spacer
spacer

PDBsum entry 2xyd

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2xyd
Jmol
Contents
Protein chain
607 a.a.
Ligands
3ES ×2
NAG-FUC ×2
NAG-NAG ×2
NAG-NAG-BMA-FUC
PEG ×4
PG4 ×2
NAG-NAG-BMA
P6G
Metals
_ZN ×2
_CL ×2
Waters ×241
HEADER    HYDROLASE                               17-NOV-10   2XYD
TITLE     HUMAN ANGIOTENISN CONVERTING ENZYME N-DOMAIN IN COMPLEX
TITLE    2 WITH PHOSPHINIC TRIPEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 30-639;
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143;
COMPND   6 EC: 3.4.15.1;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES;
COMPND   9 OTHER_DETAILS: FINAL CONSTRUCT IS UNDERGLYCOSYALTED MUTANT AND
COMPND  10  CONTAINS TWO MISMATCH MUTATIONS, P576L AND Q545R
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_COMMON: CHINESE HAMSTER;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO K1;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1
KEYWDS    HYDROLASE, ZINC METALLOPEPTIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.AKIF,S.L.SCHWAGER,C.S.ANTHONY,B.CZARNY,F.BEAU,V.DIVE,E.D.STURROCK,
AUTHOR   2 K.R.ACHARYA
REVDAT   2   11-APR-12 2XYD    1       REMARK VERSN
REVDAT   1   11-MAY-11 2XYD    0
JRNL        AUTH   M.AKIF,S.L.SCHWAGER,C.S.ANTHONY,B.CZARNY,F.BEAU,V.DIVE,
JRNL        AUTH 2 E.D.STURROCK,K.R.ACHARYA
JRNL        TITL   NOVEL MECHANISM OF INHIBITION OF HUMAN ANGIOTENSIN-
JRNL        TITL 2 I-CONVERTING ENZYME (ACE) BY A HIGHLY SPECIFIC PHOSPHINIC
JRNL        TITL 3 TRIPEPTIDE.
JRNL        REF    BIOCHEM.J.                    V. 436    53 2011
JRNL        REFN                   ISSN 0264-6021
JRNL        PMID   21352096
JRNL        DOI    10.1042/BJ20102123
REMARK   2
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.28
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.66
REMARK   3   NUMBER OF REFLECTIONS             : 78859
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.22174
REMARK   3   R VALUE            (WORKING SET) : 0.21991
REMARK   3   FREE R VALUE                     : 0.25589
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 4154
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.147
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.202
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5642
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.39
REMARK   3   BIN R VALUE           (WORKING SET) : 0.283
REMARK   3   BIN FREE R VALUE SET COUNT          : 314
REMARK   3   BIN FREE R VALUE                    : 0.287
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 9881
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 368
REMARK   3   SOLVENT ATOMS            : 241
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.57
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.877
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.01
REMARK   3    B22 (A**2) : 0.01
REMARK   3    B33 (A**2) : 0.00
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.01
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.258
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.155
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.912
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10585 ; 0.008 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14426 ; 1.160 ; 1.969
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1220 ; 5.302 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   526 ;35.523 ;23.745
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1584 ;14.970 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;16.084 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1510 ; 0.082 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8247 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6099 ; 0.497 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9807 ; 0.935 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4486 ; 1.285 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4612 ; 2.156 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3   POSITIONS. RESIDUES A130-A132 ARE DISORDERED
REMARK   4
REMARK   4 2XYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-10.
REMARK 100 THE PDBE ID CODE IS EBI-46272.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-OCT-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I04
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763
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 : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84896
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.15
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 2.5
REMARK 200  R MERGE                    (I) : 0.07
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.10
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.19
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5
REMARK 200  R MERGE FOR SHELL          (I) : 0.48
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3NXQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06 M DIVALENT CATIONS, 0.1 M
REMARK 280  TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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: PISA
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: PISA
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 38 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 54 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 111 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 146 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 318 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLN 574 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PRO 605 TO LEU
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 38 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 54 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 111 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 146 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ASN 318 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLN 574 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, PRO 605 TO LEU
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     PRO A   130
REMARK 465     ASN A   131
REMARK 465     LYS A   132
REMARK 465     PRO B   130
REMARK 465     ASN B   131
REMARK 465     LYS B   132
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A  56    CD   OE1  OE2
REMARK 470     GLN A  70    CD   OE1  NE2
REMARK 470     LEU A 129    CG   CD1  CD2
REMARK 470     THR A 133    OG1  CG2
REMARK 470     THR A 135    OG1  CG2
REMARK 470     LYS A 341    CD   CE   NZ
REMARK 470     GLU A 403    CD   OE1  OE2
REMARK 470     LYS A 517    CE   NZ
REMARK 470     LYS A 542    CE   NZ
REMARK 470     GLU B  56    CD   OE1  OE2
REMARK 470     GLN B  70    CD   OE1  NE2
REMARK 470     LYS B 341    CD   CE   NZ
REMARK 470     GLU B 403    CD   OE1  OE2
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR B 415    OG1  CG2
REMARK 470     LYS B 517    CE   NZ
REMARK 470     LYS B 542    CE   NZ
REMARK 470     TYR B 607    CG   CD1  CD2  CE1  CE2  CZ   OH
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    ALA A  12       48.81    -91.98
REMARK 500    ASN A  45       78.03   -171.01
REMARK 500    ASN A 203       67.59     27.88
REMARK 500    ALA A 258       25.54     49.14
REMARK 500    ARG A 340       16.04     59.73
REMARK 500    ASP B   2      160.21    -49.45
REMARK 500    ASN B 203       45.46     36.60
REMARK 500    LYS B 341      -51.21   -129.97
REMARK 500    ASN B 416       88.77    -69.45
REMARK 500    ASP B 417      -97.42   -129.05
REMARK 500    THR B 418      -42.41   -151.10
REMARK 500    GLN B 575      -51.44    -23.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     PG4 A 1625
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 A1620  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 365   NE2
REMARK 620 2 3ES A1611   OAG  83.6
REMARK 620 3 3ES A1611   OAD 137.4  67.9
REMARK 620 4 HIS A 361   NE2  97.5  93.4 114.5
REMARK 620 5 GLU A 389   OE1 104.8 165.3  98.4  97.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B1619  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 361   NE2
REMARK 620 2 HIS B 365   NE2  98.2
REMARK 620 3 GLU B 389   OE1  89.6 107.5
REMARK 620 4 3ES B1611   OAG 100.2  85.2 162.7
REMARK 620 5 3ES B1611   OAD 112.3 142.5  94.4  68.8
REMARK 620 N                    1     2     3     4
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: [(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-
REMARK 630  {[(BENZYLOXY)[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-CARBONYL]
REMARK 630  -AMINO}ETHYL)PHOSPHINYL]-2-[(3-PHENYLISOXAZOL-5-YL)METHYL]-1
REMARK 630  -OXO-PROPYL}AMINO)-3-(4-HYDROXY-PHENYL)
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     3ES A  1611
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: PHQ PPH 1JQ TYR
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 3ES A1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3ES B1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1622
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1623
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800  SUGAR BOUND TO ASN A  45 RESIDUES 1614 TO 1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800  SUGAR BOUND TO ASN A 416 RESIDUES 1616 TO 1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF
REMARK 800  SUGAR BOUND TO ASN A 480 RESIDUES 1612 TO 1613
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF
REMARK 800  SUGAR BOUND TO ASN B  45 RESIDUES 1614 TO 1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF
REMARK 800  SUGAR BOUND TO ASN B 416 RESIDUES 1616 TO 1618
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF
REMARK 800  SUGAR BOUND TO ASN B 480 RESIDUES 1612 TO 1613
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IUL   RELATED DB: PDB
REMARK 900  HUMAN TACE G13 MUTANT
REMARK 900 RELATED ID: 2IUX   RELATED DB: PDB
REMARK 900  HUMAN TACE MUTANT G1234
REMARK 900 RELATED ID: 2C6N   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I
REMARK 900  CONVERTING ENZYME N DOMAIN WITH LISINOPRIL
REMARK 900 RELATED ID: 1UZE   RELATED DB: PDB
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG
REMARK 900  ENALAPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN
REMARK 900   I-CONVERTING ENZYME
REMARK 900 RELATED ID: 1O86   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN
REMARK 900  CONVERING ENZYME IN COMPLEX WITH LISINOPRIL.
REMARK 900 RELATED ID: 1UZF   RELATED DB: PDB
REMARK 900  COMPLEX OF THE ANTI-HYPERTENSIVE DRUG
REMARK 900  CAPTOPRIL AN THE HUMAN TESTICULAR ANGIOTENSIN
REMARK 900   I-CONVERTING ENZYME
REMARK 900 RELATED ID: 2C6F   RELATED DB: PDB
REMARK 900  STRUCTURE OF HUMAN SOMATIC ANGIONTENSIN-I
REMARK 900  CONVERTING ENZYME N DOMAIN
REMARK 900 RELATED ID: 1O8A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN
REMARK 900  CONVERING ENZYME (NATIVE).
REMARK 900 RELATED ID: 2XY9   RELATED DB: PDB
REMARK 900  HUMAN ANGIOTENSIN CONVERTING ENZYME IN COMPLEX
REMARK 900   WITH PHOSPHINIC TRIPEPTIDE
DBREF  2XYD A    1   610  UNP    P12821   ACE_HUMAN       30    639
DBREF  2XYD B    1   610  UNP    P12821   ACE_HUMAN       30    639
SEQADV 2XYD GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION
SEQADV 2XYD GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION
SEQADV 2XYD GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION
SEQADV 2XYD GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION
SEQADV 2XYD GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION
SEQADV 2XYD ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION
SEQADV 2XYD LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION
SEQADV 2XYD GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION
SEQADV 2XYD GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION
SEQADV 2XYD GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION
SEQADV 2XYD GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION
SEQADV 2XYD GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION
SEQADV 2XYD ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION
SEQADV 2XYD LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION
SEQRES   1 A  610  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES   2 A  610  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES   3 A  610  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES   4 A  610  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES   5 A  610  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES   6 A  610  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES   7 A  610  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES   8 A  610  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES   9 A  610  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES  10 A  610  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES  11 A  610  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES  12 A  610  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES  13 A  610  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES  14 A  610  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES  15 A  610  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES  16 A  610  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES  17 A  610  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES  18 A  610  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES  19 A  610  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES  20 A  610  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES  21 A  610  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES  22 A  610  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES  23 A  610  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES  24 A  610  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES  25 A  610  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES  26 A  610  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES  27 A  610  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES  28 A  610  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES  29 A  610  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES  30 A  610  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES  31 A  610  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES  32 A  610  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES  33 A  610  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES  34 A  610  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES  35 A  610  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES  36 A  610  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES  37 A  610  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES  38 A  610  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES  39 A  610  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES  40 A  610  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES  41 A  610  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES  42 A  610  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES  43 A  610  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES  44 A  610  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES  45 A  610  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES  46 A  610  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES  47 A  610  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY
SEQRES   1 B  610  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP
SEQRES   2 B  610  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER
SEQRES   3 B  610  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER
SEQRES   4 B  610  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG
SEQRES   5 B  610  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA
SEQRES   6 B  610  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO
SEQRES   7 B  610  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE
SEQRES   8 B  610  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO
SEQRES   9 B  610  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN
SEQRES  10 B  610  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO
SEQRES  11 B  610  ASN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU
SEQRES  12 B  610  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU
SEQRES  13 B  610  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE
SEQRES  14 B  610  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER
SEQRES  15 B  610  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY
SEQRES  16 B  610  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU
SEQRES  17 B  610  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU
SEQRES  18 B  610  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS
SEQRES  19 B  610  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO
SEQRES  20 B  610  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER
SEQRES  21 B  610  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP
SEQRES  22 B  610  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN
SEQRES  23 B  610  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU
SEQRES  24 B  610  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU
SEQRES  25 B  610  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY
SEQRES  26 B  610  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR
SEQRES  27 B  610  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL
SEQRES  28 B  610  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY
SEQRES  29 B  610  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL
SEQRES  30 B  610  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA
SEQRES  31 B  610  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU
SEQRES  32 B  610  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN
SEQRES  33 B  610  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA
SEQRES  34 B  610  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL
SEQRES  35 B  610  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO
SEQRES  36 B  610  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR
SEQRES  37 B  610  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU
SEQRES  38 B  610  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN
SEQRES  39 B  610  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU
SEQRES  40 B  610  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY
SEQRES  41 B  610  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER
SEQRES  42 B  610  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA
SEQRES  43 B  610  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET
SEQRES  44 B  610  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS
SEQRES  45 B  610  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN
SEQRES  46 B  610  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN
SEQRES  47 B  610  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY
HET    3ES  A1611      51
HET    NAG  A1612      14
HET    FUC  A1613      10
HET    NAG  A1614      14
HET    NAG  A1615      14
HET    NAG  A1616      14
HET    NAG  A1617      14
HET    BMA  A1618      11
HET    FUC  A1619      10
HET     ZN  A1620       1
HET     CL  A1621       1
HET    PEG  A1622       7
HET    PEG  A1623       7
HET    PEG  A1624       7
HET    PG4  A1625      10
HET    3ES  B1611      51
HET    NAG  B1612      14
HET    FUC  B1613      10
HET    NAG  B1614      14
HET    NAG  B1615      14
HET    NAG  B1616      14
HET    NAG  B1617      14
HET    BMA  B1618      11
HET     ZN  B1619       1
HET     CL  B1620       1
HET    PG4  B1621      13
HET    P6G  B1622      19
HET    PEG  B1623       7
HETNAM     3ES [(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-
HETNAM   2 3ES  {[(BENZYLOXY)[(2S)-2-({3-[HYDROXYL(2-PHENYL-(1R)-1-
HETNAM   3 3ES  CARBONYL]-AMINO}ETHYL)PHOSPHINYL]-2-[(3-
HETNAM   4 3ES  PHENYLISOXAZOL-5-YL)METHYL]-1-OXO-PROPYL}AMINO)-3-
HETNAM   5 3ES  (4-HYDROXY-PHENYL)
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETNAM     PG4 TETRAETHYLENE GLYCOL
HETNAM     P6G HEXAETHYLENE GLYCOL
HETSYN     P6G POLYETHYLENE GLYCOL PEG400
FORMUL   3  3ES    2(C38 H38 N3 O9 P)
FORMUL   4  NAG    10(C8 H15 N O6)
FORMUL   5  FUC    3(C6 H12 O5)
FORMUL   6  BMA    2(C6 H12 O6)
FORMUL   7   ZN    2(ZN 2+)
FORMUL   8   CL    2(CL 1-)
FORMUL   9  PEG    4(C4 H10 O3)
FORMUL  10  PG4    2(C8 H18 O5)
FORMUL  11  P6G    C12 H26 O7
FORMUL  12  HOH   *241(H2 O)
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 ILE A   79  PHE A   83  5                                   5
HELIX    5   5 ASP A   85  ARG A   96  1                                  12
HELIX    6   6 LEU A   98  LEU A  103  5                                   6
HELIX    7   7 PRO A  104  ALA A  125  1                                  22
HELIX    8   8 PRO A  141  SER A  150  1                                  10
HELIX    9   9 SER A  152  GLN A  188  1                                  37
HELIX   10  10 ASP A  193  TRP A  201  1                                   9
HELIX   11  11 THR A  206  ILE A  242  1                                  37
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 GLN 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  SER A  400  1                                  17
HELIX   20  20 THR A  401  ILE A  408  1                                   8
HELIX   21  21 ASP A  417  ILE A  433  1                                  17
HELIX   22  22 PHE A  435  SER A  451  1                                  17
HELIX   23  23 PRO A  455  SER A  457  5                                   3
HELIX   24  24 ARG A  458  GLY A  472  1                                  15
HELIX   25  25 PHE A  484  LYS A  489  5                                   6
HELIX   26  26 TYR A  498  ALA A  519  1                                  22
HELIX   27  27 PRO A  524  CYS A  528  5                                   5
HELIX   28  28 SER A  533  GLY A  547  1                                  15
HELIX   29  29 PRO A  551  GLY A  561  1                                  11
HELIX   30  30 ALA A  567  ASN A  588  1                                  22
HELIX   31  31 ASP B   13  ASN B   45  1                                  33
HELIX   32  32 THR B   47  GLU B   77  1                                  31
HELIX   33  33 PRO B   78  PHE B   83  5                                   6
HELIX   34  34 ASP B   85  ARG B   96  1                                  12
HELIX   35  35 LEU B   98  LEU B  103  5                                   6
HELIX   36  36 PRO B  104  ALA B  125  1                                  22
HELIX   37  37 PRO B  141  SER B  150  1                                  10
HELIX   38  38 SER B  152  GLN B  188  1                                  37
HELIX   39  39 ASP B  193  TRP B  201  1                                   9
HELIX   40  40 THR B  206  GLY B  238  1                                  33
HELIX   41  41 TRP B  261  ASN B  263  5                                   3
HELIX   42  42 ILE B  264  VAL B  269  1                                   6
HELIX   43  43 VAL B  279  GLY B  287  1                                   9
HELIX   44  44 GLN 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  ILE B  408  1                                  25
HELIX   49  49 THR B  418  ILE B  433  1                                  16
HELIX   50  50 PHE B  435  GLY B  452  1                                  18
HELIX   51  51 PRO B  455  SER B  457  5                                   3
HELIX   52  52 ARG B  458  GLY B  472  1                                  15
HELIX   53  53 PHE B  484  LYS B  489  5                                   6
HELIX   54  54 TYR B  498  ALA B  519  1                                  22
HELIX   55  55 PRO B  524  CYS B  528  5                                   5
HELIX   56  56 SER B  533  GLY B  547  1                                  15
HELIX   57  57 PRO B  551  GLY B  561  1                                  11
HELIX   58  58 ALA B  567  ASN B  588  1                                  22
SHEET    1  AA 2 LYS A 126  CYS A 128  0
SHEET    2  AA 2 CYS A 136  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 VAL B 127  CYS B 128  0
SHEET    2  BA 2 CYS B 136  TRP B 137 -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  2.04
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.06
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.02
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.05
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.05
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.02
LINK         ND2 ASN A  45                 C1  NAG A1614     1555   1555  1.44
LINK         ND2 ASN A 416                 C1  NAG A1616     1555   1555  1.44
LINK         ND2 ASN A 480                 C1  NAG A1612     1555   1555  1.44
LINK         OAG 3ES A1611                ZN    ZN A1620     1555   1555  2.34
LINK         OAD 3ES A1611                ZN    ZN A1620     1555   1555  2.23
LINK         O6  NAG A1612                 C1  FUC A1613     1555   1555  1.44
LINK         O4  NAG A1614                 C1  NAG A1615     1555   1555  1.45
LINK         O4  NAG A1616                 C1  NAG A1617     1555   1555  1.44
LINK         O6  NAG A1616                 C1  FUC A1619     1555   1555  1.44
LINK         O4  NAG A1617                 C1  BMA A1618     1555   1555  1.44
LINK        ZN    ZN A1620                 NE2 HIS A 361     1555   1555  2.04
LINK        ZN    ZN A1620                 NE2 HIS A 365     1555   1555  1.99
LINK        ZN    ZN A1620                 OE1 GLU A 389     1555   1555  1.92
LINK         ND2 ASN B  45                 C1  NAG B1614     1555   1555  1.43
LINK         ND2 ASN B 416                 C1  NAG B1616     1555   1555  1.45
LINK         ND2 ASN B 480                 C1  NAG B1612     1555   1555  1.45
LINK         OAD 3ES B1611                ZN    ZN B1619     1555   1555  2.05
LINK         PBY 3ES B1611                ZN    ZN B1619     1555   1555  2.70
LINK         OAG 3ES B1611                ZN    ZN B1619     1555   1555  2.39
LINK         O6  NAG B1612                 C1  FUC B1613     1555   1555  1.44
LINK         O4  NAG B1614                 C1  NAG B1615     1555   1555  1.45
LINK         O4  NAG B1616                 C1  NAG B1617     1555   1555  1.45
LINK         O4  NAG B1617                 C1  BMA B1618     1555   1555  1.45
LINK        ZN    ZN B1619                 NE2 HIS B 365     1555   1555  2.01
LINK        ZN    ZN B1619                 OE1 GLU B 389     1555   1555  2.08
LINK        ZN    ZN B1619                 NE2 HIS B 361     1555   1555  1.95
CISPEP   1 ASP A  140    PRO A  141          0         8.83
CISPEP   2 TYR A  607    PRO A  608          0        -0.93
CISPEP   3 ASP B  140    PRO B  141          0         6.25
CISPEP   4 TYR B  607    PRO B  608          0         3.46
SITE     1 AC1 22 GLN A 259  HIS A 331  ALA A 332  SER A 333
SITE     2 AC1 22 ALA A 334  THR A 358  HIS A 361  GLU A 362
SITE     3 AC1 22 HIS A 365  TYR A 369  HIS A 388  GLU A 389
SITE     4 AC1 22 ASP A 393  LYS A 489  PHE A 490  HIS A 491
SITE     5 AC1 22 THR A 496  TYR A 498  TYR A 501  PHE A 505
SITE     6 AC1 22  ZN A1620  PEG A1622
SITE     1 AC2  4 HIS A 361  HIS A 365  GLU A 389  3ES A1611
SITE     1 AC3  4 TYR A 202  PRO A 497  ARG A 500  HOH A2040
SITE     1 AC4  2 ALA A 334  3ES A1611
SITE     1 AC5  2 ARG A  96  GLY A 190
SITE     1 AC6  6 ARG A 453  TYR A 465  ARG B 453  ASP B 462
SITE     2 AC6  6 TYR B 465  HOH B2077
SITE     1 AC7 25 GLN B 259  HIS B 331  ALA B 332  SER B 333
SITE     2 AC7 25 ALA B 334  THR B 358  HIS B 361  GLU B 362
SITE     3 AC7 25 HIS B 365  TYR B 369  HIS B 388  GLU B 389
SITE     4 AC7 25 ASP B 393  LYS B 489  PHE B 490  HIS B 491
SITE     5 AC7 25 THR B 496  TYR B 498  TYR B 501  PHE B 505
SITE     6 AC7 25  ZN B1619  PEG B1623  HOH B2066  HOH B2104
SITE     7 AC7 25 HOH B2105
SITE     1 AC8  4 HIS B 361  HIS B 365  GLU B 389  3ES B1611
SITE     1 AC9  4 TYR B 202  PRO B 497  ARG B 500  HOH B2027
SITE     1 BC1  7 GLN A 286  GLY A 287  HIS A 292  GLN B 286
SITE     2 BC1  7 GLY B 287  HIS B 292  P6G B1622
SITE     1 BC2  5 ARG A 295  ILE A 408  ARG B 295  VAL B 296
SITE     2 BC2  5 PG4 B1621
SITE     1 BC3  2 TRP B 335  3ES B1611
SITE     1 BC4  4 ASN A  45  THR A  47  GLU A  49  ASN A  50
SITE     1 BC5  4 PHE A  10  ASN A 416  PRO A 524  GLN A 527
SITE     1 BC6  5 ASN A 480  THR A 482  TYR A 607  ARG B 245
SITE     2 BC6  5 GLU B 596
SITE     1 BC7  5 ASN B  45  THR B  47  GLU B  49  ASN B  50
SITE     2 BC7  5 ARG B  53
SITE     1 BC8  4 ASN B 416  GLU B 522  PRO B 524  GLN B 527
SITE     1 BC9  6 ARG A 245  GLU A 596  GLU B 161  THR B 478
SITE     2 BC9  6 ASN B 480  THR B 482
CRYST1   72.837   76.437   82.954  89.11  64.43  75.87 P 1           2
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      0.013729 -0.003456 -0.006961        0.00000
SCALE2      0.000000  0.013491  0.001393        0.00000
SCALE3      0.000000  0.000000  0.013435        0.00000
      
PROCHECK
Go to PROCHECK summary
 References