HEADER LYASE/LYASE INHIBITOR 20-SEP-13 4MTY
TITLE STRUCTURE AT 1A RESOLUTION OF A HELICAL AROMATIC FOLDAMER-PROTEIN
TITLE 2 COMPLEX.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC,
COMPND 5 CARBONIC ANHYDRASE II, CA-II;
COMPND 6 EC: 4.2.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CA2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MIXED ALPHA BETA, LYASE-LYASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.OGAYONE,J.BURATTO,B.LANGLOIS D'ESTAINTOT,M.STUPFEL,T.GRANIER,
AUTHOR 2 B.GALLOIS,Y.HUC
REVDAT 5 20-SEP-23 4MTY 1 REMARK LINK
REVDAT 4 19-JUL-17 4MTY 1 TITLE
REVDAT 3 05-JUL-17 4MTY 1 TITLE
REVDAT 2 22-JAN-14 4MTY 1 JRNL
REVDAT 1 11-DEC-13 4MTY 0
JRNL AUTH J.BURATTO,C.COLOMBO,M.STUPFEL,S.J.DAWSON,C.DOLAIN,
JRNL AUTH 2 B.LANGLOIS D'ESTAINTOT,L.FISCHER,T.GRANIER,M.LAGUERRE,
JRNL AUTH 3 B.GALLOIS,I.HUC
JRNL TITL STRUCTURE OF A COMPLEX FORMED BY A PROTEIN AND A HELICAL
JRNL TITL 2 AROMATIC OLIGOAMIDE FOLDAMER AT 2.1 A RESOLUTION.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 53 883 2014
JRNL REFN ISSN 1433-7851
JRNL PMID 24288253
JRNL DOI 10.1002/ANIE.201309160
REMARK 2
REMARK 2 RESOLUTION. 1.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 128692
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) : 0.106
REMARK 3 R VALUE (WORKING SET) : 0.105
REMARK 3 FREE R VALUE : 0.123
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6479
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) : 1.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9121
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.1620
REMARK 3 BIN FREE R VALUE SET COUNT : 446
REMARK 3 BIN FREE R VALUE : 0.1820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2019
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 99
REMARK 3 SOLVENT ATOMS : 398
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.017
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.018
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.010
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.408
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2294 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2059 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3141 ; 1.898 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4765 ; 1.499 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 289 ; 6.942 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;34.525 ;24.653
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 345 ;10.460 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;22.054 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 324 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2654 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 543 ; 0.007 ; 0.020
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): 1093 ; 1.209 ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1092 ; 1.203 ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1385 ; 1.568 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2189 ; 7.426 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 57 ;28.896 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2380 ; 9.710 ; 5.000
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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4MTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000082361.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-08
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA CCP4_3.2.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128713
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.490
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : 0.09800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1470
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15 MM HCA2, 50 MM TRIS PH 8.5, 150
REMARK 280 MM NACL, 2MM 4-(HYDROXYMERCURY)BENZOATE, 2.7 M (NH4)2SO4, 3 MM
REMARK 280 NAN3, 0.75 MM BENZAMIDE N-(3-HYDROXYBENZYL)-4-SULFAMOYL., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 20.77950
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 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 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 MET A 1
REMARK 465 SER A 2
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 HIS A 4 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 LYS A 45 CD CE NZ
REMARK 470 GLN A 53 NE2
REMARK 470 GLN A 74 CG CD OE1 NE2
REMARK 470 LYS A 80 CE NZ
REMARK 470 ASP A 85 OD1
REMARK 470 LYS A 126 NZ
REMARK 470 LYS A 132 CE NZ
REMARK 470 LYS A 148 NZ
REMARK 470 LYS A 158 CD CE NZ
REMARK 470 LYS A 169 NZ
REMARK 470 LYS A 171 NZ
REMARK 470 LYS A 212 CB
REMARK 470 LYS A 227 CE NZ
REMARK 470 GLU A 238 CD OE1 OE2
REMARK 470 LYS A 260 CG CD CE NZ
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. = -4.5 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 GLU A 220 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 PHE A 225 CB - CG - CD1 ANGL. DEV. = 5.3 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 ASN A 11 12.49 -141.65
REMARK 500 ARG A 27 46.34 -151.88
REMARK 500 GLU A 106 -61.32 -92.06
REMARK 500 LYS A 111 -4.35 74.77
REMARK 500 PHE A 175 63.52 -150.52
REMARK 500 PHE A 175 63.52 -151.90
REMARK 500 ASN A 243 48.74 -93.52
REMARK 500 LYS A 251 -140.97 55.13
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 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 103.8
REMARK 620 3 HIS A 119 ND1 112.5 99.7
REMARK 620 4 SBW A 302 N02 110.7 114.2 114.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A 309 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 134 O
REMARK 620 2 CYS A 205 SG 82.8
REMARK 620 3 HOH A 531 O 59.1 121.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HGB A 304 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 136 O
REMARK 620 2 HGB A 304 C7 98.5
REMARK 620 3 GLU A 204 O 92.7 87.8
REMARK 620 4 CYS A 205 SG 83.6 176.8 94.5
REMARK 620 5 HOH A 531 O 133.4 97.1 131.6 79.7
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 ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SBW A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SBW A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HGB A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SBW A 310
DBREF 4MTY A 1 260 UNP P00918 CAH2_HUMAN 1 260
SEQRES 1 A 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 A 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 A 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 A 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 A 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 A 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 A 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 A 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 A 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 A 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 A 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 A 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 A 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 A 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 A 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 A 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 A 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 A 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 A 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET ZN A 301 1
HET SBW A 302 21
HET SBW A 303 21
HET HGB A 304 10
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET GOL A 308 6
HET HG A 309 1
HET SBW A 310 21
HETNAM ZN ZINC ION
HETNAM SBW N-(3-HYDROXYBENZYL)-4-SULFAMOYLBENZAMIDE
HETNAM HGB 4-(HYDROXYMERCURY)BENZOIC ACID
HETNAM GOL GLYCEROL
HETNAM HG MERCURY (II) ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 SBW 3(C14 H14 N2 O4 S)
FORMUL 5 HGB C7 H6 HG O3
FORMUL 6 GOL 4(C3 H8 O3)
FORMUL 10 HG HG 2+
FORMUL 12 HOH *398(H2 O)
HELIX 1 1 HIS A 15 ASP A 19 5 5
HELIX 2 2 PHE A 20 GLY A 25 5 6
HELIX 3 3 LYS A 126 GLY A 128 5 3
HELIX 4 4 ASP A 129 VAL A 134 1 6
HELIX 5 5 LYS A 153 GLY A 155 5 3
HELIX 6 6 LEU A 156 LEU A 163 1 8
HELIX 7 7 ASP A 164 ILE A 166 5 3
HELIX 8 8 ASP A 179 LEU A 184 5 6
HELIX 9 9 SER A 218 ARG A 226 1 9
SHEET 1 A 2 ASP A 32 ILE A 33 0
SHEET 2 A 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 B10 LYS A 39 TYR A 40 0
SHEET 2 B10 LYS A 256 ALA A 257 1 O ALA A 257 N LYS A 39
SHEET 3 B10 TYR A 190 GLY A 195 -1 N THR A 192 O LYS A 256
SHEET 4 B10 VAL A 206 LEU A 211 -1 O VAL A 206 N GLY A 195
SHEET 5 B10 LEU A 140 VAL A 149 1 N GLY A 144 O LEU A 211
SHEET 6 B10 ALA A 116 ASN A 124 -1 N LEU A 118 O ILE A 145
SHEET 7 B10 TYR A 88 TRP A 97 -1 N HIS A 94 O HIS A 119
SHEET 8 B10 PHE A 66 PHE A 70 -1 N VAL A 68 O PHE A 93
SHEET 9 B10 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 10 B10 SER A 172 ASP A 174 -1 O ALA A 173 N ILE A 59
SHEET 1 C 6 LYS A 45 SER A 50 0
SHEET 2 C 6 VAL A 78 GLY A 82 -1 O VAL A 78 N SER A 50
SHEET 3 C 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 C 6 ALA A 116 ASN A 124 -1 O HIS A 119 N HIS A 94
SHEET 5 C 6 LEU A 140 VAL A 149 -1 O ILE A 145 N LEU A 118
SHEET 6 C 6 ILE A 215 VAL A 217 1 O ILE A 215 N PHE A 146
LINK NE2 HIS A 94 ZN ZN A 301 1555 1555 2.00
LINK NE2 HIS A 96 ZN ZN A 301 1555 1555 2.02
LINK ND1 HIS A 119 ZN ZN A 301 1555 1555 2.02
LINK O VAL A 134 HG HG A 309 1555 1555 3.05
LINK O GLN A 136 HG HGB A 304 1555 1555 2.94
LINK O GLU A 204 HG HGB A 304 1555 1555 3.07
LINK SG ACYS A 205 HG HGB A 304 1555 1555 2.34
LINK SG BCYS A 205 HG HG A 309 1555 1555 2.31
LINK ZN ZN A 301 N02 SBW A 302 1555 1555 1.96
LINK HG HGB A 304 O HOH A 531 1555 1555 2.94
LINK HG HG A 309 O HOH A 531 1555 1555 2.48
CISPEP 1 SER A 29 PRO A 30 0 -3.75
CISPEP 2 PRO A 200 PRO A 201 0 15.59
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 SBW A 302
SITE 1 AC2 15 HIS A 94 HIS A 96 HIS A 119 PHE A 130
SITE 2 AC2 15 LEU A 197 THR A 198 THR A 199 PRO A 201
SITE 3 AC2 15 TRP A 208 ZN A 301 GOL A 308 SBW A 310
SITE 4 AC2 15 HOH A 431 HOH A 684 HOH A 745
SITE 1 AC3 12 HIS A 3 TRP A 5 HIS A 10 ASN A 11
SITE 2 AC3 12 HIS A 15 TRP A 16 ASP A 19 PHE A 20
SITE 3 AC3 12 ARG A 181 GLY A 182 HOH A 575 HOH A 787
SITE 1 AC4 10 GLN A 135 GLN A 136 PRO A 137 GLU A 204
SITE 2 AC4 10 CYS A 205 HG A 309 HOH A 531 HOH A 637
SITE 3 AC4 10 HOH A 642 HOH A 706
SITE 1 AC5 9 ASN A 62 HIS A 64 ALA A 65 ASN A 67
SITE 2 AC5 9 GLN A 92 HIS A 94 HOH A 416 HOH A 568
SITE 3 AC5 9 HOH A 612
SITE 1 AC6 4 LYS A 39 GLN A 254 LYS A 256 HOH A 660
SITE 1 AC7 7 TYR A 7 PRO A 13 ASP A 242 TRP A 244
SITE 2 AC7 7 HOH A 535 HOH A 616 HOH A 789
SITE 1 AC8 5 GLN A 92 PHE A 130 SBW A 302 SBW A 310
SITE 2 AC8 5 HOH A 721
SITE 1 AC9 5 VAL A 134 GLN A 136 CYS A 205 HGB A 304
SITE 2 AC9 5 HOH A 531
SITE 1 BC1 11 LEU A 57 PHE A 70 ASP A 72 ILE A 91
SITE 2 BC1 11 SBW A 302 GOL A 308 HOH A 434 HOH A 443
SITE 3 BC1 11 HOH A 469 HOH A 594 HOH A 721
CRYST1 42.444 41.559 72.064 90.00 104.41 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 0.023560 0.000000 0.006055 0.00000
SCALE2 0.000000 0.024062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014328 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
