HEADER HYDRO-LYASE 16-NOV-94 1CVH
TITLE STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS HYDRO-LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.IPPOLITO,D.W.CHRISTIANSON
REVDAT 4 07-FEB-24 1CVH 1 REMARK SEQADV LINK
REVDAT 3 29-NOV-17 1CVH 1 HELIX
REVDAT 2 24-FEB-09 1CVH 1 VERSN
REVDAT 1 07-FEB-95 1CVH 0
JRNL AUTH J.A.IPPOLITO,D.W.CHRISTIANSON
JRNL TITL STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC
JRNL TITL 2 BINDING SITE.
JRNL REF BIOCHEMISTRY V. 33 15241 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 7803386
JRNL DOI 10.1021/BI00255A004
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 7746
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2025
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 111
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.017 ; 0.300
REMARK 3 ANGLE DISTANCE (A) : 0.041 ; 0.600
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.035 ; 0.600
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.007 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.089 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.188 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.222 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.241 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.100 ; 15.000
REMARK 3 STAGGERED (DEGREES) : 15.800; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.298 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.518 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.256 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.438 ; 1.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CVH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172561.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 43.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 20.85000
REMARK 290 SMTRY3 2 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 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 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 SECONDARY STRUCTURE ELEMENTS WERE DEFINED USING THE PROGRAM
REMARK 400 *DSSP* (W. KABSCH, C. SANDER, BIOPOLYMERS, V. 22, P. 2577,
REMARK 400 1983).
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 HOH A 264 O HOH A 265 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 162 O HOH A 320 2445 1.69
REMARK 500 CG LYS A 133 O HOH A 371 1565 2.07
REMARK 500 CE LYS A 133 O HOH A 371 1565 2.11
REMARK 500 N GLY A 102 OD1 ASP A 130 1545 2.17
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 GLU A 106 CD GLU A 106 OE1 -0.075
REMARK 500 GLU A 236 CD GLU A 236 OE1 -0.075
REMARK 500 GLU A 239 CD GLU A 239 OE2 0.094
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 PHE A 20 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 LYS A 24 CA - CB - CG ANGL. DEV. = 19.8 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP A 32 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 34 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 THR A 37 CA - CB - CG2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 TYR A 51 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 58 CD - NE - CZ ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 71 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ASP A 72 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 75 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLU A 106 CG - CD - OE1 ANGL. DEV. = 13.4 DEGREES
REMARK 500 GLN A 158 O - C - N ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLU A 187 OE1 - CD - OE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 SER A 197 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 THR A 208 N - CA - CB ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 GLU A 236 CG - CD - OE1 ANGL. DEV. = 14.1 DEGREES
REMARK 500 GLU A 236 CG - CD - OE2 ANGL. DEV. = -13.9 DEGREES
REMARK 500 ASN A 253 O - C - N ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = 3.7 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
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 LEU A 57 -52.16 -124.32
REMARK 500 ALA A 65 -171.21 -170.58
REMARK 500 LYS A 111 -2.87 76.85
REMARK 500 VAL A 135 3.17 -67.42
REMARK 500 ASN A 244 53.99 -100.96
REMARK 500 ASN A 253 -42.71 91.89
REMARK 500 ARG A 254 155.42 -48.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 58 0.08 SIDE CHAIN
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 262 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 119 ND1 119.0
REMARK 620 3 HOH A 263 O 117.8 102.2
REMARK 620 4 HOH A 264 O 110.4 103.4 101.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 262
DBREF 1CVH A 5 260 UNP P00918 CAH2_HUMAN 4 258
SEQADV 1CVH CYS A 96 UNP P00918 HIS 95 CONFLICT
SEQRES 1 A 255 TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS TRP HIS
SEQRES 2 A 255 LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN SER PRO
SEQRES 3 A 255 VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP PRO SER
SEQRES 4 A 255 LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA THR SER
SEQRES 5 A 255 LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN VAL GLU
SEQRES 6 A 255 PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS GLY GLY
SEQRES 7 A 255 PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE HIS PHE
SEQRES 8 A 255 CYS TRP GLY SER LEU ASP GLY GLN GLY SER GLU HIS THR
SEQRES 9 A 255 VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS LEU VAL
SEQRES 10 A 255 HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS ALA VAL
SEQRES 11 A 255 GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE PHE LEU
SEQRES 12 A 255 LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS VAL VAL
SEQRES 13 A 255 ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS SER ALA
SEQRES 14 A 255 ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU PRO GLU
SEQRES 15 A 255 SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU THR THR
SEQRES 16 A 255 PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL LEU LYS
SEQRES 17 A 255 GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU LYS PHE
SEQRES 18 A 255 ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO GLU GLU
SEQRES 19 A 255 LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO LEU LYS
SEQRES 20 A 255 ASN ARG GLN ILE LYS ALA SER PHE
HET ZN A 262 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
FORMUL 3 HOH *111(H2 O)
HELIX 1 HA PRO A 13 LYS A 18 5 6
HELIX 2 HB PRO A 21 LYS A 24 5 4
HELIX 3 HC THR A 125 TYR A 128 5 3
HELIX 4 HD PHE A 131 ALA A 134 1 4
HELIX 5 HE PRO A 155 ILE A 167 5158-163 RIGHT-HANDED ALPHA 13
HELIX 6 HF PRO A 181 LEU A 184 5 4
HELIX 7 HG SER A 220 PHE A 226 1 7
SHEET 1 S110 SER A 173 ASP A 175 0
SHEET 2 S110 SER A 56 ASN A 61 -1 O ILE A 59 N ALA A 174
SHEET 3 S110 PHE A 66 PHE A 70 -1 O ASN A 67 N LEU A 60
SHEET 4 S110 TYR A 88 TRP A 97 -1 O PHE A 93 N VAL A 68
SHEET 5 S110 ALA A 116 ASN A 124 -1 O HIS A 119 N HIS A 94
SHEET 6 S110 LEU A 141 VAL A 150 -1 O LEU A 144 N LEU A 120
SHEET 7 S110 VAL A 207 LEU A 212 1 O ILE A 210 N GLY A 145
SHEET 8 S110 TYR A 191 GLY A 196 -1 O TRP A 192 N VAL A 211
SHEET 9 S110 LYS A 257 ALA A 258 -1 O LYS A 257 N THR A 193
SHEET 10 S110 LYS A 39 TYR A 40 1 O LYS A 39 N ALA A 258
LINK NE2 HIS A 94 ZN ZN A 262 1555 1555 2.22
LINK ND1 HIS A 119 ZN ZN A 262 1555 1555 2.13
LINK ZN ZN A 262 O HOH A 263 1555 1555 2.39
LINK ZN ZN A 262 O HOH A 264 1555 1555 2.46
CISPEP 1 SER A 29 PRO A 30 0 -6.56
CISPEP 2 PRO A 201 PRO A 202 0 5.71
SITE 1 AC1 4 HIS A 94 HIS A 119 HOH A 263 HOH A 264
CRYST1 42.700 41.700 73.000 90.00 104.60 90.00 P 1 21 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 0.023419 0.000000 0.006100 0.00000
SCALE2 0.000000 0.023981 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014156 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
