HEADER ANTIMICROBIAL PROTEIN 19-SEP-13 4MTH
TITLE CRYSTAL STRUCTURE OF MATURE HUMAN REGIIIALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGENERATING ISLET-DERIVED PROTEIN 3-ALPHA 15 KDA FORM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: REG-3-ALPHA, HEPATOINTESTINAL PANCREATIC PROTEIN, HIP/PAP,
COMPND 5 HUMAN PROISLET PEPTIDE, PANCREATITIS-ASSOCIATED PROTEIN 1,
COMPND 6 REGENERATING ISLET-DERIVED PROTEIN III-ALPHA, REG III-ALPHA;
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: HIP, PAP, PAP1, REG3A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 3(A)
KEYWDS HIP/PAP, REGIII-GAMMA, C-TYPE LECTIN, ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.DEREBE
REVDAT 3 15-NOV-17 4MTH 1 REMARK
REVDAT 2 25-DEC-13 4MTH 1 JRNL
REVDAT 1 27-NOV-13 4MTH 0
JRNL AUTH S.MUKHERJEE,H.ZHENG,M.G.DEREBE,K.M.CALLENBERG,C.L.PARTCH,
JRNL AUTH 2 D.ROLLINS,D.C.PROPHETER,J.RIZO,M.GRABE,Q.X.JIANG,L.V.HOOPER
JRNL TITL ANTIBACTERIAL MEMBRANE ATTACK BY A PORE-FORMING INTESTINAL
JRNL TITL 2 C-TYPE LECTIN.
JRNL REF NATURE V. 505 103 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 24256734
JRNL DOI 10.1038/NATURE12729
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.1_357
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) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.130
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 23163
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1876
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 26.1359 - 3.1665 0.99 2414 214 0.1830 0.1998
REMARK 3 2 3.1665 - 2.5140 0.99 2290 201 0.1884 0.2275
REMARK 3 3 2.5140 - 2.1964 0.98 2236 200 0.1899 0.2019
REMARK 3 4 2.1964 - 1.9957 0.99 2236 201 0.1693 0.1915
REMARK 3 5 1.9957 - 1.8527 0.96 2162 191 0.1653 0.2070
REMARK 3 6 1.8527 - 1.7435 0.95 2113 184 0.1770 0.1898
REMARK 3 7 1.7435 - 1.6562 0.92 2058 183 0.1719 0.2317
REMARK 3 8 1.6562 - 1.5841 0.90 1998 174 0.1851 0.2167
REMARK 3 9 1.5841 - 1.5231 0.88 1978 169 0.1965 0.2385
REMARK 3 10 1.5231 - 1.4710 0.81 1802 159 0.2185 0.2621
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 : 0.40
REMARK 3 B_SOL : 60.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.01530
REMARK 3 B22 (A**2) : 3.49740
REMARK 3 B33 (A**2) : -0.48210
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 : 0.006 NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4MTH 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_1000082344.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24610
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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 : 2.3000
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 (%): 45.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 8000, 0.1M MES PH 6.0, 0.1M
REMARK 280 NACL, 10MM NAAC, 5% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 15.38100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.07600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.76400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.07600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 15.38100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.76400
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 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 OE2 GLU A 134 O HOH A 454 2.17
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 MET A 37 CA - C - N ANGL. DEV. = 15.2 DEGREES
REMARK 500 MET A 37 O - C - N ANGL. DEV. = -18.3 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 ILE A 38 106.21 53.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 MET A 37 -12.19
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 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 444 O
REMARK 620 2 HOH A 354 O 88.6
REMARK 620 3 HOH A 473 O 74.1 162.7
REMARK 620 4 HOH A 413 O 125.1 134.9 59.3
REMARK 620 5 HOH A 447 O 99.9 98.3 85.1 103.2
REMARK 620 6 HOH A 318 O 159.9 99.5 97.0 59.8 60.9
REMARK 620 7 HIS A 50 NE2 93.7 91.4 89.6 60.8 163.4 104.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 335 O
REMARK 620 2 GLU A 121 OE1 105.7
REMARK 620 3 HIS A 107 NE2 112.3 115.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 465 O
REMARK 620 2 HOH A 469 O 138.9
REMARK 620 3 HIS A 145 NE2 97.0 90.3
REMARK 620 N 1 2
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 203
DBREF 4MTH A 38 175 UNP Q06141 REG3A_HUMAN 38 175
SEQADV 4MTH MET A 37 UNP Q06141 INITIATING METHIONINE
SEQRES 1 A 139 MET ILE ARG CYS PRO LYS GLY SER LYS ALA TYR GLY SER
SEQRES 2 A 139 HIS CYS TYR ALA LEU PHE LEU SER PRO LYS SER TRP THR
SEQRES 3 A 139 ASP ALA ASP LEU ALA CYS GLN LYS ARG PRO SER GLY ASN
SEQRES 4 A 139 LEU VAL SER VAL LEU SER GLY ALA GLU GLY SER PHE VAL
SEQRES 5 A 139 SER SER LEU VAL LYS SER ILE GLY ASN SER TYR SER TYR
SEQRES 6 A 139 VAL TRP ILE GLY LEU HIS ASP PRO THR GLN GLY THR GLU
SEQRES 7 A 139 PRO ASN GLY GLU GLY TRP GLU TRP SER SER SER ASP VAL
SEQRES 8 A 139 MET ASN TYR PHE ALA TRP GLU ARG ASN PRO SER THR ILE
SEQRES 9 A 139 SER SER PRO GLY HIS CYS ALA SER LEU SER ARG SER THR
SEQRES 10 A 139 ALA PHE LEU ARG TRP LYS ASP TYR ASN CYS ASN VAL ARG
SEQRES 11 A 139 LEU PRO TYR VAL CYS LYS PHE THR ASP
HET ZN A 201 1
HET ZN A 202 1
HET ZN A 203 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
FORMUL 5 HOH *181(H2 O)
HELIX 1 1 SER A 60 GLN A 69 1 10
HELIX 2 2 SER A 81 LYS A 93 1 13
HELIX 3 3 ASN A 136 ILE A 140 5 5
HELIX 4 4 SER A 152 ALA A 154 5 3
SHEET 1 A 4 LYS A 45 TYR A 47 0
SHEET 2 A 4 HIS A 50 LYS A 59 -1 O TYR A 52 N LYS A 45
SHEET 3 A 4 LEU A 167 PHE A 173 -1 O TYR A 169 N PHE A 55
SHEET 4 A 4 ASN A 75 LEU A 76 -1 N ASN A 75 O LYS A 172
SHEET 1 B 4 GLU A 121 TRP A 122 0
SHEET 2 B 4 TYR A 101 HIS A 107 -1 N HIS A 107 O GLU A 121
SHEET 3 B 4 CYS A 146 SER A 150 -1 O LEU A 149 N VAL A 102
SHEET 4 B 4 TRP A 158 TYR A 161 -1 O LYS A 159 N SER A 148
SSBOND 1 CYS A 40 CYS A 51 1555 1555 2.04
SSBOND 2 CYS A 68 CYS A 171 1555 1555 2.03
SSBOND 3 CYS A 146 CYS A 163 1555 1555 2.04
LINK ZN ZN A 202 O HOH A 444 1555 1555 2.11
LINK ZN ZN A 202 O HOH A 354 1555 1555 2.14
LINK ZN ZN A 201 O HOH A 335 1555 1555 2.24
LINK ZN ZN A 203 O HOH A 465 1555 1555 2.27
LINK ZN ZN A 202 O HOH A 473 1555 1555 2.29
LINK ZN ZN A 203 O HOH A 469 1555 1555 2.30
LINK ZN ZN A 202 O HOH A 413 1555 1555 2.38
LINK ZN ZN A 202 O HOH A 447 1555 1555 2.41
LINK ZN ZN A 202 O HOH A 318 1555 1555 2.49
LINK OE1 GLU A 121 ZN ZN A 201 1555 1555 1.96
LINK NE2 HIS A 107 ZN ZN A 201 1555 1555 2.03
LINK NE2 HIS A 145 ZN ZN A 203 1555 1555 2.11
LINK NE2 HIS A 50 ZN ZN A 202 1555 1555 2.32
SITE 1 AC1 4 HIS A 107 GLU A 121 ASP A 175 HOH A 335
SITE 1 AC2 7 HIS A 50 HOH A 318 HOH A 354 HOH A 413
SITE 2 AC2 7 HOH A 444 HOH A 447 HOH A 473
SITE 1 AC3 3 HIS A 145 HOH A 465 HOH A 469
CRYST1 30.762 49.528 92.152 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 0.032508 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020191 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010852 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
