1  OD2
REMARK 470     LEU B 375    CG   CD1  CD2
REMARK 470     VAL B 377    CG1  CG2
REMARK 470     ARG B 380    CD   NE   CZ   NH1  NH2
REMARK 470     SER B 400    OG
REMARK 470     GLU B 403    CG   CD   OE1  OE2
REMARK 470     LEU B 405    CG   CD1  CD2
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     GLN B 444    CG   CD   OE1  NE2
REMARK 470     SER B 451    OG
REMARK 470     GLU B 513    CG   CD   OE1  OE2
REMARK 470     LEU B 515    CG   CD1  CD2
REMARK 470     GLU B 522    CG   CD   OE1  OE2
REMARK 470     ILE B 530    CD1
REMARK 470     SER B 533    OG
REMARK 470     LYS B 535    CG   CD   CE   NZ
REMARK 470     LYS B 539    CG   CD   CE   NZ
REMARK 470     SER B 548    OG
REMARK 470     ARG B 550    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN B 553    CG   CD   OE1  NE2
REMARK 470     VAL B 555    CG1  CG2
REMARK 470     LEU B 562    CG   CD1  CD2
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 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; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     ILE A   46   CD1
REMARK 480     ILE A   92   CD1
REMARK 480     LYS A  126   CE   NZ
REMARK 480     LYS A  274   CD   CE   NZ
REMARK 480     GLU B   66   CD   OE1  OE2
REMARK 480     LEU B   98   CD1  CD2
REMARK 480     ILE B  408   CD1
REMARK 480     LYS B  427   CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLY A    16     OH   TYR A    76              1.99
REMARK 500   O    GLY B     4     N    GLN B     6              2.03
REMARK 500   ND2  ASN B   480     O5   NAG B   691              2.06
REMARK 500   OD1  ASN A   480     C1   NAG A   691              2.07
REMARK 500   O    LEU B   129     N    ASN B   131              2.08
REMARK 500   NH1  ARG B   235     O    HOH B  2004              2.10
REMARK 500   O    THR B   280     N    MET B   283              2.18
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    ARG A 381   CB    ARG A 381   CG      0.221
REMARK 500    ARG A 381   CG    ARG A 381   CD      0.151
REMARK 500    ASN B  25   CB    ASN B  25   CG     -0.147
REMARK 500    ARG B 541   CB    ARG B 541   CG      0.167
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLU A  63   C   -  N   -  CA  ANGL. DEV. = -16.9 DEGREES
REMARK 500    LEU A 174   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    THR A 280   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES
REMARK 500    THR A 349   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES
REMARK 500    VAL A 351   N   -  CA  -  CB  ANGL. DEV. = -17.1 DEGREES
REMARK 500    ARG A 380   N   -  CA  -  C   ANGL. DEV. = -18.3 DEGREES
REMARK 500    ARG A 381   CB  -  CA  -  C   ANGL. DEV. =  12.7 DEGREES
REMARK 500    ARG A 380   CA  -  C   -  N   ANGL. DEV. = -13.7 DEGREES
REMARK 500    PRO A 402   C   -  N   -  CA  ANGL. DEV. =  12.2 DEGREES
REMARK 500    GLY A 523   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES
REMARK 500    PRO A 524   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES
REMARK 500    ARG A 550   CA  -  CB  -  CG  ANGL. DEV. =  13.5 DEGREES
REMARK 500    PRO A 551   C   -  N   -  CA  ANGL. DEV. =  10.8 DEGREES
REMARK 500    PRO B   3   N   -  CA  -  C   ANGL. DEV. =  20.9 DEGREES
REMARK 500    LEU B   5   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES
REMARK 500    TYR B  76   N   -  CA  -  C   ANGL. DEV. =  22.2 DEGREES
REMARK 500    PRO B  78   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES
REMARK 500    PRO B  78   C   -  N   -  CD  ANGL. DEV. = -27.3 DEGREES
REMARK 500    GLU B 305   N   -  CA  -  C   ANGL. DEV. =  26.5 DEGREES
REMARK 500    PRO B 308   C   -  N   -  CD  ANGL. DEV. = -31.9 DEGREES
REMARK 500    ARG B 350   C   -  N   -  CA  ANGL. DEV. = -18.7 DEGREES
REMARK 500    LEU B 441   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    ARG B 541   C   -  N   -  CA  ANGL. DEV. = -16.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PRO A   7      -91.50    -39.22
REMARK 500    ARG A  53      -70.15    -59.48
REMARK 500    LEU A  75       -4.48   -140.27
REMARK 500    GLN A  81       -0.81     94.18
REMARK 500    GLN A  87        3.61    -59.57
REMARK 500    ALA A 101       -1.17    -53.44
REMARK 500    PRO A 104      152.45    -50.00
REMARK 500    TYR A 111      -73.34    -45.25
REMARK 500    PRO A 130      -71.05    -65.98
REMARK 500    LYS A 132      104.85    -58.65
REMARK 500    THR A 133       71.21    -64.59
REMARK 500    ASP A 189       20.73    -79.55
REMARK 500    PHE A 191      176.15    -58.01
REMARK 500    ALA A 250      -13.77    -47.89
REMARK 500    MET A 256      -35.87    -37.85
REMARK 500    GLU A 262        1.19    -55.16
REMARK 500    VAL A 269      118.27    -38.77
REMARK 500    PRO A 272     -164.05    -76.04
REMARK 500    LEU A 277       41.17    -81.82
REMARK 500    GLU A 298      -73.29    -60.36
REMARK 500    GLU A 299      -27.67    -35.98
REMARK 500    LEU A 304       47.49    -78.17
REMARK 500    PRO A 322      165.70    -42.24
REMARK 500    ASP A 324        0.21    -67.85
REMARK 500    ARG A 326       91.87    -63.44
REMARK 500    GLU A 327      114.36    -34.18
REMARK 500    ARG A 340       10.66     50.78
REMARK 500    GLN A 347      143.13   -172.67
REMARK 500    VAL A 351       53.94     36.43
REMARK 500    ASP A 374       42.60    -75.53
REMARK 500    PRO A 376     -158.48    -65.62
REMARK 500    ARG A 380      -16.91   -141.39
REMARK 500    ILE A 391      -49.73    -29.23
REMARK 500    ASN A 416       45.53    -82.90
REMARK 500    ASP A 417     -166.90   -105.55
REMARK 500    ARG A 458       25.58   -141.79
REMARK 500    GLU A 481       36.96    -87.42
REMARK 500    PHE A 484       74.19   -150.83
REMARK 500    PHE A 490      -38.40    -31.48
REMARK 500    VAL A 495       68.55     36.31
REMARK 500    ILE A 499       -0.52    -53.13
REMARK 500    ILE A 530       28.39    -74.24
REMARK 500    ARG A 532       18.07     49.24
REMARK 500    GLN A 545        3.65    -65.18
REMARK 500    GLU A 596       54.23    -90.60
REMARK 500    GLN A 598      -11.92     82.60
REMARK 500    PRO A 604     -156.85    -55.72
REMARK 500    ASN A 606       97.47   -160.89
REMARK 500    PRO B   3     -130.31     -0.42
REMARK 500    LEU B   5       70.50    -64.65
REMARK 500
REMARK 500 THIS ENTRY HAS      92 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 PHE B   83     THR B   84                  149.98
REMARK 500 ASP B   85     PRO B   86                  114.34
REMARK 500 PRO B   86     GLN B   87                   87.10
REMARK 500 ASP B  140     PRO B  141                   34.38
REMARK 500 GLU B  609     GLY B  610                  148.15
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 B  76         0.08    SIDE CHAIN
REMARK 500    TYR B 215         0.07    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    ARG A 380        -10.01
REMARK 500    ARG B 541         11.74
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    THR A 349        22.5      L          L   OUTSIDE RANGE
REMARK 500    ARG A 350        17.8      L          L   OUTSIDE RANGE
REMARK 500    PRO B   3        19.8      L          L   OUTSIDE RANGE
REMARK 500    GLU B  74        24.5      L          L   OUTSIDE RANGE
REMARK 500    TYR B  76        22.6      L          L   OUTSIDE RANGE
REMARK 500    PRO B  78        46.2      L          L   OUTSIDE RANGE
REMARK 500    GLU B 305        17.1      L          L   OUTSIDE RANGE
REMARK 500    ARG B 326        24.5      L          L   OUTSIDE RANGE
REMARK 500    ILE B 530       -33.0      S          R   CBETA WRONG HAND
REMARK 500
REMARK 500 REMARK: NULL
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 LPR A 705   O3  116.7
REMARK 620 3 GLU A 389   OE1 103.0  95.6
REMARK 620 4 LPR A 705   O2  101.2  50.2 144.7
REMARK 620 5 HIS A 361   NE2 108.7 118.4 112.8  82.8
REMARK 620 N                    1     2     3     4
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 365   NE2
REMARK 620 2 GLU B 389   OE1  83.4
REMARK 620 3 LPR B 705   O2   94.4 153.7
REMARK 620 4 LPR B 705   O3  126.5  94.1  66.1
REMARK 620 5 HIS B 361   NE2 106.8 122.6  83.2 118.6
REMARK 620 N                    1     2     3     4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: [N2-[(S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-PROLINE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630   M RES C SSSEQI
REMARK 630     LPR A   705
REMARK 630     LPR B   705
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP:    CLT LYS PRO
REMARK 630 DETAILS: 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 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 693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LPR A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LPR B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2433
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A2434
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C6F   RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I CONVERTING ENZYME
REMARK 900 N DOMAIN
DBREF  2C6N A    1   612  UNP    Q59GY8   ACE_HUMAN       38    649
DBREF  2C6N B    1   612  UNP    Q59GY8   ACE_HUMAN       38    649
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
MODRES 2C6N ASN A   25  ASN  GLYCOSYLATION SITE
MODRES 2C6N ASN A  117  ASN  GLYCOSYLATION SITE
MODRES 2C6N ASN A  480  ASN  GLYCOSYLATION SITE
MODRES 2C6N ASN B   25  ASN  GLYCOSYLATION SITE
MODRES 2C6N ASN B  117  ASN  GLYCOSYLATION SITE
MODRES 2C6N ASN B  480  ASN  GLYCOSYLATION SITE
HET    NAG  A 691      14
HET    NAG  A 696      14
HET    NAG  A 693      14
HET    NAG  A 695      14
HET     ZN  A 701       1
HET     CL  A 703       1
HET    LPR  A 705      29
HET    GOL  A2433       6
HET    GOL  A2434       6
HET    NAG  B 691      14
HET    NAG  B 696      14
HET    NDG  B 693      14
HET    NAG  B 695      14
HET     ZN  B 701       1
HET     CL  B 702       1
HET    LPR  B 705      29
HET    ACT  B 710       4
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
HETNAM     LPR [N2-[(S)-1-CARBOXY-3-PHENYLPROPYL]-L-LYSYL-L-PROLINE
HETNAM     GOL GLYCEROL
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     ACT ACETATE ION
HETSYN     LPR LISINOPRIL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  NAG    7(C8 H15 N O6)
FORMUL   6   ZN    2(ZN 2+)
FORMUL   7   CL    2(CL 1-)
FORMUL   8  LPR    2(C21 H31 N3 O5)
FORMUL   9  GOL    2(C3 H8 O3)
FORMUL  12  NDG    C8 H15 N O6
FORMUL  17  ACT    C2 H3 O2 1-
FORMUL  18  HOH   *19(H2 O)
HELIX    1   1 ASP A    2  GLN A    6  5                                   5
HELIX    2   2 ASP A   13  ALA A   15  5                                   3
HELIX    3   3 GLY A   16  ASN A   45  1                                  30
HELIX    4   4 THR A   47  GLU A   77  1                                  31
HELIX    5   5 ASP A   85  ARG A   96  1                                  12
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  LYS A  187  1                                  36
HELIX    9   9 ASP A  193  ARG A  199  1                                   7
HELIX   10  10 THR A  206  GLY A  238  1                                  33
HELIX   11  11 ILE A  264  VAL A  269  1                                   6
HELIX   12  12 SER A  281  GLY A  287  1                                   7
HELIX   13  13 ASN A  289  LEU A  304  1                                  16
HELIX   14  14 PRO A  310  GLY A  316  1                                   7
HELIX   15  15 THR A  352  LYS A  373  1                                  22
HELIX   16  16 ASN A  384  ILE A  408  1                                  25
HELIX   17  17 ASP A  417  ILE A  433  1                                  17
HELIX   18  18 ALA A  434  SER A  451  1                                  18
HELIX   19  19 PRO A  455  SER A  457  5                                   3
HELIX   20  20 ARG A  458  GLY A  472  1                                  15
HELIX   21  21 ASP A  485  LYS A  489  5                                   5
HELIX   22  22 TYR A  498  GLY A  520  1                                  23
HELIX   23  23 PRO A  524  CYS A  528  5                                   5
HELIX   24  24 SER A  533  GLN A  545  1                                  13
HELIX   25  25 PRO A  551  GLY A  561  1                                  11
HELIX   26  26 ALA A  567  ASN A  588  1                                  22
HELIX   27  27 GLU B   14  ASN B   45  1                                  32
HELIX   28  28 ALA B   48  GLU B   77  1                                  30
HELIX   29  29 GLN B   87  ARG B   96  1                                  10
HELIX   30  30 LEU B   98  LEU B  103  5                                   6
HELIX   31  31 PRO B  104  SER B  123  1                                  20
HELIX   32  32 PRO B  141  SER B  150  1                                  10
HELIX   33  33 SER B  152  ILE B  169  1                                  18
HELIX   34  34 LEU B  171  GLN B  188  1                                  18
HELIX   35  35 ASP B  193  SER B  200  1                                   8
HELIX   36  36 TRP B  201  ASN B  203  5                                   3
HELIX   37  37 THR B  206  GLY B  238  1                                  33
HELIX   38  38 TRP B  261  VAL B  268  5                                   8
HELIX   39  39 MET B  283  GLY B  287  5                                   5
HELIX   40  40 ASN B  289  LEU B  304  1                                  16
HELIX   41  41 PRO B  310  GLY B  316  1                                   7
HELIX   42  42 THR B  352  TYR B  372  1                                  21
HELIX   43  43 PRO B  376  ARG B  380  5                                   5
HELIX   44  44 ASN B  384  THR B  401  1                                  18
HELIX   45  45 THR B  401  ILE B  408  1                                   8
HELIX   46  46 THR B  418  ILE B  433  1                                  16
HELIX   47  47 ALA B  434  SER B  451  1                                  18
HELIX   48  48 PRO B  455  TYR B  459  5                                   5
HELIX   49  49 ASN B  460  TYR B  470  1                                  11
HELIX   50  50 PHE B  484  LYS B  489  5                                   6
HELIX   51  51 TYR B  498  ALA B  519  1                                  22
HELIX   52  52 PRO B  524  CYS B  528  5                                   5
HELIX   53  53 SER B  533  GLN B  545  1                                  13
HELIX   54  54 PRO B  551  VAL B  560  1                                  10
HELIX   55  55 ALA B  567  ASN B  588  1                                  22
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 LYS B 126  CYS B 128  0
SHEET    2  BA 2 CYS B 136  SER B 138 -1  O  TRP B 137   N  VAL B 127
SHEET    1  BB 2 ILE B 248  PRO B 249  0
SHEET    2  BB 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248
SHEET    1  BC 2 SER B 333  ASP B 336  0
SHEET    2  BC 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  2.58
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.03
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  1.81
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.05
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03
LINK         ND2 ASN A  25                 C1  NAG A 693     1555   1555  1.49
LINK         ND2 ASN A  25                 O5  NAG A 693     1555   1555  1.70
LINK         ND2 ASN A 117                 C1  NAG A 695     1555   1555  1.47
LINK         CG  ASN A 480                 C1  NAG A 691     1555   1555  1.97
LINK         ND2 ASN A 480                 C1  NAG A 691     1555   1555  1.45
LINK         O4  NAG A 691                 C1  NAG A 696     1555   1555  1.46
LINK        ZN    ZN A 701                 NE2 HIS A 365     1555   1555  2.17
LINK        ZN    ZN A 701                 O3  LPR A 705     1555   1555  2.53
LINK        ZN    ZN A 701                 OE1 GLU A 389     1555   1555  1.79
LINK        ZN    ZN A 701                 O2  LPR A 705     1555   1555  2.60
LINK        ZN    ZN A 701                 NE2 HIS A 361     1555   1555  2.05
LINK         ND2 ASN B  25                 O   NDG B 693     1555   1555  1.76
LINK         ND2 ASN B  25                 C1  NDG B 693     1555   1555  1.45
LINK         ND2 ASN B 117                 C1  NAG B 695     1555   1555  1.43
LINK         ND2 ASN B 480                 C1  NAG B 691     1555   1555  1.46
LINK         O4  NAG B 691                 C1  NAG B 696     1555   1555  1.41
LINK        ZN    ZN B 701                 NE2 HIS B 365     1555   1555  2.19
LINK        ZN    ZN B 701                 OE1 GLU B 389     1555   1555  1.75
LINK        ZN    ZN B 701                 O2  LPR B 705     1555   1555  2.01
LINK        ZN    ZN B 701                 O3  LPR B 705     1555   1555  2.01
LINK        ZN    ZN B 701                 NE2 HIS B 361     1555   1555  1.96
CISPEP   1 ASP A  140    PRO A  141          0         9.89
CISPEP   2 TYR A  607    PRO A  608          0        10.76
CISPEP   3 ASP B    2    PRO B    3          0       -10.95
CISPEP   4 TYR B  607    PRO B  608          0        10.96
SITE     1 AC1  4 ASN A 480  THR A 482  HIS A 483  NAG A 696
SITE     1 AC2  1 NAG A 691
SITE     1 AC3  2 ASN A  25  GLU A  29
SITE     1 AC4  5 GLN A 110  ALA A 113  LEU A 114  ASN A 117
SITE     2 AC4  5 ARG A 120
SITE     1 AC5  3 ASN B 480  THR B 482  NAG B 696
SITE     1 AC6  1 NAG B 691
SITE     1 AC7  6 GLN B  22  ASN B  25  SER B  26  GLU B  29
SITE     2 AC7  6 ARG B 340  PRO B 376
SITE     1 AC8  3 ALA B 113  ASN B 117  ARG B 120
SITE     1 AC9  4 HIS A 361  HIS A 365  GLU A 389  LPR A 705
SITE     1 BC1  3 TYR A 202  PRO A 497  ARG A 500
SITE     1 BC2  4 HIS B 361  HIS B 365  GLU B 389  LPR B 705
SITE     1 BC3  4 TYR B 202  PRO B 385  PRO B 497  ARG B 500
SITE     1 BC4  3 ARG A 453  ASP A 462  TYR A 465
SITE     1 BC5 13 GLN A 259  HIS A 331  ALA A 332  HIS A 361
SITE     2 BC5 13 GLU A 362  HIS A 365  GLU A 389  LYS A 489
SITE     3 BC5 13 HIS A 491  THR A 496  TYR A 498  TYR A 501
SITE     4 BC5 13  ZN A 701
SITE     1 BC6 13 GLN B 259  HIS B 331  ALA B 332  HIS B 361
SITE     2 BC6 13 GLU B 362  HIS B 365  GLU B 389  LYS B 489
SITE     3 BC6 13 HIS B 491  THR B 496  TYR B 498  TYR B 501
SITE     4 BC6 13  ZN B 701
SITE     1 BC7  5 GLN A 586  LEU B 223  LYS B 469  GLY B 593
SITE     2 BC7  5 TRP B 594
SITE     1 BC8  5 GLU A 219  LEU A 223  LYS A 469  GLY A 593
SITE     2 BC8  5 TRP A 594
CRYST1  101.300  210.900  171.000  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      0.009872  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004742  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005848        0.00000
      
PROCHECK
Go to PROCHECK summary
 References