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PDBsum entry 2iul

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Hydrolase PDB id
2iul
Jmol
Contents
Protein chain
583 a.a.
Ligands
NAG
NAG-NAG
ACT ×2
FUC
BMA-BMA
Metals
_ZN
_CL ×2
Waters ×335
HEADER    HYDROLASE                               06-JUN-06   2IUL
TITLE     HUMAN TACE G13 MUTANT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES 68-658;
COMPND   5 SYNONYM: HUMAN TESTIS ACE G13 MUTANT, TESTIS-SPECIFIC
COMPND   6  ISOFORM, ACE-T, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE
COMPND   7  II;
COMPND   8 EC: 3.4.15.1, 3.2.1.-;
COMPND   9 ENGINEERED: YES;
COMPND  10 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY CELLS
KEYWDS    HYDROLASE, PHOSPHORYLATION, CARBOXYPEPTIDASE,
KEYWDS   2 METAL-BINDING, TRANSMEMBRANE, METALLOPROTEASE, PEPTIDYL
KEYWDS   3 DIPEPTIDASE, ALTERNATIVE SPLICING, TYPE-I
KEYWDS   4 MEMBRANE-ANCHORED PROTEIN, GLYCOSIDASE, POLYMORPHISM,
KEYWDS   5 GLYCOPROTEIN, AC, ZINC, MUTANT, MEMBRANE, CHLORIDE,
KEYWDS   6 PROTEASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.M.WATERMEYER,B.T.SEWELL,R.NATESH,H.R.CORRADI,K.R.ACHARYA,
AUTHOR   2 E.D.STURROCK
REVDAT   2   24-FEB-09 2IUL    1       VERSN
REVDAT   1   25-OCT-06 2IUL    0
JRNL        AUTH   J.M.WATERMEYER,B.T.SEWELL,S.L.SCHWAGER,R.NATESH,
JRNL        AUTH 2 H.R.CORRADI,K.R.ACHARYA,E.D.STURROCK
JRNL        TITL   STRUCTURE OF TESTIS ACE GLYCOSYLATION MUTANTS AND
JRNL        TITL 2 EVIDENCE FOR CONSERVED DOMAIN MOVEMENT.
JRNL        REF    BIOCHEMISTRY                  V.  45 12654 2006
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   17042482
JRNL        DOI    10.1021/BI061146Z
REMARK   2
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 2.01
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 71.61
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3
REMARK   3   NUMBER OF REFLECTIONS             : 40225
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) : 0.182
REMARK   3   R VALUE            (WORKING SET) : 0.180
REMARK   3   FREE R VALUE                     : 0.220
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1297
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) : 2.02
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2172
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210
REMARK   3   BIN FREE R VALUE SET COUNT          : 80
REMARK   3   BIN FREE R VALUE                    : 0.3100
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4779
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 85
REMARK   3   SOLVENT ATOMS            : 335
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.59
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.10000
REMARK   3    B22 (A**2) : -0.26000
REMARK   3    B33 (A**2) : 0.16000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.192
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.163
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.374
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4972 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6780 ; 1.198 ; 1.954
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   589 ; 5.178 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   243 ;35.326 ;24.115
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   790 ;14.138 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;20.780 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   727 ; 0.079 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3823 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2389 ; 0.189 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3411 ; 0.302 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   316 ; 0.125 ; 0.200
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):    56 ; 0.201 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.114 ; 0.200
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):  3024 ; 0.603 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4722 ; 0.972 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2286 ; 1.465 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2054 ; 2.249 ; 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   : 1.20
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
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2IUL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  06-JUN-06.
REMARK 100 THE PDBE ID CODE IS EBI-29010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 4.70
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX14.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40225
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
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     (%) : 96.2
REMARK 200  DATA REDUNDANCY                : 12.400
REMARK 200  R MERGE                    (I) : 0.06000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 6.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1O8A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 44.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH4.7 15%,
REMARK 280  PEG 4000, 10UM ZINC SULPHATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       28.31650
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.23300
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.36150
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.23300
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.31650
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.36150
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE:  1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400  CONVERTS ANGIOTENSIN I TO ANGIOTENSIN II BY RELEASE OF
REMARK 400  THE TERMINAL HIS-LEU, THIS RESULTS IN AN INCREASE OF THE
REMARK 400  VASOCONSTRICTOR ACTIVITY OF ANGIOTENSIN. ALSO ABLE TO INACTIVATE
REMARK 400  BRADYKININ, A POTENT VASODILATOR. HAS ALSO A GLYCOSIDASE ACTIVITY
REMARK 400  WHICH RELEASES GPI-ANCHORED PROTEINS FROM THE MEMBRANE BY CLEAVING
REMARK 400  THE MANNOSE LINKAGE IN THE GPI MOIETY (BY SIMILARITY).
REMARK 400
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 121 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 186 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 368 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 617 TO GLN
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 A    37
REMARK 465     VAL A    38
REMARK 465     THR A    39
REMARK 465     GLU A   436
REMARK 465     ASN A   624
REMARK 465     SER A   625
REMARK 465     ALA A   626
REMARK 465     ARG A   627
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  64    CG   CD   OE1  OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480   M RES CSSEQI  ATOMS
REMARK 480     LYS A  79    CG   CD   CE   NZ
REMARK 480     GLN A  98    CG   CD  OE1  NE2
REMARK 480     GLN A 106    CG   CD  OE1  NE2
REMARK 480     GLN A 108    CB   CG   CD  OE1  NE2
REMARK 480     LYS A 113    CE   NZ
REMARK 480     LYS A 117    CD   CE   NZ
REMARK 480     SER A 298    OG
REMARK 480     GLU A 303    CG   CD  OE1  OE2
REMARK 480     LYS A 307    CG   CD   CE   NZ
REMARK 480     LYS A 363    CE   NZ
REMARK 480     LYS A 425    CE   NZ
REMARK 480     LYS A 613    CE   NZ
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    LYS A 113   CD    LYS A 113   CE     -0.263
REMARK 500    LYS A 117   CG    LYS A 117   CD      0.229
REMARK 500    SER A 298   CB    SER A 298   OG      0.170
REMARK 500    LYS A 425   CD    LYS A 425   CE      0.253
REMARK 500    LYS A 613   CD    LYS A 613   CE     -0.187
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    LYS A 113   CD  -  CE  -  NZ  ANGL. DEV. =  39.5 DEGREES
REMARK 500    LYS A 113   CG  -  CD  -  CE  ANGL. DEV. =  28.2 DEGREES
REMARK 500    LYS A 613   CG  -  CD  -  CE  ANGL. DEV. = -24.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  72       74.51   -166.61
REMARK 500    GLU A 123     -129.59     50.28
REMARK 500    ASP A 300       98.32    -66.58
REMARK 500    LYS A 363      -39.04   -134.05
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 CYS A  152     HIS A  153                  145.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1634  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACT A1627   OXT
REMARK 620 2 HIS A 383   NE2  99.5
REMARK 620 3 GLU A 411   OE1 152.5  91.0
REMARK 620 4 ACT A1627   O    54.5 117.5  98.2
REMARK 620 5 HIS A 387   NE2  94.8 107.8 106.1 127.6
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1632
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A1633
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1629
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1630
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1634
REMARK 900
REMARK 900 RELATED ENTRIES
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: 1O8A   RELATED DB: PDB
REMARK 900  CRYSTAL STRUCTURE OF HUMAN ANGIOTENSIN
REMARK 900  CONVERING ENZYME (NATIVE).
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: 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: 2IUX   RELATED DB: PDB
REMARK 900  HUMAN TACE MUTANT G1234
DBREF  2IUL A   37   627  UNP    P22966   ACET_HUMAN      68    658
SEQADV 2IUL GLN A   90  UNP  P22966    ASN   121 ENGINEERED MUTATION
SEQADV 2IUL GLN A  155  UNP  P22966    ASN   186 ENGINEERED MUTATION
SEQADV 2IUL GLN A  337  UNP  P22966    ASN   368 ENGINEERED MUTATION
SEQADV 2IUL GLN A  586  UNP  P22966    ASN   617 ENGINEERED MUTATION
SEQRES   1 A  591  LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL GLU
SEQRES   2 A  591  GLU TYR ASP ARG THR SER GLN VAL VAL TRP ASN GLU TYR
SEQRES   3 A  591  ALA GLU ALA ASN TRP ASN TYR ASN THR ASN ILE THR THR
SEQRES   4 A  591  GLU THR SER LYS ILE LEU LEU GLN LYS ASN MET GLN ILE
SEQRES   5 A  591  ALA GLN HIS THR LEU LYS TYR GLY THR GLN ALA ARG LYS
SEQRES   6 A  591  PHE ASP VAL ASN GLN LEU GLN ASN THR THR ILE LYS ARG
SEQRES   7 A  591  ILE ILE LYS LYS VAL GLN ASP LEU GLU ARG ALA ALA LEU
SEQRES   8 A  591  PRO ALA GLN GLU LEU GLU GLU TYR ASN LYS ILE LEU LEU
SEQRES   9 A  591  ASP MET GLU THR THR TYR SER VAL ALA THR VAL CYS HIS
SEQRES  10 A  591  PRO GLN GLY SER CYS LEU GLN LEU GLU PRO ASP LEU THR
SEQRES  11 A  591  ASN VAL MET ALA THR SER ARG LYS TYR GLU ASP LEU LEU
SEQRES  12 A  591  TRP ALA TRP GLU GLY TRP ARG ASP LYS ALA GLY ARG ALA
SEQRES  13 A  591  ILE LEU GLN PHE TYR PRO LYS TYR VAL GLU LEU ILE ASN
SEQRES  14 A  591  GLN ALA ALA ARG LEU ASN GLY TYR VAL ASP ALA GLY ASP
SEQRES  15 A  591  SER TRP ARG SER MET TYR GLU THR PRO SER LEU GLU GLN
SEQRES  16 A  591  ASP LEU GLU ARG LEU PHE GLN GLU LEU GLN PRO LEU TYR
SEQRES  17 A  591  LEU ASN LEU HIS ALA TYR VAL ARG ARG ALA LEU HIS ARG
SEQRES  18 A  591  HIS TYR GLY ALA GLN HIS ILE ASN LEU GLU GLY PRO ILE
SEQRES  19 A  591  PRO ALA HIS LEU LEU GLY ASN MET TRP ALA GLN THR TRP
SEQRES  20 A  591  SER ASN ILE TYR ASP LEU VAL VAL PRO PHE PRO SER ALA
SEQRES  21 A  591  PRO SER MET ASP THR THR GLU ALA MET LEU LYS GLN GLY
SEQRES  22 A  591  TRP THR PRO ARG ARG MET PHE LYS GLU ALA ASP ASP PHE
SEQRES  23 A  591  PHE THR SER LEU GLY LEU LEU PRO VAL PRO PRO GLU PHE
SEQRES  24 A  591  TRP GLN LYS SER MET LEU GLU LYS PRO THR ASP GLY ARG
SEQRES  25 A  591  GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR ASN
SEQRES  26 A  591  GLY LYS ASP PHE ARG ILE LYS GLN CYS THR THR VAL ASN
SEQRES  27 A  591  LEU GLU ASP LEU VAL VAL ALA HIS HIS GLU MET GLY HIS
SEQRES  28 A  591  ILE GLN TYR PHE MET GLN TYR LYS ASP LEU PRO VAL ALA
SEQRES  29 A  591  LEU ARG GLU GLY ALA ASN PRO GLY PHE HIS GLU ALA ILE
SEQRES  30 A  591  GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO LYS HIS
SEQRES  31 A  591  LEU HIS SER LEU ASN LEU LEU SER SER GLU GLY GLY SER
SEQRES  32 A  591  ASP GLU HIS ASP ILE ASN PHE LEU MET LYS MET ALA LEU
SEQRES  33 A  591  ASP LYS ILE ALA PHE ILE PRO PHE SER TYR LEU VAL ASP
SEQRES  34 A  591  GLN TRP ARG TRP ARG VAL PHE ASP GLY SER ILE THR LYS
SEQRES  35 A  591  GLU ASN TYR ASN GLN GLU TRP TRP SER LEU ARG LEU LYS
SEQRES  36 A  591  TYR GLN GLY LEU CYS PRO PRO VAL PRO ARG THR GLN GLY
SEQRES  37 A  591  ASP PHE ASP PRO GLY ALA LYS PHE HIS ILE PRO SER SER
SEQRES  38 A  591  VAL PRO TYR ILE ARG TYR PHE VAL SER PHE ILE ILE GLN
SEQRES  39 A  591  PHE GLN PHE HIS GLU ALA LEU CYS GLN ALA ALA GLY HIS
SEQRES  40 A  591  THR GLY PRO LEU HIS LYS CYS ASP ILE TYR GLN SER LYS
SEQRES  41 A  591  GLU ALA GLY GLN ARG LEU ALA THR ALA MET LYS LEU GLY
SEQRES  42 A  591  PHE SER ARG PRO TRP PRO GLU ALA MET GLN LEU ILE THR
SEQRES  43 A  591  GLY GLN PRO GLN MET SER ALA SER ALA MET LEU SER TYR
SEQRES  44 A  591  PHE LYS PRO LEU LEU ASP TRP LEU ARG THR GLU ASN GLU
SEQRES  45 A  591  LEU HIS GLY GLU LYS LEU GLY TRP PRO GLN TYR ASN TRP
SEQRES  46 A  591  THR PRO ASN SER ALA ARG
HET    NAG  A1624      14
HET    NAG  A1625      14
HET    NAG  A1626      14
HET    FUC  A1631      10
HET    BMA  A1632      11
HET    BMA  A1633      11
HET    ACT  A1627       4
HET    ACT  A1628       4
HET     CL  A1629       1
HET     CL  A1630       1
HET     ZN  A1634       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     FUC ALPHA-L-FUCOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     ACT ACETATE ION
HETNAM      CL CHLORIDE ION
HETNAM      ZN ZINC ION
HETSYN     NAG NAG
FORMUL   2  NAG    3(C8 H15 N O6)
FORMUL   3  FUC    C6 H12 O5
FORMUL   3  BMA    2(C6 H12 O6)
FORMUL   4  ACT    2(C2 H3 O2 1-)
FORMUL   6   CL    2(CL 1-)
FORMUL   8   ZN    ZN 2+
FORMUL   9  HOH   *335(H2 O1)
HELIX    1   1 ASP A   40  THR A   71  1                                  32
HELIX    2   2 THR A   74  ARG A  100  1                                  27
HELIX    3   3 ASP A  103  LEU A  107  5                                   5
HELIX    4   4 ASN A  109  GLN A  120  1                                  12
HELIX    5   5 LEU A  122  LEU A  127  5                                   6
HELIX    6   6 PRO A  128  ALA A  149  1                                  22
HELIX    7   7 PRO A  163  SER A  172  1                                  10
HELIX    8   8 LYS A  174  ALA A  189  1                                  16
HELIX    9   9 ALA A  189  GLN A  195  1                                   7
HELIX   10  10 PHE A  196  ASN A  211  1                                  16
HELIX   11  11 ASP A  215  SER A  222  1                                   8
HELIX   12  12 MET A  223  GLU A  225  5                                   3
HELIX   13  13 SER A  228  LEU A  240  1                                  13
HELIX   14  14 LEU A  240  GLY A  260  1                                  21
HELIX   15  15 TRP A  283  ASN A  285  5                                   3
HELIX   16  16 ILE A  286  VAL A  291  1                                   6
HELIX   17  17 ASP A  300  GLN A  308  1                                   9
HELIX   18  18 THR A  311  LEU A  326  1                                  16
HELIX   19  19 PRO A  332  SER A  339  1                                   8
HELIX   20  20 ASN A  374  TYR A  394  1                                  21
HELIX   21  21 PRO A  398  ARG A  402  5                                   5
HELIX   22  22 ASN A  406  SER A  422  1                                  17
HELIX   23  23 THR A  423  LEU A  430  1                                   8
HELIX   24  24 SER A  439  ASP A  473  1                                  35
HELIX   25  25 ASN A  480  GLY A  494  1                                  15
HELIX   26  26 PHE A  506  LYS A  511  5                                   6
HELIX   27  27 TYR A  520  ALA A  541  1                                  22
HELIX   28  28 PRO A  546  CYS A  550  5                                   5
HELIX   29  29 SER A  555  LEU A  568  1                                  14
HELIX   30  30 PRO A  573  GLY A  583  1                                  11
HELIX   31  31 ALA A  589  HIS A  610  1                                  22
SHEET    1  AA 2 THR A 150  CYS A 152  0
SHEET    2  AA 2 CYS A 158  GLN A 160 -1  O  LEU A 159   N  VAL A 151
SHEET    1  AB 2 ILE A 270  PRO A 271  0
SHEET    2  AB 2 LEU A 495  CYS A 496  1  N  CYS A 496   O  ILE A 270
SHEET    1  AC 2 SER A 355  ASP A 358  0
SHEET    2  AC 2 PHE A 365  LYS A 368 -1  O  ARG A 366   N  TRP A 357
SSBOND   1 CYS A  152    CYS A  158                          1555   1555  2.05
SSBOND   2 CYS A  352    CYS A  370                          1555   1555  2.04
SSBOND   3 CYS A  538    CYS A  550                          1555   1555  2.03
LINK         ND2 ASN A  72                 C1  NAG A1624     1555   1555  1.48
LINK         ND2 ASN A 109                 C1  NAG A1625     1555   1555  1.44
LINK         O4  NAG A1625                 C1  NAG A1626     1555   1555  1.44
LINK         O6  NAG A1625                 C1  FUC A1631     1555   1555  1.33
LINK         O4  NAG A1626                 C1  BMA A1632     1555   1555  1.44
LINK         O   ACT A1627                ZN    ZN A1634     1555   1555  2.04
LINK         O3  BMA A1632                 C1  BMA A1633     1555   1555  1.45
LINK        ZN    ZN A1634                 NE2 HIS A 383     1555   1555  2.05
LINK        ZN    ZN A1634                 OE1 GLU A 411     1555   1555  1.99
LINK        ZN    ZN A1634                 NE2 HIS A 387     1555   1555  2.05
LINK        ZN    ZN A1634                 OXT ACT A1627     1555   1555  2.48
CISPEP   1 GLU A  162    PRO A  163          0        12.18
CISPEP   2 GLY A  437    GLY A  438          0         2.24
SITE     1 AC1  5 ASN A  72  THR A  74  GLU A  76  ARG A 348
SITE     2 AC1  5 HOH A2331
SITE     1 AC2  4 ASN A 109  ILE A 112  NAG A1626  FUC A1631
SITE     1 AC3  2 NAG A1625  BMA A1632
SITE     1 AC4  3 SER A  45  GLU A  49  NAG A1625
SITE     1 AC5  3 GLU A  43  NAG A1626  BMA A1633
SITE     1 AC6  3 GLU A  43  LYS A  46  BMA A1632
SITE     1 AC7  8 ALA A 354  HIS A 383  GLU A 384  HIS A 387
SITE     2 AC7  8 GLU A 411  TYR A 523   ZN A1634  HOH A2182
SITE     1 AC8  7 GLN A 281  LYS A 511  HIS A 513  TYR A 520
SITE     2 AC8  7 TYR A 523  HOH A2333  HOH A2334
SITE     1 AC9  4 ARG A 186  TRP A 485  TRP A 486  ARG A 489
SITE     1 BC1  4 TYR A 224  PRO A 407  PRO A 519  ARG A 522
SITE     1 BC2  4 HIS A 383  HIS A 387  GLU A 411  ACT A1627
CRYST1   56.633   84.723  134.466  90.00  90.00  90.00 P 21 21 21    4
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      0.017658  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011803  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007437        0.00000
      
PROCHECK
Go to PROCHECK summary
 References