HEADER HYDRO-LYASE 22-DEC-94 1YDD
TITLE STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC
TITLE 2 ANHYDRASE II
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 S.K.NAIR,D.W.CHRISTIANSON
REVDAT 4 14-FEB-24 1YDD 1 REMARK SEQADV LINK
REVDAT 3 29-NOV-17 1YDD 1 HELIX
REVDAT 2 24-FEB-09 1YDD 1 VERSN
REVDAT 1 14-FEB-95 1YDD 0
JRNL AUTH S.K.NAIR,J.F.KREBS,D.W.CHRISTIANSON,C.A.FIERKE
JRNL TITL STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN
JRNL TITL 2 CARBONIC ANHYDRASE II.
JRNL REF BIOCHEMISTRY V. 34 3981 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7696263
JRNL DOI 10.1021/BI00012A016
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 9724
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) : 0.187
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 : 2042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 101
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) : 0.013 ; 0.030
REMARK 3 ANGLE DISTANCE (A) : 0.026 ; 0.050
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.010 ; 0.025
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.096 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.185 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.246 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.260 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 15.600; 20.000
REMARK 3 STAGGERED (DEGREES) : 17.200; 20.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.376 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.666 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.289 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.517 ; 1.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YDD 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_1000177372.
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 (%): 42.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
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 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 SER A 2
REMARK 465 HIS A 3
REMARK 465 LYS A 261
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 359 O HOH A 360 2.03
REMARK 500 OD2 ASP A 162 O HOH A 291 2.17
REMARK 500 OH TYR A 88 O HOH A 359 2.18
REMARK 500 NZ LYS A 252 O HOH A 352 2.19
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 ND2 ASN A 178 NZ LYS A 225 2455 1.56
REMARK 500 NH1 ARG A 58 O GLU A 238 2555 2.19
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 26 CD GLU A 26 OE2 0.083
REMARK 500 GLU A 106 CD GLU A 106 OE2 0.091
REMARK 500 GLU A 117 CD GLU A 117 OE2 0.084
REMARK 500 SER A 188 CB SER A 188 OG 0.084
REMARK 500 GLU A 221 CD GLU A 221 OE1 0.069
REMARK 500 GLU A 234 CD GLU A 234 OE1 0.073
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 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 SER A 29 CA - C - O ANGL. DEV. = -20.4 DEGREES
REMARK 500 SER A 29 O - C - N ANGL. DEV. = 17.6 DEGREES
REMARK 500 PRO A 30 CA - N - CD ANGL. DEV. = -10.6 DEGREES
REMARK 500 PRO A 30 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO A 30 N - CD - CG ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 TYR A 88 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LEU A 148 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ASP A 162 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 182 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PRO A 201 CA - C - O ANGL. DEV. = -21.4 DEGREES
REMARK 500 PRO A 201 O - C - N ANGL. DEV. = 12.0 DEGREES
REMARK 500 PRO A 202 CA - N - CD ANGL. DEV. = -11.1 DEGREES
REMARK 500 PRO A 202 N - CA - CB ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO A 202 N - CD - CG ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 227 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 243 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -4.2 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 -62.95 -109.51
REMARK 500 PHE A 176 69.63 -151.53
REMARK 500 PRO A 202 5.75 -64.43
REMARK 500 ASN A 244 47.64 -102.80
REMARK 500 ASN A 253 -53.18 96.48
REMARK 500 ARG A 254 147.87 -38.91
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 0.19 SIDE CHAIN
REMARK 500 ARG A 182 0.09 SIDE CHAIN
REMARK 500 ARG A 254 0.13 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 96 NE2 111.5
REMARK 620 3 HIS A 119 ND1 110.9 96.9
REMARK 620 4 AZM A 264 N1 93.7 130.3 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 263 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 137 O
REMARK 620 2 GLU A 205 O 87.6
REMARK 620 3 CYS A 206 SG 89.6 93.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZM A 264
DBREF 1YDD A 2 261 UNP P00918 CAH2_HUMAN 1 259
SEQADV 1YDD ARG A 198 UNP P00918 LEU 196 CONFLICT
SEQRES 1 A 259 SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES 2 A 259 HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES 3 A 259 GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES 4 A 259 ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES 5 A 259 ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES 6 A 259 ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES 7 A 259 LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES 8 A 259 PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES 9 A 259 GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES 10 A 259 HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES 11 A 259 LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES 12 A 259 ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES 13 A 259 LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES 14 A 259 LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES 15 A 259 LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES 16 A 259 ARG THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES 17 A 259 VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES 18 A 259 LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES 19 A 259 PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES 20 A 259 PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 262 1
HET HG A 263 1
HET AZM A 264 13
HETNAM ZN ZINC ION
HETNAM HG MERCURY (II) ION
HETNAM AZM 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE
FORMUL 2 ZN ZN 2+
FORMUL 3 HG HG 2+
FORMUL 4 AZM C4 H6 N4 O3 S2
FORMUL 5 HOH *101(H2 O)
HELIX 1 A PRO A 13 LYS A 18 5 6
HELIX 2 B PRO A 21 LYS A 24 5 4
HELIX 3 C THR A 125 TYR A 128 5 3
HELIX 4 D PHE A 131 ALA A 134 1 4
HELIX 5 E PRO A 155 ILE A 167 5158-163 RIGHT HANDED ALPHA 13
HELIX 6 F PRO A 181 LEU A 184 5 4
HELIX 7 G SER A 220 PHE A 226 1 7
SHEET 1 S10 SER A 173 ASP A 175 0
SHEET 2 S10 SER A 56 ASN A 61 -1 O ILE A 59 N ALA A 174
SHEET 3 S10 PHE A 66 PHE A 70 -1 O ASN A 67 N LEU A 60
SHEET 4 S10 TYR A 88 TRP A 97 -1 O PHE A 93 N VAL A 68
SHEET 5 S10 ALA A 116 ASN A 124 -1 O HIS A 119 N HIS A 94
SHEET 6 S10 LEU A 141 VAL A 150 -1 O LEU A 144 N LEU A 120
SHEET 7 S10 VAL A 207 LEU A 212 1 O ILE A 210 N GLY A 145
SHEET 8 S10 TYR A 191 GLY A 196 -1 O TRP A 192 N VAL A 211
SHEET 9 S10 LYS A 257 ALA A 258 -1 O LYS A 257 N THR A 193
SHEET 10 S10 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 2.29
LINK NE2 HIS A 96 ZN ZN A 262 1555 1555 1.90
LINK ND1 HIS A 119 ZN ZN A 262 1555 1555 2.05
LINK O GLN A 137 HG HG A 263 1555 1555 2.80
LINK O GLU A 205 HG HG A 263 1555 1555 3.25
LINK SG CYS A 206 HG HG A 263 1555 1555 2.28
LINK ZN ZN A 262 N1 AZM A 264 1555 1555 1.70
CISPEP 1 SER A 29 PRO A 30 0 4.46
CISPEP 2 PRO A 201 PRO A 202 0 -6.39
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 AZM A 264
SITE 1 AC2 3 GLN A 137 GLU A 205 CYS A 206
SITE 1 AC3 9 HIS A 94 HIS A 96 HIS A 119 VAL A 121
SITE 2 AC3 9 PHE A 131 ARG A 198 THR A 199 THR A 200
SITE 3 AC3 9 ZN A 262
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
