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HEADER HYDROLASE 29-JAN-25 9N2W
TITLE DIENELACTONE HYDROLASE FAMILY PROTEIN SADLH FROM SOLIMONAS AQUATICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLIMONAS AQUATICA;
SOURCE 3 ORGANISM_TAXID: 489703;
SOURCE 4 GENE: SAMN04488038_103247;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS SULFINIC ACID, DIENELACTONE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.D.F.SCHNETTLER FERNANDEZ,E.C.CAMPBELL,F.HOLLFELDER
REVDAT 1 18-FEB-26 9N2W 0
JRNL AUTH J.D.F.SCHNETTLER,E.C.CAMPBELL,R.KHASHIEV,J.O.KLEIN,
JRNL AUTH 2 F.HOLLFELDER
JRNL TITL METAL-INDEPENDENT ORGANOPHOSPHATE HYDROLYSIS IN A PROTEIN
JRNL TITL 2 FAMILY POSSESSING A CATALYTIC TRIAD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 41834
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2110
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 69.0000 - 4.6900 0.98 2804 147 0.1923 0.2409
REMARK 3 2 4.6900 - 3.7200 0.96 2711 140 0.1812 0.2414
REMARK 3 3 3.7200 - 3.2500 0.95 2631 146 0.2218 0.2801
REMARK 3 4 3.2500 - 2.9500 0.98 2715 129 0.2499 0.2595
REMARK 3 5 2.9500 - 2.7400 0.98 2732 132 0.2581 0.3000
REMARK 3 6 2.7400 - 2.5800 0.98 2723 128 0.2363 0.3500
REMARK 3 7 2.5800 - 2.4500 0.97 2674 132 0.2417 0.3246
REMARK 3 8 2.4500 - 2.3400 0.97 2696 134 0.2463 0.2666
REMARK 3 9 2.3400 - 2.2500 0.85 2368 135 0.2908 0.3145
REMARK 3 10 2.2500 - 2.1700 0.91 2484 158 0.3791 0.4924
REMARK 3 11 2.1700 - 2.1100 0.96 2594 181 0.2644 0.3597
REMARK 3 12 2.1100 - 2.0500 0.97 2680 142 0.2612 0.2966
REMARK 3 13 2.0500 - 1.9900 0.96 2633 128 0.2851 0.3345
REMARK 3 14 1.9900 - 1.9400 0.94 2615 142 0.3882 0.4559
REMARK 3 15 1.9400 - 1.9000 0.97 2664 136 0.4944 0.4859
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.017
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.02
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 : 0.008 3704
REMARK 3 ANGLE : 1.148 5030
REMARK 3 CHIRALITY : 0.055 546
REMARK 3 PLANARITY : 0.010 676
REMARK 3 DIHEDRAL : 8.035 530
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 9N2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-25.
REMARK 100 THE DEPOSITION ID IS D_1000292326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41834
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 69.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04279
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
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 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES 7.5 PH (BUFFER) 4.3 M NACL
REMARK 280 (PRECIPITANT), PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
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 38.20400
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 OD2 CSD B 119 O HOH B 301 2.17
REMARK 500 OD2 CSD A 119 CE1 HIS A 200 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 GLU A 67 19.23 59.28
REMARK 500 ALA A 110 -9.90 -57.23
REMARK 500 CSD A 119 -118.83 54.09
REMARK 500 CYS A 119 -112.35 53.81
REMARK 500 HIS A 142 54.96 37.64
REMARK 500 VAL A 199 -159.67 -114.84
REMARK 500 ALA B 25 142.24 -174.68
REMARK 500 THR B 26 130.54 -33.63
REMARK 500 CSD B 119 -115.49 50.21
REMARK 500 CYS B 119 -111.17 49.66
REMARK 500 HIS B 142 55.04 36.39
REMARK 500 GLN B 154 28.09 34.75
REMARK 500 VAL B 199 -149.49 -116.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7JIZ RELATED DB: PDB
REMARK 900 RELATED ID: 8VB3 RELATED DB: PDB
REMARK 900 RELATED ID: 7JKA RELATED DB: PDB
DBREF1 9N2W A 1 237 UNP A0A1H9CZH3_9GAMM
DBREF2 9N2W A A0A1H9CZH3 1 237
DBREF1 9N2W B 1 237 UNP A0A1H9CZH3_9GAMM
DBREF2 9N2W B A0A1H9CZH3 1 237
SEQRES 1 A 237 MET LYS SER GLN GLN VAL VAL TYR ARG GLY ALA GLY ARG
SEQRES 2 A 237 ARG PHE LEU GLY GLU LEU TYR TRP ASP GLU ALA ALA THR
SEQRES 3 A 237 GLN PRO ALA PRO GLY VAL LEU VAL PHE PRO ASP ALA PHE
SEQRES 4 A 237 GLY LEU ALA ASP HIS ALA ARG GLU ARG ALA GLN ARG LEU
SEQRES 5 A 237 ALA GLN LEU GLY TYR VAL ALA LEU ALA ALA ASP LEU HIS
SEQRES 6 A 237 GLY GLU GLY ALA VAL TYR GLU ASP VAL ALA SER MET ARG
SEQRES 7 A 237 VAL HIS LEU GLN PRO LEU PHE GLU ASN ARG ALA ASP TRP
SEQRES 8 A 237 ARG ALA ARG ALA GLN ALA ALA LEU ALA ALA LEU GLN ALA
SEQRES 9 A 237 GLN THR PRO VAL ASP ALA GLN ARG LEU ALA ALA ILE GLY
SEQRES 10 A 237 PHE CSD LEU GLY GLY ALA THR CYS LEU GLU LEU ALA ARG
SEQRES 11 A 237 CYS GLY ALA PRO LEU LYS ALA ILE VAL GLY PHE HIS ALA
SEQRES 12 A 237 GLY VAL LEU ALA PRO LEU PRO GLY ASP GLU GLN LYS ILE
SEQRES 13 A 237 GLN ALA LYS VAL LEU LEU CYS GLN GLY ALA ASP ASP PRO
SEQRES 14 A 237 LEU ILE LYS LYS GLU ASN MET ALA ALA VAL GLU ALA GLU
SEQRES 15 A 237 LEU ARG ARG ASP ARG VAL ASP TRP GLN LEU ILE VAL TYR
SEQRES 16 A 237 GLY ASN ALA VAL HIS SER PHE THR ASN ARG ASP ALA ALA
SEQRES 17 A 237 THR ARG GLN SER PRO ALA MET ALA TYR ASP ALA ALA ALA
SEQRES 18 A 237 ASP ARG ARG SER TRP ALA ALA MET GLN GLY LEU LEU ALA
SEQRES 19 A 237 GLU VAL PHE
SEQRES 1 B 237 MET LYS SER GLN GLN VAL VAL TYR ARG GLY ALA GLY ARG
SEQRES 2 B 237 ARG PHE LEU GLY GLU LEU TYR TRP ASP GLU ALA ALA THR
SEQRES 3 B 237 GLN PRO ALA PRO GLY VAL LEU VAL PHE PRO ASP ALA PHE
SEQRES 4 B 237 GLY LEU ALA ASP HIS ALA ARG GLU ARG ALA GLN ARG LEU
SEQRES 5 B 237 ALA GLN LEU GLY TYR VAL ALA LEU ALA ALA ASP LEU HIS
SEQRES 6 B 237 GLY GLU GLY ALA VAL TYR GLU ASP VAL ALA SER MET ARG
SEQRES 7 B 237 VAL HIS LEU GLN PRO LEU PHE GLU ASN ARG ALA ASP TRP
SEQRES 8 B 237 ARG ALA ARG ALA GLN ALA ALA LEU ALA ALA LEU GLN ALA
SEQRES 9 B 237 GLN THR PRO VAL ASP ALA GLN ARG LEU ALA ALA ILE GLY
SEQRES 10 B 237 PHE CSD LEU GLY GLY ALA THR CYS LEU GLU LEU ALA ARG
SEQRES 11 B 237 CYS GLY ALA PRO LEU LYS ALA ILE VAL GLY PHE HIS ALA
SEQRES 12 B 237 GLY VAL LEU ALA PRO LEU PRO GLY ASP GLU GLN LYS ILE
SEQRES 13 B 237 GLN ALA LYS VAL LEU LEU CYS GLN GLY ALA ASP ASP PRO
SEQRES 14 B 237 LEU ILE LYS LYS GLU ASN MET ALA ALA VAL GLU ALA GLU
SEQRES 15 B 237 LEU ARG ARG ASP ARG VAL ASP TRP GLN LEU ILE VAL TYR
SEQRES 16 B 237 GLY ASN ALA VAL HIS SER PHE THR ASN ARG ASP ALA ALA
SEQRES 17 B 237 THR ARG GLN SER PRO ALA MET ALA TYR ASP ALA ALA ALA
SEQRES 18 B 237 ASP ARG ARG SER TRP ALA ALA MET GLN GLY LEU LEU ALA
SEQRES 19 B 237 GLU VAL PHE
MODRES 9N2W CSD A 119 CYS MODIFIED RESIDUE
MODRES 9N2W CSD B 119 CYS MODIFIED RESIDUE
HET CSD A 119 8
HET CSD B 119 8
HETNAM CSD 3-SULFINOALANINE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 HOH *142(H2 O)
HELIX 1 AA1 ALA A 42 LEU A 55 1 14
HELIX 2 AA2 ASP A 73 ASN A 87 1 15
HELIX 3 AA3 ASN A 87 ALA A 104 1 18
HELIX 4 AA4 CSD A 119 ARG A 130 1 12
HELIX 5 AA5 LYS A 172 ASP A 186 1 15
HELIX 6 AA6 ASP A 206 GLN A 211 5 6
HELIX 7 AA7 ASP A 218 PHE A 237 1 20
HELIX 8 AA8 ALA B 42 LEU B 55 1 14
HELIX 9 AA9 ASP B 73 ARG B 78 1 6
HELIX 10 AB1 LEU B 81 ASN B 87 1 7
HELIX 11 AB2 ASN B 87 ALA B 104 1 18
HELIX 12 AB3 CSD B 119 ARG B 130 1 12
HELIX 13 AB4 LYS B 172 ARG B 187 1 16
HELIX 14 AB5 ASP B 206 GLN B 211 5 6
HELIX 15 AB6 ASP B 218 PHE B 237 1 20
SHEET 1 AA116 LYS A 2 GLY A 10 0
SHEET 2 AA116 ARG A 13 TRP A 21 -1 O PHE A 15 N TYR A 8
SHEET 3 AA116 VAL A 58 ALA A 61 -1 O ALA A 59 N TYR A 20
SHEET 4 AA116 ALA A 29 PHE A 35 1 N PRO A 30 O VAL A 58
SHEET 5 AA116 VAL A 108 PHE A 118 1 O ASP A 109 N ALA A 29
SHEET 6 AA116 ALA A 137 PHE A 141 1 O PHE A 141 N GLY A 117
SHEET 7 AA116 LYS A 159 GLY A 165 1 O CYS A 163 N GLY A 140
SHEET 8 AA116 TRP A 190 TYR A 195 1 O ILE A 193 N LEU A 162
SHEET 9 AA116 TRP B 190 TYR B 195 -1 O LEU B 192 N VAL A 194
SHEET 10 AA116 LYS B 159 GLY B 165 1 N LEU B 162 O ILE B 193
SHEET 11 AA116 ALA B 137 PHE B 141 1 N GLY B 140 O CYS B 163
SHEET 12 AA116 VAL B 108 PHE B 118 1 N GLY B 117 O PHE B 141
SHEET 13 AA116 ALA B 29 PHE B 35 1 N ALA B 29 O ASP B 109
SHEET 14 AA116 VAL B 58 ALA B 61 1 O VAL B 58 N PRO B 30
SHEET 15 AA116 ARG B 13 TRP B 21 -1 N GLU B 18 O ALA B 61
SHEET 16 AA116 LYS B 2 GLY B 10 -1 N GLY B 10 O ARG B 13
LINK C PHE A 118 N ACSD A 119 1555 1555 1.34
LINK C ACSD A 119 N LEU A 120 1555 1555 1.33
LINK OD2ACSD A 119 NE2 HIS A 200 1555 1555 1.34
LINK C PHE B 118 N ACSD B 119 1555 1555 1.34
LINK C ACSD B 119 N LEU B 120 1555 1555 1.33
CRYST1 53.446 76.408 72.459 90.00 107.77 90.00 P 1 21 1 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 0.018710 0.000000 0.005996 0.00000
SCALE2 0.000000 0.013088 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014492 0.00000
TER 1816 PHE A 237
TER 3632 PHE B 237
MASTER 240 0 2 15 16 0 0 6 3772 2 21 38
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