HEADER LYASE 21-SEP-15 5DVX
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC-DOMAIN OF HUMAN CARBONIC ANHYDRASE
TITLE 2 IX AT 1.6 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 9;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC-DOMAIN (UNP RESIDUES 140-399);
COMPND 5 SYNONYM: CARBONATE DEHYDRATASE IX,CARBONIC ANHYDRASE IX,CAIX,MEMBRANE
COMPND 6 ANTIGEN MN,P54/58N,RENAL CELL CARCINOMA-ASSOCIATED ANTIGEN G250,RCC-
COMPND 7 ASSOCIATED ANTIGEN G250,PMW1;
COMPND 8 EC: 4.2.1.1;
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 GENE: CA9, G250, MN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CARBONIC ANHYDRASE IX, CATALYTIC DOMAIN, WATER NETWORK, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.P.MAHON,L.SOCORRO,J.M.DRISCOLL,R.MCKENNA
REVDAT 5 04-DEC-19 5DVX 1 REMARK
REVDAT 4 27-SEP-17 5DVX 1 JRNL REMARK
REVDAT 3 07-SEP-16 5DVX 1 JRNL
REVDAT 2 17-AUG-16 5DVX 1 JRNL
REVDAT 1 03-AUG-16 5DVX 0
JRNL AUTH B.P.MAHON,A.BHATT,L.SOCORRO,J.M.DRISCOLL,C.OKOH,
JRNL AUTH 2 C.L.LOMELINO,M.Y.MBOGE,J.J.KURIAN,C.TU,M.AGBANDJE-MCKENNA,
JRNL AUTH 3 S.C.FROST,R.MCKENNA
JRNL TITL THE STRUCTURE OF CARBONIC ANHYDRASE IX IS ADAPTED FOR LOW-PH
JRNL TITL 2 CATALYSIS.
JRNL REF BIOCHEMISTRY V. 55 4642 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27439028
JRNL DOI 10.1021/ACS.BIOCHEM.6B00243
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 77844
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.320
REMARK 3 FREE R VALUE TEST SET COUNT : 3607
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.8368 - 4.7125 0.99 6196 145 0.1572 0.1492
REMARK 3 2 4.7125 - 3.7487 1.00 6272 142 0.1311 0.1444
REMARK 3 3 3.7487 - 3.2773 1.00 6239 149 0.1506 0.1832
REMARK 3 4 3.2773 - 2.9787 1.00 6260 155 0.1631 0.1765
REMARK 3 5 2.9787 - 2.7658 1.00 6202 147 0.1693 0.1987
REMARK 3 6 2.7658 - 2.6031 1.00 6262 166 0.1650 0.1741
REMARK 3 7 2.6031 - 2.4730 1.00 6229 148 0.1645 0.2026
REMARK 3 8 2.4730 - 2.3656 1.00 6266 159 0.1693 0.2121
REMARK 3 9 2.3656 - 2.2746 1.00 6233 144 0.1721 0.1909
REMARK 3 10 2.2746 - 2.1962 1.00 6253 153 0.1767 0.2484
REMARK 3 11 2.1962 - 2.1276 1.00 6253 143 0.1829 0.2391
REMARK 3 12 2.1276 - 2.0669 1.00 6216 152 0.1752 0.1807
REMARK 3 13 2.0669 - 2.0125 1.00 6240 143 0.1769 0.2183
REMARK 3 14 2.0125 - 1.9635 1.00 6290 145 0.1762 0.2109
REMARK 3 15 1.9635 - 1.9189 1.00 6256 158 0.1889 0.1801
REMARK 3 16 1.9189 - 1.8781 0.99 6213 122 0.1928 0.2003
REMARK 3 17 1.8781 - 1.8405 0.99 6168 156 0.1910 0.2232
REMARK 3 18 1.8405 - 1.8058 0.97 6001 152 0.1810 0.2144
REMARK 3 19 1.8058 - 1.7736 0.95 6014 125 0.1820 0.1880
REMARK 3 20 1.7736 - 1.7435 0.92 5691 144 0.1824 0.2361
REMARK 3 21 1.7435 - 1.7154 0.87 5449 134 0.1876 0.2190
REMARK 3 22 1.7154 - 1.6891 0.83 5162 107 0.1901 0.2170
REMARK 3 23 1.6891 - 1.6642 0.78 4902 121 0.1964 0.2010
REMARK 3 24 1.6642 - 1.6408 0.73 4536 114 0.1952 0.2259
REMARK 3 25 1.6408 - 1.6186 0.71 4450 98 0.1969 0.2000
REMARK 3 26 1.6186 - 1.5976 0.61 3827 85 0.2070 0.2348
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.88
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4324
REMARK 3 ANGLE : 1.151 5897
REMARK 3 CHIRALITY : 0.047 641
REMARK 3 PLANARITY : 0.006 777
REMARK 3 DIHEDRAL : 15.337 1644
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0796 3.4303 -6.2038
REMARK 3 T TENSOR
REMARK 3 T11: 0.0689 T22: 0.0632
REMARK 3 T33: 0.0775 T12: -0.0000
REMARK 3 T13: -0.0111 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.0381 L22: 0.0295
REMARK 3 L33: 0.7488 L12: -0.0120
REMARK 3 L13: 0.0289 L23: -0.2685
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: 0.0280 S13: 0.0043
REMARK 3 S21: 0.0472 S22: -0.0303 S23: -0.0048
REMARK 3 S31: -0.1097 S32: 0.0061 S33: -0.0350
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5DVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-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 : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9177
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86682
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.56500
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: PHENIX
REMARK 200 STARTING MODEL: 3IAI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL, PH 8.5, 8% (W/V) PEG
REMARK 280 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 28.93850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.48200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.37200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.48200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.93850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.37200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 HIS B 140
REMARK 465 SER B 396
REMARK 465 SER B 397
REMARK 465 PRO B 398
REMARK 465 ARG B 399
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 NH2 ARG A 221 O HOH A 501 1.25
REMARK 500 N HIS A 140 O HOH A 502 1.58
REMARK 500 OE1 GLU B 242 O HOH B 501 2.06
REMARK 500 CD ARG A 221 O HOH A 515 2.12
REMARK 500 OE1 GLU B 192 O HOH B 502 2.12
REMARK 500 NH2 ARG A 295 O HOH A 503 2.16
REMARK 500 NE2 HIS A 140 O HOH A 504 2.17
REMARK 500 NH2 ARG A 194 OE2 GLU A 305 2.17
REMARK 500 OD2 ASP B 146 O HOH B 503 2.17
REMARK 500 OE2 GLU A 285 O HOH A 505 2.18
REMARK 500 O HOH B 502 O HOH B 684 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 HIS A 140 CG HIS A 140 CD2 0.102
REMARK 500 HIS A 140 CG HIS A 140 CD2 0.102
REMARK 500 HIS A 140 CG HIS A 140 ND1 -0.129
REMARK 500 HIS A 140 CG HIS A 140 ND1 -0.128
REMARK 500 HIS A 140 C HIS A 140 O 0.161
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 PRO A 391 -168.30 -75.77
REMARK 500 ALA A 392 -86.13 -67.47
REMARK 500 ALA B 232 108.38 -8.64
REMARK 500 ALA B 232 108.38 -55.58
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 HIS A 140 TRP A 141 -91.31
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 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 140 ND1
REMARK 620 2 TRP A 141 N 96.3
REMARK 620 3 TRP A 141 O 168.2 77.7
REMARK 620 4 HIS A 200 NE2 93.4 147.3 86.8
REMARK 620 5 HIS B 244 NE2 136.3 84.5 33.9 67.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 226 NE2
REMARK 620 2 HIS A 228 NE2 105.0
REMARK 620 3 HIS A 251 ND1 113.8 97.2
REMARK 620 4 HOH A 606 O 106.5 115.3 118.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 409 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 244 NE2
REMARK 620 2 TRP B 141 N 108.0
REMARK 620 3 TRP B 141 O 101.6 76.8
REMARK 620 4 HIS B 200 NE2 103.8 147.1 88.8
REMARK 620 5 HOH B 671 O 91.9 89.8 163.3 97.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 226 NE2
REMARK 620 2 HIS B 228 NE2 105.5
REMARK 620 3 HIS B 251 ND1 114.9 98.3
REMARK 620 4 HOH B 575 O 103.9 114.1 119.7
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 405
DBREF 5DVX A 140 399 UNP Q16790 CAH9_HUMAN 140 399
DBREF 5DVX B 140 399 UNP Q16790 CAH9_HUMAN 140 399
SEQADV 5DVX SER A 174 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 5DVX SER A 183 UNP Q16790 LEU 183 ENGINEERED MUTATION
SEQADV 5DVX LYS A 213 UNP Q16790 ALA 213 ENGINEERED MUTATION
SEQADV 5DVX LYS A 258 UNP Q16790 ALA 258 ENGINEERED MUTATION
SEQADV 5DVX TYR A 259 UNP Q16790 PHE 259 ENGINEERED MUTATION
SEQADV 5DVX SER A 350 UNP Q16790 MET 350 ENGINEERED MUTATION
SEQADV 5DVX SER B 174 UNP Q16790 CYS 174 ENGINEERED MUTATION
SEQADV 5DVX SER B 183 UNP Q16790 LEU 183 ENGINEERED MUTATION
SEQADV 5DVX LYS B 213 UNP Q16790 ALA 213 ENGINEERED MUTATION
SEQADV 5DVX LYS B 258 UNP Q16790 ALA 258 ENGINEERED MUTATION
SEQADV 5DVX TYR B 259 UNP Q16790 PHE 259 ENGINEERED MUTATION
SEQADV 5DVX SER B 350 UNP Q16790 MET 350 ENGINEERED MUTATION
SEQRES 1 A 260 HIS TRP ARG TYR GLY GLY ASP PRO PRO TRP PRO ARG VAL
SEQRES 2 A 260 SER PRO ALA CYS ALA GLY ARG PHE GLN SER PRO VAL ASP
SEQRES 3 A 260 ILE ARG PRO GLN LEU ALA ALA PHE SER PRO ALA LEU ARG
SEQRES 4 A 260 PRO LEU GLU LEU SER GLY PHE GLN LEU PRO PRO LEU PRO
SEQRES 5 A 260 GLU LEU ARG LEU ARG ASN ASN GLY HIS SER VAL GLN LEU
SEQRES 6 A 260 THR LEU PRO PRO GLY LEU GLU MET LYS LEU GLY PRO GLY
SEQRES 7 A 260 ARG GLU TYR ARG ALA LEU GLN LEU HIS LEU HIS TRP GLY
SEQRES 8 A 260 ALA ALA GLY ARG PRO GLY SER GLU HIS THR VAL GLU GLY
SEQRES 9 A 260 HIS ARG PHE PRO ALA GLU ILE HIS VAL VAL HIS LEU SER
SEQRES 10 A 260 THR LYS TYR ALA ARG VAL ASP GLU ALA LEU GLY ARG PRO
SEQRES 11 A 260 GLY GLY LEU ALA VAL LEU ALA ALA PHE LEU GLU GLU GLY
SEQRES 12 A 260 PRO GLU GLU ASN SER ALA TYR GLU GLN LEU LEU SER ARG
SEQRES 13 A 260 LEU GLU GLU ILE ALA GLU GLU GLY SER GLU THR GLN VAL
SEQRES 14 A 260 PRO GLY LEU ASP ILE SER ALA LEU LEU PRO SER ASP PHE
SEQRES 15 A 260 SER ARG TYR PHE GLN TYR GLU GLY SER LEU THR THR PRO
SEQRES 16 A 260 PRO CYS ALA GLN GLY VAL ILE TRP THR VAL PHE ASN GLN
SEQRES 17 A 260 THR VAL SER LEU SER ALA LYS GLN LEU HIS THR LEU SER
SEQRES 18 A 260 ASP THR LEU TRP GLY PRO GLY ASP SER ARG LEU GLN LEU
SEQRES 19 A 260 ASN PHE ARG ALA THR GLN PRO LEU ASN GLY ARG VAL ILE
SEQRES 20 A 260 GLU ALA SER PHE PRO ALA GLY VAL ASP SER SER PRO ARG
SEQRES 1 B 260 HIS TRP ARG TYR GLY GLY ASP PRO PRO TRP PRO ARG VAL
SEQRES 2 B 260 SER PRO ALA CYS ALA GLY ARG PHE GLN SER PRO VAL ASP
SEQRES 3 B 260 ILE ARG PRO GLN LEU ALA ALA PHE SER PRO ALA LEU ARG
SEQRES 4 B 260 PRO LEU GLU LEU SER GLY PHE GLN LEU PRO PRO LEU PRO
SEQRES 5 B 260 GLU LEU ARG LEU ARG ASN ASN GLY HIS SER VAL GLN LEU
SEQRES 6 B 260 THR LEU PRO PRO GLY LEU GLU MET LYS LEU GLY PRO GLY
SEQRES 7 B 260 ARG GLU TYR ARG ALA LEU GLN LEU HIS LEU HIS TRP GLY
SEQRES 8 B 260 ALA ALA GLY ARG PRO GLY SER GLU HIS THR VAL GLU GLY
SEQRES 9 B 260 HIS ARG PHE PRO ALA GLU ILE HIS VAL VAL HIS LEU SER
SEQRES 10 B 260 THR LYS TYR ALA ARG VAL ASP GLU ALA LEU GLY ARG PRO
SEQRES 11 B 260 GLY GLY LEU ALA VAL LEU ALA ALA PHE LEU GLU GLU GLY
SEQRES 12 B 260 PRO GLU GLU ASN SER ALA TYR GLU GLN LEU LEU SER ARG
SEQRES 13 B 260 LEU GLU GLU ILE ALA GLU GLU GLY SER GLU THR GLN VAL
SEQRES 14 B 260 PRO GLY LEU ASP ILE SER ALA LEU LEU PRO SER ASP PHE
SEQRES 15 B 260 SER ARG TYR PHE GLN TYR GLU GLY SER LEU THR THR PRO
SEQRES 16 B 260 PRO CYS ALA GLN GLY VAL ILE TRP THR VAL PHE ASN GLN
SEQRES 17 B 260 THR VAL SER LEU SER ALA LYS GLN LEU HIS THR LEU SER
SEQRES 18 B 260 ASP THR LEU TRP GLY PRO GLY ASP SER ARG LEU GLN LEU
SEQRES 19 B 260 ASN PHE ARG ALA THR GLN PRO LEU ASN GLY ARG VAL ILE
SEQRES 20 B 260 GLU ALA SER PHE PRO ALA GLY VAL ASP SER SER PRO ARG
HET ZN A 401 1
HET ZN A 402 1
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET CL A 406 1
HET CL A 407 1
HET TRS A 408 8
HET ZN A 409 1
HET ZN B 401 1
HET GOL B 402 6
HET GOL B 403 6
HET GOL B 404 6
HET CL B 405 1
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 ZN 4(ZN 2+)
FORMUL 5 GOL 6(C3 H8 O3)
FORMUL 8 CL 3(CL 1-)
FORMUL 10 TRS C4 H12 N O3 1+
FORMUL 17 HOH *626(H2 O)
HELIX 1 AA1 PRO A 148 SER A 153 1 6
HELIX 2 AA2 PRO A 154 GLY A 158 5 5
HELIX 3 AA3 ARG A 167 ALA A 171 5 5
HELIX 4 AA4 ARG A 261 LEU A 266 1 6
HELIX 5 AA5 ASN A 286 SER A 294 1 9
HELIX 6 AA6 ARG A 295 ALA A 300 5 6
HELIX 7 AA7 ASP A 312 LEU A 317 5 6
HELIX 8 AA8 SER A 352 THR A 362 1 11
HELIX 9 AA9 PRO B 148 VAL B 152 5 5
HELIX 10 AB1 SER B 153 GLY B 158 5 6
HELIX 11 AB2 ARG B 167 ALA B 171 5 5
HELIX 12 AB3 ARG B 261 LEU B 266 1 6
HELIX 13 AB4 ASN B 286 SER B 294 1 9
HELIX 14 AB5 ARG B 295 ALA B 300 5 6
HELIX 15 AB6 ASP B 312 LEU B 317 5 6
HELIX 16 AB7 SER B 352 THR B 362 1 11
SHEET 1 AA1 2 ASP A 165 ILE A 166 0
SHEET 2 AA1 2 THR A 240 VAL A 241 1 O THR A 240 N ILE A 166
SHEET 1 AA210 ALA A 172 PHE A 173 0
SHEET 2 AA210 GLU A 387 ALA A 388 1 O ALA A 388 N ALA A 172
SHEET 3 AA210 TYR A 324 SER A 330 -1 N GLN A 326 O GLU A 387
SHEET 4 AA210 GLN A 338 PHE A 345 -1 O VAL A 340 N GLY A 329
SHEET 5 AA210 LEU A 272 GLU A 281 1 N ALA A 276 O THR A 343
SHEET 6 AA210 ALA A 248 SER A 256 -1 N HIS A 254 O ALA A 273
SHEET 7 AA210 ARG A 218 TRP A 229 -1 N LEU A 223 O VAL A 253
SHEET 8 AA210 VAL A 202 THR A 205 -1 N LEU A 204 O LEU A 225
SHEET 9 AA210 LEU A 193 ASN A 197 -1 N ARG A 196 O GLN A 203
SHEET 10 AA210 GLU A 305 VAL A 308 -1 O THR A 306 N LEU A 195
SHEET 1 AA3 6 GLU A 181 SER A 183 0
SHEET 2 AA3 6 GLU A 211 GLY A 215 -1 O LYS A 213 N GLU A 181
SHEET 3 AA3 6 ARG A 218 TRP A 229 -1 O ARG A 218 N LEU A 214
SHEET 4 AA3 6 ALA A 248 SER A 256 -1 O VAL A 253 N LEU A 223
SHEET 5 AA3 6 LEU A 272 GLU A 281 -1 O ALA A 273 N HIS A 254
SHEET 6 AA3 6 VAL A 349 LEU A 351 1 O VAL A 349 N GLU A 280
SHEET 1 AA4 2 ASP B 165 ILE B 166 0
SHEET 2 AA4 2 THR B 240 VAL B 241 1 O THR B 240 N ILE B 166
SHEET 1 AA510 ALA B 172 PHE B 173 0
SHEET 2 AA510 GLU B 387 ALA B 388 1 O ALA B 388 N ALA B 172
SHEET 3 AA510 TYR B 324 SER B 330 -1 N GLN B 326 O GLU B 387
SHEET 4 AA510 GLN B 338 PHE B 345 -1 O VAL B 340 N GLY B 329
SHEET 5 AA510 LEU B 272 GLU B 281 1 N ALA B 276 O THR B 343
SHEET 6 AA510 ALA B 248 SER B 256 -1 N HIS B 254 O ALA B 273
SHEET 7 AA510 ARG B 218 TRP B 229 -1 N LEU B 223 O VAL B 253
SHEET 8 AA510 VAL B 202 THR B 205 -1 N LEU B 204 O LEU B 225
SHEET 9 AA510 LEU B 193 ASN B 197 -1 N ARG B 196 O GLN B 203
SHEET 10 AA510 GLU B 305 VAL B 308 -1 O VAL B 308 N LEU B 193
SHEET 1 AA6 6 GLU B 181 SER B 183 0
SHEET 2 AA6 6 GLU B 211 GLY B 215 -1 O LYS B 213 N GLU B 181
SHEET 3 AA6 6 ARG B 218 TRP B 229 -1 O TYR B 220 N MET B 212
SHEET 4 AA6 6 ALA B 248 SER B 256 -1 O VAL B 253 N LEU B 223
SHEET 5 AA6 6 LEU B 272 GLU B 281 -1 O ALA B 273 N HIS B 254
SHEET 6 AA6 6 VAL B 349 LEU B 351 1 O VAL B 349 N GLU B 280
SSBOND 1 CYS A 156 CYS A 336 1555 1555 2.05
SSBOND 2 CYS B 156 CYS B 336 1555 1555 2.05
LINK ND1AHIS A 140 ZN ZN A 402 1555 1555 2.05
LINK N TRP A 141 ZN ZN A 402 1555 1555 2.16
LINK O TRP A 141 ZN ZN A 402 1555 1555 2.31
LINK NE2 HIS A 200 ZN ZN A 402 1555 1555 2.07
LINK NE2 HIS A 226 ZN ZN A 401 1555 1555 2.03
LINK NE2 HIS A 228 ZN ZN A 401 1555 1555 2.08
LINK NE2 HIS A 244 ZN ZN A 409 1555 1555 2.06
LINK ND1 HIS A 251 ZN ZN A 401 1555 1555 2.05
LINK N TRP B 141 ZN ZN A 409 1555 1555 2.06
LINK O TRP B 141 ZN ZN A 409 1555 1555 2.27
LINK NE2 HIS B 200 ZN ZN A 409 1555 1555 2.07
LINK NE2 HIS B 226 ZN ZN B 401 1555 1555 2.04
LINK NE2 HIS B 228 ZN ZN B 401 1555 1555 2.06
LINK ND1 HIS B 251 ZN ZN B 401 1555 1555 2.04
LINK ZN ZN A 401 O HOH A 606 1555 1555 1.94
LINK ZN ZN A 409 O HOH B 671 1555 1555 2.12
LINK ZN ZN B 401 O HOH B 575 1555 1555 1.92
LINK O HIS A 140 CB AGLU B 242 1555 2555 1.41
LINK O HIS A 140 CB BGLU B 242 1555 2555 1.46
LINK NE2 HIS B 244 ZN ZN A 402 1555 2554 2.09
CISPEP 1 ASP A 146 PRO A 147 0 -2.79
CISPEP 2 SER A 162 PRO A 163 0 -0.30
CISPEP 3 LEU A 190 PRO A 191 0 2.79
CISPEP 4 PRO A 334 PRO A 335 0 13.03
CISPEP 5 ASP B 146 PRO B 147 0 -1.02
CISPEP 6 SER B 162 PRO B 163 0 0.45
CISPEP 7 LEU B 190 PRO B 191 0 2.29
CISPEP 8 PRO B 334 PRO B 335 0 13.03
SITE 1 AC1 4 HIS A 226 HIS A 228 HIS A 251 HOH A 606
SITE 1 AC2 4 HIS A 140 TRP A 141 HIS A 200 HIS B 244
SITE 1 AC3 4 GLN A 224 HOH A 506 HOH A 638 HOH A 755
SITE 1 AC4 8 ARG A 151 GLN A 326 TYR A 327 GLU A 328
SITE 2 AC4 8 ILE A 341 HOH A 512 HOH A 538 HOH A 595
SITE 1 AC5 8 ARG A 151 VAL A 152 GLU A 387 HOH A 521
SITE 2 AC5 8 HOH A 646 GLY B 393 VAL B 394 ASP B 395
SITE 1 AC6 2 ARG A 159 GLN A 338
SITE 1 AC7 2 GLU A 242 HOH A 579
SITE 1 AC8 5 LEU A 373 PHE A 375 HOH A 575 HOH A 611
SITE 2 AC8 5 HOH A 675
SITE 1 AC9 4 HIS A 244 TRP B 141 HIS B 200 HOH B 671
SITE 1 AD1 4 HIS B 226 HIS B 228 HIS B 251 HOH B 575
SITE 1 AD2 6 GLN B 224 VAL B 253 HOH B 586 HOH B 602
SITE 2 AD2 6 HOH B 611 HOH B 683
SITE 1 AD3 4 PRO B 269 GLY B 270 GLU B 328 HOH B 511
SITE 1 AD4 6 PRO A 208 PHE B 160 ARG B 384 HOH B 514
SITE 2 AD4 6 HOH B 547 HOH B 707
SITE 1 AD5 2 ARG B 159 GLN B 338
CRYST1 57.877 102.744 108.964 90.00 90.00 90.00 P 21 21 21 8
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 0.017278 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009733 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
