HEADER HYDROLASE 16-OCT-11 3U8B
TITLE FUNCTIONALLY SELECTIVE INHIBITION OF GROUP IIA PHOSPHOLIPASE A2
TITLE 2 REVEALS A ROLE FOR VIMENTIN IN REGULATING ARACHIDONIC ACID METABOLISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE A2, MEMBRANE ASSOCIATED;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GIIC SPLA2, GROUP IIA PHOSPHOLIPASE A2, NON-PANCREATIC
COMPND 5 SECRETORY PHOSPHOLIPASE A2, NPS-PLA2, PHOSPHATIDYLCHOLINE 2-
COMPND 6 ACYLHYDROLASE 2A;
COMPND 7 EC: 3.1.1.4;
COMPND 8 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: PLA2G2A, PLA2B, PLA2L, RASF-A;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS SECRETED PHOSPHOLIPASE A2, PHOSPHOLIPASE A2 ACTIVITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.K.LEE,K.J.BRYANT,R.BOUVERET,P.-W.LEI,A.P.DUFF,S.J.HARROP,E.P.HUANG,
AUTHOR 2 R.P.HARVEY,M.H.GELB,P.P.GRAY,P.M.CURMI,A.M.CUNNINGHAM,W.B.CHURCH,
AUTHOR 3 K.F.SCOTT
REVDAT 2 12-JUN-13 3U8B 1 JRNL
REVDAT 1 17-OCT-12 3U8B 0
JRNL AUTH L.K.LEE,K.J.BRYANT,R.BOUVERET,P.W.LEI,A.P.DUFF,S.J.HARROP,
JRNL AUTH 2 E.P.HUANG,R.P.HARVEY,M.H.GELB,P.P.GRAY,P.M.CURMI,
JRNL AUTH 3 A.M.CUNNINGHAM,W.B.CHURCH,K.F.SCOTT
JRNL TITL SELECTIVE INHIBITION OF HUMAN GROUP IIA-SECRETED
JRNL TITL 2 PHOSPHOLIPASE A2 (HGIIA) SIGNALING REVEALS ARACHIDONIC ACID
JRNL TITL 3 METABOLISM IS ASSOCIATED WITH COLOCALIZATION OF HGIIA TO
JRNL TITL 4 VIMENTIN IN RHEUMATOID SYNOVIOCYTES.
JRNL REF J.BIOL.CHEM. V. 288 15269 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23482564
JRNL DOI 10.1074/JBC.M112.397893
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 6906
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.620
REMARK 3 FREE R VALUE TEST SET COUNT : 319
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 2.8958 - 2.2990 1.00 3233 157 0.2639 0.3082
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.65
REMARK 3 K_SOL : 0.43
REMARK 3 B_SOL : 56.02
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.600
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.020
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) : 1.64250
REMARK 3 B22 (A**2) : 1.64250
REMARK 3 B33 (A**2) : -3.28500
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.018 1002
REMARK 3 ANGLE : 1.765 1339
REMARK 3 CHIRALITY : 0.096 134
REMARK 3 PLANARITY : 0.011 170
REMARK 3 DIHEDRAL : 11.553 370
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 1:31)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9294 35.4618 0.1399
REMARK 3 T TENSOR
REMARK 3 T11: 0.4721 T22: 0.4924
REMARK 3 T33: 0.4605 T12: 0.0223
REMARK 3 T13: 0.0304 T23: -0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 3.4437 L22: 1.4812
REMARK 3 L33: 3.0599 L12: 0.8114
REMARK 3 L13: -0.8019 L23: 0.0836
REMARK 3 S TENSOR
REMARK 3 S11: 0.3005 S12: -0.0910 S13: 0.4104
REMARK 3 S21: 0.1059 S22: -0.1917 S23: 0.1948
REMARK 3 S31: 0.1835 S32: 0.1824 S33: -0.0846
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 32:104)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9330 28.8354 -7.4524
REMARK 3 T TENSOR
REMARK 3 T11: 0.4290 T22: 0.5372
REMARK 3 T33: 0.4173 T12: -0.0371
REMARK 3 T13: 0.0311 T23: -0.0787
REMARK 3 L TENSOR
REMARK 3 L11: 4.9972 L22: 2.8668
REMARK 3 L33: 4.4858 L12: 1.2205
REMARK 3 L13: -0.8085 L23: 0.9888
REMARK 3 S TENSOR
REMARK 3 S11: -0.2315 S12: 0.5347 S13: 0.0146
REMARK 3 S21: -0.1360 S22: 0.2666 S23: -0.2546
REMARK 3 S31: 0.2811 S32: -0.0729 S33: -0.0152
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 105:124)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5348 33.7941 1.0355
REMARK 3 T TENSOR
REMARK 3 T11: 0.4734 T22: 0.8196
REMARK 3 T33: 0.6189 T12: 0.0799
REMARK 3 T13: 0.0282 T23: -0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 2.0859 L22: 2.1300
REMARK 3 L33: 1.7189 L12: 0.1495
REMARK 3 L13: -0.0616 L23: 0.4469
REMARK 3 S TENSOR
REMARK 3 S11: 0.2611 S12: 0.3266 S13: 0.1088
REMARK 3 S21: -0.3293 S22: -0.7016 S23: 0.7157
REMARK 3 S31: -0.1159 S32: -0.9177 S33: 0.3553
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 3U8B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB068432.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90020
REMARK 200 MONOCHROMATOR : BENT GE(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6906
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.299
REMARK 200 RESOLUTION RANGE LOW (A) : 24.446
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL PH 7.4, 10 MM CACL2,
REMARK 280 0.5 MM BETA-OCTYL GLUCOSIDE AND 4 M NACL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.71967
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 59.43933
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.57950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 74.29917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 14.85983
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 29.71967
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 59.43933
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 74.29917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 44.57950
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 14.85983
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL
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 BIOMT1 2 0.500000 0.866025 0.000000 -37.34150
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 64.67738
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 14.85983
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 56 CG CD CE NZ
REMARK 480 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 74 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 79 CG CD CE
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 48 CB - CG - OD1 ANGL. DEV. = 7.1 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 33 145.14 -171.37
REMARK 500 THR A 61 -87.61 -135.62
REMARK 500 TYR A 111 57.13 -112.18
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 CA A 126 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 152 O
REMARK 620 2 TYR A 112 O 100.9
REMARK 620 3 ASN A 114 OD1 91.4 94.9
REMARK 620 4 HOH A 134 O 90.2 167.6 90.1
REMARK 620 5 GLY A 25 O 164.7 93.5 82.4 75.9
REMARK 620 6 PHE A 23 O 88.7 93.5 171.4 81.3 95.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 127 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 48 OD2
REMARK 620 2 GLY A 29 O 174.3
REMARK 620 3 HIS A 27 O 91.1 93.2
REMARK 620 4 GLY A 31 O 93.1 91.0 86.1
REMARK 620 5 ASP A 48 OD1 55.3 119.3 114.2 140.6
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 CL A 125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 127
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 128
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U8D RELATED DB: PDB
REMARK 900 RELATED ID: 3U8H RELATED DB: PDB
REMARK 900 RELATED ID: 3U8I RELATED DB: PDB
DBREF 3U8B A 1 124 UNP P14555 PA2GA_HUMAN 21 144
SEQRES 1 A 124 ASN LEU VAL ASN PHE HIS ARG MET ILE LYS LEU THR THR
SEQRES 2 A 124 GLY LYS GLU ALA ALA LEU SER TYR GLY PHE TYR GLY CYS
SEQRES 3 A 124 HIS CYS GLY VAL GLY GLY ARG GLY SER PRO LYS ASP ALA
SEQRES 4 A 124 THR ASP ARG CYS CYS VAL THR HIS ASP CYS CYS TYR LYS
SEQRES 5 A 124 ARG LEU GLU LYS ARG GLY CYS GLY THR LYS PHE LEU SER
SEQRES 6 A 124 TYR LYS PHE SER ASN SER GLY SER ARG ILE THR CYS ALA
SEQRES 7 A 124 LYS GLN ASP SER CYS ARG SER GLN LEU CYS GLU CYS ASP
SEQRES 8 A 124 LYS ALA ALA ALA THR CYS PHE ALA ARG ASN LYS THR THR
SEQRES 9 A 124 TYR ASN LYS LYS TYR GLN TYR TYR SER ASN LYS HIS CYS
SEQRES 10 A 124 ARG GLY SER THR PRO ARG CYS
HET CL A 125 1
HET CA A 126 1
HET CA A 127 1
HET CL A 128 1
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
FORMUL 2 CL 2(CL 1-)
FORMUL 3 CA 2(CA 2+)
FORMUL 6 HOH *53(H2 O)
HELIX 1 1 ASN A 1 GLY A 14 1 14
HELIX 2 2 GLU A 16 GLY A 22 1 7
HELIX 3 3 ASP A 38 ARG A 57 1 20
HELIX 4 4 ASP A 81 ASN A 101 1 21
HELIX 5 5 LYS A 102 TYR A 105 5 4
HELIX 6 6 ASN A 106 TYR A 111 1 6
HELIX 7 7 SER A 113 CYS A 117 5 5
SHEET 1 A 2 PHE A 68 SER A 71 0
SHEET 2 A 2 ARG A 74 CYS A 77 -1 O THR A 76 N SER A 69
SSBOND 1 CYS A 26 CYS A 117 1555 1555 2.01
SSBOND 2 CYS A 28 CYS A 44 1555 1555 2.05
SSBOND 3 CYS A 43 CYS A 97 1555 1555 2.04
SSBOND 4 CYS A 49 CYS A 124 1555 1555 2.03
SSBOND 5 CYS A 50 CYS A 90 1555 1555 2.03
SSBOND 6 CYS A 59 CYS A 83 1555 1555 2.03
SSBOND 7 CYS A 77 CYS A 88 1555 1555 2.05
LINK CA CA A 126 O HOH A 152 1555 1555 2.17
LINK OD2 ASP A 48 CA CA A 127 1555 1555 2.24
LINK O TYR A 112 CA CA A 126 1555 1555 2.28
LINK O GLY A 29 CA CA A 127 1555 1555 2.28
LINK O HIS A 27 CA CA A 127 1555 1555 2.28
LINK OD1 ASN A 114 CA CA A 126 1555 1555 2.38
LINK CA CA A 126 O HOH A 134 1555 1555 2.38
LINK O GLY A 25 CA CA A 126 1555 1555 2.39
LINK O GLY A 31 CA CA A 127 1555 1555 2.40
LINK OD1 ASP A 48 CA CA A 127 1555 1555 2.44
LINK O PHE A 23 CA CA A 126 1555 1555 2.51
SITE 1 AC1 3 GLY A 32 ASN A 114 LYS A 115
SITE 1 AC2 6 PHE A 23 GLY A 25 TYR A 112 ASN A 114
SITE 2 AC2 6 HOH A 134 HOH A 152
SITE 1 AC3 4 HIS A 27 GLY A 29 GLY A 31 ASP A 48
SITE 1 AC4 3 ASN A 4 ARG A 7 ARG A 118
CRYST1 74.683 74.683 89.159 90.00 90.00 120.00 P 61 2 2 12
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 0.013390 0.007731 0.000000 0.00000
SCALE2 0.000000 0.015461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
