HEADER HYDROLASE 14-JUL-09 3IAR
TITLE THE CRYSTAL STRUCTURE OF HUMAN ADENOSINE DEAMINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE DEAMINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 5-363;
COMPND 5 SYNONYM: ADENOSINE AMINOHYDROLASE;
COMPND 6 EC: 3.5.4.4;
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: ADA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF
KEYWDS DEAMINASE, ADENOSINE DEAMINASE, ADENOSINE, PURINE METABOLISM,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, DISEASE
KEYWDS 3 MUTATION, HEREDITARY HEMOLYTIC ANEMIA, HYDROLASE, NUCLEOTIDE
KEYWDS 4 METABOLISM, SCID
EXPDTA X-RAY DIFFRACTION
AUTHOR E.UGOCHUKWU,Y.ZHANG,E.HAPKA,W.W.YUE,J.E.BRAY,J.MUNIZ,N.BURGESS-BROWN,
AUTHOR 2 A.CHAIKUAD,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,
AUTHOR 3 K.L.KAVANAGH,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 2 13-JUL-11 3IAR 1 VERSN
REVDAT 1 11-AUG-09 3IAR 0
JRNL AUTH E.UGOCHUKWU,Y.ZHANG,E.HAPKA,W.W.YUE,J.E.BRAY,J.MUNIZ,
JRNL AUTH 2 N.BURGESS-BROWN,A.CHAIKUAD,K.L.KAVANAGH,U.OPPERMANN
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN ADENOSINE DEAMINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 52324
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.630
REMARK 3 FREE R VALUE TEST SET COUNT : 1901
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 29.7035 - 3.6613 0.99 3869 143 0.1360 0.1707
REMARK 3 2 3.6613 - 2.9069 1.00 3756 141 0.1289 0.1513
REMARK 3 3 2.9069 - 2.5397 1.00 3740 135 0.1360 0.1640
REMARK 3 4 2.5397 - 2.3076 1.00 3704 140 0.1341 0.1660
REMARK 3 5 2.3076 - 2.1422 1.00 3706 142 0.1240 0.1598
REMARK 3 6 2.1422 - 2.0160 1.00 3678 137 0.1280 0.1743
REMARK 3 7 2.0160 - 1.9150 1.00 3655 146 0.1299 0.1796
REMARK 3 8 1.9150 - 1.8317 1.00 3675 133 0.1334 0.2047
REMARK 3 9 1.8317 - 1.7612 1.00 3675 134 0.1359 0.1575
REMARK 3 10 1.7612 - 1.7004 1.00 3628 131 0.1340 0.1726
REMARK 3 11 1.7004 - 1.6472 0.99 3645 151 0.1373 0.1645
REMARK 3 12 1.6472 - 1.6002 0.98 3585 129 0.1495 0.1673
REMARK 3 13 1.6002 - 1.5580 0.92 3342 134 0.1680 0.2053
REMARK 3 14 1.5580 - 1.5200 0.76 2765 105 0.1939 0.2191
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 : 0.32
REMARK 3 B_SOL : 32.94
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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 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 : 0.014 3020
REMARK 3 ANGLE : 1.518 4106
REMARK 3 CHIRALITY : 0.098 444
REMARK 3 PLANARITY : 0.009 540
REMARK 3 DIHEDRAL : 16.224 1123
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:74)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2713 7.4552 -4.6709
REMARK 3 T TENSOR
REMARK 3 T11: 0.0861 T22: 0.0820
REMARK 3 T33: -0.0094 T12: -0.0044
REMARK 3 T13: 0.0036 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.1280 L22: 0.0410
REMARK 3 L33: 0.0419 L12: 0.0334
REMARK 3 L13: 0.1902 L23: 0.0008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.0749 S13: -0.0133
REMARK 3 S21: -0.0411 S22: 0.0249 S23: -0.0058
REMARK 3 S31: -0.0298 S32: 0.0284 S33: -0.0048
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 75:196)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7735 2.2968 9.4301
REMARK 3 T TENSOR
REMARK 3 T11: 0.0792 T22: 0.0609
REMARK 3 T33: -0.0250 T12: 0.0009
REMARK 3 T13: -0.0148 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0787 L22: 0.1254
REMARK 3 L33: 0.0111 L12: -0.0322
REMARK 3 L13: 0.0169 L23: -0.0810
REMARK 3 S TENSOR
REMARK 3 S11: 0.0149 S12: 0.0012 S13: -0.0046
REMARK 3 S21: 0.0749 S22: -0.0198 S23: -0.0149
REMARK 3 S31: -0.0408 S32: 0.0024 S33: 0.0081
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 197:238)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0428 -12.3661 9.2914
REMARK 3 T TENSOR
REMARK 3 T11: 0.0703 T22: 0.0368
REMARK 3 T33: 0.0070 T12: -0.0065
REMARK 3 T13: -0.0035 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.0419 L22: -0.1887
REMARK 3 L33: 1.6956 L12: -0.0177
REMARK 3 L13: 0.7330 L23: 0.0441
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: -0.0331 S13: -0.1269
REMARK 3 S21: 0.0275 S22: 0.0289 S23: 0.0074
REMARK 3 S31: -0.0428 S32: -0.0962 S33: -0.0626
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 239:256)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4473 -15.7957 3.1508
REMARK 3 T TENSOR
REMARK 3 T11: 0.0857 T22: 0.0875
REMARK 3 T33: 0.0791 T12: -0.0273
REMARK 3 T13: 0.0139 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.7238 L22: -0.2019
REMARK 3 L33: 0.8145 L12: 0.0304
REMARK 3 L13: -0.3652 L23: 0.0877
REMARK 3 S TENSOR
REMARK 3 S11: 0.0132 S12: 0.0044 S13: -0.1347
REMARK 3 S21: -0.0091 S22: -0.0072 S23: -0.0676
REMARK 3 S31: -0.0706 S32: 0.0080 S33: -0.0038
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 257:339)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2726 -0.4035 -2.7503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0561 T22: 0.0629
REMARK 3 T33: -0.0274 T12: 0.0013
REMARK 3 T13: -0.0066 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.2440 L22: 0.1657
REMARK 3 L33: -0.2251 L12: -0.0116
REMARK 3 L13: -0.0591 L23: -0.0720
REMARK 3 S TENSOR
REMARK 3 S11: 0.0172 S12: 0.0314 S13: -0.0120
REMARK 3 S21: -0.0243 S22: -0.0112 S23: 0.0108
REMARK 3 S31: -0.0367 S32: 0.0140 S33: -0.0017
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 340:362)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4976 7.9565 12.5073
REMARK 3 T TENSOR
REMARK 3 T11: 0.0614 T22: 0.0851
REMARK 3 T33: 0.0049 T12: 0.0049
REMARK 3 T13: 0.0292 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: -0.0007 L22: 0.1822
REMARK 3 L33: 0.1382 L12: 0.0283
REMARK 3 L13: 0.0364 L23: 0.0450
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: -0.0094 S13: 0.0072
REMARK 3 S21: 0.1216 S22: 0.0230 S23: 0.0384
REMARK 3 S31: -0.0673 S32: -0.1546 S33: -0.0303
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 3IAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52538
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 29.698
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.25100
REMARK 200 R SYM FOR SHELL (I) : 0.25100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: PDB ENTRY 1KRM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.20M NANO3, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 30.53500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.33000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.75500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.33000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.53500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.75500
REMARK 290 SMTRY3 4 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 4
REMARK 465 GLU A 365
REMARK 465 ASN A 366
REMARK 465 LEU A 367
REMARK 465 TYR A 368
REMARK 465 PHE A 369
REMARK 465 GLN A 370
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 GLU A 44 CD OE1 OE2
REMARK 470 GLN A 138 CD OE1 NE2
REMARK 470 GLU A 320 CD OE1 OE2
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 696 O HOH A 989 1.98
REMARK 500 O HOH A 458 O HOH A 697 2.04
REMARK 500 O HOH A 482 O HOH A 965 2.12
REMARK 500 O HOH A 792 O HOH A 1033 2.15
REMARK 500 O HOH A 433 O HOH A 946 2.16
REMARK 500 O HOH A 529 O HOH A 1044 2.17
REMARK 500 O HOH A 394 O HOH A 985 2.19
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 ASP A 8 45.54 -87.45
REMARK 500 LEU A 56 -119.16 -118.30
REMARK 500 THR A 176 -14.78 90.49
REMARK 500 HIS A 238 -86.13 75.15
REMARK 500 ASP A 295 -77.42 70.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 424 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH A 445 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 452 DISTANCE = 5.70 ANGSTROMS
REMARK 525 HOH A 466 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH A 474 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH A 487 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 498 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH A 550 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH A 552 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 582 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A 617 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 624 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH A 667 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 688 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 996 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A1029 DISTANCE = 5.51 ANGSTROMS
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 NI A 1 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 15 NE2
REMARK 620 2 HIS A 17 NE2 110.4
REMARK 620 3 HIS A 214 NE2 88.9 94.5
REMARK 620 4 ASP A 295 OD1 87.7 92.8 172.7
REMARK 620 5 3D1 A 501 N6 128.1 121.4 90.6 86.4
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 3D1 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 371
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 372
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KRM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOVINE ADENOSINE DEAMINASE COMPLEXED
REMARK 900 WITH 6-HYDROXYL-1,6-DIHYDROPURINE RIBOSIDE
DBREF 3IAR A 5 363 UNP P00813 ADA_HUMAN 5 363
SEQADV 3IAR MET A 4 UNP P00813 INITIATING METHIONINE
SEQADV 3IAR ALA A 364 UNP P00813 EXPRESSION TAG
SEQADV 3IAR GLU A 365 UNP P00813 EXPRESSION TAG
SEQADV 3IAR ASN A 366 UNP P00813 EXPRESSION TAG
SEQADV 3IAR LEU A 367 UNP P00813 EXPRESSION TAG
SEQADV 3IAR TYR A 368 UNP P00813 EXPRESSION TAG
SEQADV 3IAR PHE A 369 UNP P00813 EXPRESSION TAG
SEQADV 3IAR GLN A 370 UNP P00813 EXPRESSION TAG
SEQRES 1 A 367 MET PRO ALA PHE ASP LYS PRO LYS VAL GLU LEU HIS VAL
SEQRES 2 A 367 HIS LEU ASP GLY SER ILE LYS PRO GLU THR ILE LEU TYR
SEQRES 3 A 367 TYR GLY ARG ARG ARG GLY ILE ALA LEU PRO ALA ASN THR
SEQRES 4 A 367 ALA GLU GLY LEU LEU ASN VAL ILE GLY MET ASP LYS PRO
SEQRES 5 A 367 LEU THR LEU PRO ASP PHE LEU ALA LYS PHE ASP TYR TYR
SEQRES 6 A 367 MET PRO ALA ILE ALA GLY CYS ARG GLU ALA ILE LYS ARG
SEQRES 7 A 367 ILE ALA TYR GLU PHE VAL GLU MET LYS ALA LYS GLU GLY
SEQRES 8 A 367 VAL VAL TYR VAL GLU VAL ARG TYR SER PRO HIS LEU LEU
SEQRES 9 A 367 ALA ASN SER LYS VAL GLU PRO ILE PRO TRP ASN GLN ALA
SEQRES 10 A 367 GLU GLY ASP LEU THR PRO ASP GLU VAL VAL ALA LEU VAL
SEQRES 11 A 367 GLY GLN GLY LEU GLN GLU GLY GLU ARG ASP PHE GLY VAL
SEQRES 12 A 367 LYS ALA ARG SER ILE LEU CYS CYS MET ARG HIS GLN PRO
SEQRES 13 A 367 ASN TRP SER PRO LYS VAL VAL GLU LEU CYS LYS LYS TYR
SEQRES 14 A 367 GLN GLN GLN THR VAL VAL ALA ILE ASP LEU ALA GLY ASP
SEQRES 15 A 367 GLU THR ILE PRO GLY SER SER LEU LEU PRO GLY HIS VAL
SEQRES 16 A 367 GLN ALA TYR GLN GLU ALA VAL LYS SER GLY ILE HIS ARG
SEQRES 17 A 367 THR VAL HIS ALA GLY GLU VAL GLY SER ALA GLU VAL VAL
SEQRES 18 A 367 LYS GLU ALA VAL ASP ILE LEU LYS THR GLU ARG LEU GLY
SEQRES 19 A 367 HIS GLY TYR HIS THR LEU GLU ASP GLN ALA LEU TYR ASN
SEQRES 20 A 367 ARG LEU ARG GLN GLU ASN MET HIS PHE GLU ILE CYS PRO
SEQRES 21 A 367 TRP SER SER TYR LEU THR GLY ALA TRP LYS PRO ASP THR
SEQRES 22 A 367 GLU HIS ALA VAL ILE ARG LEU LYS ASN ASP GLN ALA ASN
SEQRES 23 A 367 TYR SER LEU ASN THR ASP ASP PRO LEU ILE PHE LYS SER
SEQRES 24 A 367 THR LEU ASP THR ASP TYR GLN MET THR LYS ARG ASP MET
SEQRES 25 A 367 GLY PHE THR GLU GLU GLU PHE LYS ARG LEU ASN ILE ASN
SEQRES 26 A 367 ALA ALA LYS SER SER PHE LEU PRO GLU ASP GLU LYS ARG
SEQRES 27 A 367 GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR GLY MET PRO
SEQRES 28 A 367 PRO SER ALA SER ALA GLY GLN ASN LEU ALA GLU ASN LEU
SEQRES 29 A 367 TYR PHE GLN
HET 3D1 A 501 18
HET NI A 1 1
HET NO3 A 371 4
HET NO3 A 2 4
HET GOL A 372 6
HETNAM 3D1 (2R,3S,5R)-5-(6-AMINO-9H-PURIN-9-YL)-TETRAHYDRO-2-
HETNAM 2 3D1 (HYDROXYMETHYL)FURAN-3-OL
HETNAM NI NICKEL (II) ION
HETNAM NO3 NITRATE ION
HETNAM GOL GLYCEROL
HETSYN 3D1 2'-DEOXYADENOSINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 3D1 C10 H13 N5 O3
FORMUL 3 NI NI 2+
FORMUL 4 NO3 2(N O3 1-)
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *691(H2 O)
HELIX 1 1 HIS A 17 SER A 21 5 5
HELIX 2 2 LYS A 23 GLY A 35 1 13
HELIX 3 3 THR A 42 GLY A 51 1 10
HELIX 4 4 THR A 57 ALA A 63 1 7
HELIX 5 5 LYS A 64 TYR A 67 5 4
HELIX 6 6 TYR A 68 ALA A 73 1 6
HELIX 7 7 CYS A 75 LYS A 92 1 18
HELIX 8 8 SER A 103 ALA A 108 5 6
HELIX 9 9 ILE A 115 GLN A 119 5 5
HELIX 10 10 THR A 125 GLY A 145 1 21
HELIX 11 11 GLN A 158 ASN A 160 5 3
HELIX 12 12 TRP A 161 TYR A 172 1 12
HELIX 13 13 GLY A 190 LEU A 193 5 4
HELIX 14 14 LEU A 194 GLY A 208 1 15
HELIX 15 15 SER A 220 ILE A 230 1 11
HELIX 16 16 TYR A 240 GLU A 244 5 5
HELIX 17 17 ASP A 245 GLU A 255 1 11
HELIX 18 18 CYS A 262 THR A 269 1 8
HELIX 19 19 HIS A 278 ASP A 286 1 9
HELIX 20 20 ASP A 296 LYS A 301 1 6
HELIX 21 21 THR A 303 GLY A 316 1 14
HELIX 22 22 THR A 318 SER A 332 1 15
HELIX 23 23 PRO A 336 GLY A 352 1 17
HELIX 24 24 PRO A 354 LEU A 363 1 10
SHEET 1 A 8 LYS A 11 GLU A 13 0
SHEET 2 A 8 VAL A 95 TYR A 102 1 O VAL A 96 N LYS A 11
SHEET 3 A 8 LYS A 147 MET A 155 1 O CYS A 153 N TYR A 102
SHEET 4 A 8 VAL A 177 ALA A 183 1 O ASP A 181 N CYS A 154
SHEET 5 A 8 HIS A 210 ALA A 215 1 O HIS A 214 N LEU A 182
SHEET 6 A 8 ARG A 235 HIS A 238 1 O GLY A 237 N VAL A 213
SHEET 7 A 8 HIS A 258 ILE A 261 1 O GLU A 260 N LEU A 236
SHEET 8 A 8 TYR A 290 LEU A 292 1 O SER A 291 N PHE A 259
LINK NE2 HIS A 15 NI NI A 1 1555 1555 2.10
LINK NE2 HIS A 17 NI NI A 1 1555 1555 2.04
LINK NE2 HIS A 214 NI NI A 1 1555 1555 2.21
LINK OD1 ASP A 295 NI NI A 1 1555 1555 2.12
LINK N6 3D1 A 501 NI NI A 1 1555 1555 2.15
CISPEP 1 GLU A 113 PRO A 114 0 -4.56
SITE 1 AC1 14 NI A 1 HIS A 17 ASP A 19 LEU A 62
SITE 2 AC1 14 PHE A 65 LEU A 106 GLY A 184 HIS A 214
SITE 3 AC1 14 GLU A 217 HIS A 238 ASP A 295 ASP A 296
SITE 4 AC1 14 HOH A 781 HOH A 814
SITE 1 AC2 5 HIS A 15 HIS A 17 HIS A 214 ASP A 295
SITE 2 AC2 5 3D1 A 501
SITE 1 AC3 7 LYS A 111 THR A 125 PRO A 126 ASP A 127
SITE 2 AC3 7 LYS A 164 HOH A 727 HOH A1058
SITE 1 AC4 10 PRO A 5 PHE A 7 ASP A 8 LYS A 11
SITE 2 AC4 10 TYR A 29 ARG A 33 GLU A 93 ASP A 305
SITE 3 AC4 10 HOH A 702 HOH A 827
SITE 1 AC5 8 PRO A 116 TRP A 117 HIS A 157 HOH A 397
SITE 2 AC5 8 HOH A 485 HOH A 613 HOH A 795 HOH A 797
CRYST1 61.070 73.510 76.660 90.00 90.00 90.00 P 21 21 21 4
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 0.016375 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013604 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013045 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
