HEADER LYASE 15-NOV-15 5FNI
TITLE NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
TITLE 2 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
TITLE 3 COMBINATION
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PACA
KEYWDS LYASE, FRAGMENTS, CARBONIC ANHYDRASE, METALLOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.A.WOODS,O.DOLEZAL,B.REN,J.H.RYAN,T.S.PEAT,S.A.POULSEN
REVDAT 5 10-JAN-24 5FNI 1 REMARK LINK
REVDAT 4 08-MAY-19 5FNI 1 REMARK
REVDAT 3 19-APR-17 5FNI 1 REMARK
REVDAT 2 23-MAR-16 5FNI 1 JRNL
REVDAT 1 02-MAR-16 5FNI 0
JRNL AUTH L.WOODS,O.DOLEZAL,B.REN,J.H.RYAN,T.S.PEAT,S.POULSEN
JRNL TITL NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE
JRNL TITL 2 AND X-RAY CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT
JRNL TITL 3 SCREENING COMBINATION.
JRNL REF J.MED.CHEM. V. 59 2192 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26882437
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01940
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 30348
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) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1596
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1793
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 109
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2059
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 241
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23000
REMARK 3 B22 (A**2) : 0.07000
REMARK 3 B33 (A**2) : 0.17000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.603
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2241 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2087 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3050 ; 1.944 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4843 ; 1.051 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 278 ; 6.822 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;38.315 ;24.712
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 374 ;13.150 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;18.931 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 315 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2591 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 522 ; 0.002 ; 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): 1082 ; 1.977 ; 1.842
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1081 ; 1.971 ; 1.839
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1367 ; 2.759 ; 3.103
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1159 ; 3.393 ; 2.263
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): 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 RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5FNI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1290065528.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-15
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 : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953700
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31958
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 41.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: 4CQ0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 MG/ML PROTEIN WITH 2.7 M AMMONIUM
REMARK 280 SULFATE, 100 MM TRIS PH 8.5 AT 8 C IN SITTING DROPS., VAPOR
REMARK 280 DIFFUSION, SITTING DROP
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 20.77200
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 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 2124 O HOH A 2128 1.90
REMARK 500 O HOH A 2196 O HOH A 2198 2.12
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 NZ LYS A 24 O1 GOL A 1263 1655 2.04
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 ASP A 101 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 190 CB - CG - OD2 ANGL. DEV. = -5.9 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 ARG A 27 52.25 -144.67
REMARK 500 ARG A 27 47.66 -142.52
REMARK 500 LYS A 111 -1.61 72.84
REMARK 500 PHE A 176 63.65 -151.12
REMARK 500 ASN A 244 49.21 -93.29
REMARK 500 LYS A 252 -134.01 56.64
REMARK 500 LYS A 252 -134.10 56.70
REMARK 500 ASN A 253 60.53 -103.58
REMARK 500 ASN A 253 60.53 -103.65
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 A1262 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 104.9
REMARK 620 3 HIS A 119 ND1 114.5 96.0
REMARK 620 4 YIH A1265 N14 106.6 131.4 103.4
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 1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YIH A 1265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FNG RELATED DB: PDB
REMARK 900 NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
REMARK 900 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
REMARK 900 COMBINATION
REMARK 900 RELATED ID: 5FNH RELATED DB: PDB
REMARK 900 NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
REMARK 900 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
REMARK 900 COMBINATION
REMARK 900 RELATED ID: 5FNJ RELATED DB: PDB
REMARK 900 NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
REMARK 900 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
REMARK 900 COMBINATION
REMARK 900 RELATED ID: 5FNK RELATED DB: PDB
REMARK 900 NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
REMARK 900 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
REMARK 900 COMBINATION
REMARK 900 RELATED ID: 5FNL RELATED DB: PDB
REMARK 900 NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
REMARK 900 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
REMARK 900 COMBINATION
REMARK 900 RELATED ID: 5FNM RELATED DB: PDB
REMARK 900 NATIVE STATE MASS SPECTROMETRY, SURFACE PLASMON RESONANCE AND X-RAY
REMARK 900 CRYSTALLOGRAPHY CORRELATE STRONGLY AS A FRAGMENT SCREENING
REMARK 900 COMBINATION
DBREF 5FNI A 1 261 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 A1262 1
HET GOL A1263 6
HET DMS A1264 4
HET YIH A1265 15
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM YIH 5-[[3,4-BIS(CHLORANYL)PHENOXY]METHYL]-1,2,4-TRIAZA-3-
HETNAM 2 YIH AZANIDACYCLOPENTA-1,4-DIENE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 GOL C3 H8 O3
FORMUL 4 DMS C2 H6 O S
FORMUL 5 YIH C8 H5 CL2 N4 O 1-
FORMUL 6 HOH *241(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 127 GLY A 129 5 3
HELIX 4 4 ASP A 130 VAL A 135 1 6
HELIX 5 5 LYS A 154 GLY A 156 5 3
HELIX 6 6 LEU A 157 LEU A 164 1 8
HELIX 7 7 ASP A 165 LYS A 168 5 4
HELIX 8 8 ASP A 180 LEU A 185 5 6
HELIX 9 9 SER A 219 ARG A 227 1 9
SHEET 1 AA 2 ASP A 32 ILE A 33 0
SHEET 2 AA 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 AB 6 LYS A 39 TYR A 40 0
SHEET 2 AB 6 LYS A 257 ALA A 258 1 N ALA A 258 O LYS A 39
SHEET 3 AB 6 TYR A 191 GLY A 196 -1 O THR A 193 N LYS A 257
SHEET 4 AB 6 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 AB 6 LEU A 141 VAL A 150 1 O LEU A 141 N THR A 208
SHEET 6 AB 6 ILE A 216 VAL A 218 -1 O ILE A 216 N LYS A 149
SHEET 1 AC 9 LYS A 39 TYR A 40 0
SHEET 2 AC 9 LYS A 257 ALA A 258 1 N ALA A 258 O LYS A 39
SHEET 3 AC 9 TYR A 191 GLY A 196 -1 O THR A 193 N LYS A 257
SHEET 4 AC 9 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 AC 9 LEU A 141 VAL A 150 1 O LEU A 141 N THR A 208
SHEET 6 AC 9 ALA A 116 ASN A 124 -1 O ALA A 116 N LEU A 148
SHEET 7 AC 9 TYR A 88 TRP A 97 -1 O ARG A 89 N TRP A 123
SHEET 8 AC 9 VAL A 78 GLY A 81 -1 O LEU A 79 N TYR A 88
SHEET 9 AC 9 LEU A 47 SER A 50 -1 O SER A 48 N LYS A 80
SHEET 1 AD10 LYS A 39 TYR A 40 0
SHEET 2 AD10 LYS A 257 ALA A 258 1 N ALA A 258 O LYS A 39
SHEET 3 AD10 TYR A 191 GLY A 196 -1 O THR A 193 N LYS A 257
SHEET 4 AD10 VAL A 207 LEU A 212 -1 O VAL A 207 N GLY A 196
SHEET 5 AD10 LEU A 141 VAL A 150 1 O LEU A 141 N THR A 208
SHEET 6 AD10 ALA A 116 ASN A 124 -1 O ALA A 116 N LEU A 148
SHEET 7 AD10 TYR A 88 TRP A 97 -1 O ARG A 89 N TRP A 123
SHEET 8 AD10 PHE A 66 PHE A 70 -1 O PHE A 66 N PHE A 95
SHEET 9 AD10 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 10 AD10 SER A 173 ASP A 175 1 O ALA A 174 N ILE A 59
SHEET 1 AE 2 ILE A 216 VAL A 218 0
SHEET 2 AE 2 LEU A 141 VAL A 150 -1 O PHE A 147 N ILE A 216
LINK NE2 HIS A 94 ZN ZN A1262 1555 1555 2.03
LINK NE2 HIS A 96 ZN ZN A1262 1555 1555 2.02
LINK ND1 HIS A 119 ZN ZN A1262 1555 1555 2.10
LINK ZN ZN A1262 N14 YIH A1265 1555 1555 1.95
CISPEP 1 SER A 29 PRO A 30 0 -2.40
CISPEP 2 PRO A 201 PRO A 202 0 7.36
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 YIH A1265
SITE 1 AC2 4 HIS A 17 LYS A 24 SER A 188 LEU A 189
SITE 1 AC3 4 TYR A 7 ASP A 243 TRP A 245 HOH A2108
SITE 1 AC4 10 GLN A 92 HIS A 94 HIS A 96 HIS A 119
SITE 2 AC4 10 LEU A 198 THR A 199 THR A 200 TRP A 209
SITE 3 AC4 10 ZN A1262 HOH A2241
CRYST1 42.687 41.544 72.090 90.00 104.44 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 0.023426 0.000000 0.006032 0.00000
SCALE2 0.000000 0.024071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014324 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
