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HEADER HYDROLASE 04-FEB-21 7NEI
TITLE NOVEL POLYESTER HYDROLASE LEIPZIG 7 (PHL-7)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL-7);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, CUTINASE, POLYETHYLENE TEREPHTHALATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.K.RICHTER,N.STRATER
REVDAT 1 23-JUN-21 7NEI 0
JRNL AUTH C.SONNENDECKER,J.OESER,P.K.RICHTER,P.HILLE,Z.ZHAO,C.FISCHER,
JRNL AUTH 2 H.LIPPOLD,P.BLAZQUEZ-SANCHEZ,F.ENGELBERGER,
JRNL AUTH 3 C.A.RAMIREZ-SARMIENTO,T.OESER,Y.LIHANOVA,R.FRANK,H.G.JAHNKE,
JRNL AUTH 4 S.BILLIG,B.ABEL,N.STRATER,J.MATYSIK,W.ZIMMERMANN
JRNL TITL LOW CARBON FOOTPRINT RECYCLING OF POST-CONSUMER PET PLASTIC
JRNL TITL 2 WITH A METAGENOMIC POLYESTER HYDROLASE.
JRNL REF CHEMSUSCHEM 2021
JRNL REFN ISSN 1864-564X
JRNL PMID 34129279
JRNL DOI 10.1002/CSSC.202101062
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2-3874
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 127577
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.133
REMARK 3 R VALUE (WORKING SET) : 0.132
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 6202
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 49.2200 - 4.0400 0.99 4617 264 0.1347 0.1456
REMARK 3 2 4.0400 - 3.2100 1.00 4491 235 0.1301 0.1681
REMARK 3 3 3.2100 - 2.8000 1.00 4448 181 0.1275 0.1499
REMARK 3 4 2.8000 - 2.5400 1.00 4411 242 0.1207 0.1273
REMARK 3 5 2.5400 - 2.3600 1.00 4400 199 0.1124 0.1513
REMARK 3 6 2.3600 - 2.2200 1.00 4396 203 0.1140 0.1369
REMARK 3 7 2.2200 - 2.1100 1.00 4335 274 0.1155 0.1374
REMARK 3 8 2.1100 - 2.0200 1.00 4319 234 0.1259 0.1520
REMARK 3 9 2.0200 - 1.9400 1.00 4334 222 0.1237 0.1483
REMARK 3 10 1.9400 - 1.8700 1.00 4345 229 0.1217 0.1579
REMARK 3 11 1.8700 - 1.8200 1.00 4334 238 0.1234 0.1638
REMARK 3 12 1.8200 - 1.7600 1.00 4341 236 0.1241 0.1524
REMARK 3 13 1.7600 - 1.7200 1.00 4358 203 0.1270 0.1781
REMARK 3 14 1.7200 - 1.6800 0.99 4313 228 0.1221 0.1417
REMARK 3 15 1.6800 - 1.6400 1.00 4325 237 0.1215 0.1617
REMARK 3 16 1.6400 - 1.6000 1.00 4370 195 0.1204 0.1480
REMARK 3 17 1.6000 - 1.5700 1.00 4314 224 0.1221 0.1579
REMARK 3 18 1.5700 - 1.5400 1.00 4302 209 0.1269 0.1724
REMARK 3 19 1.5400 - 1.5100 1.00 4288 242 0.1306 0.1652
REMARK 3 20 1.5100 - 1.4900 1.00 4329 217 0.1388 0.1844
REMARK 3 21 1.4900 - 1.4600 0.98 4231 206 0.1575 0.2150
REMARK 3 22 1.4600 - 1.4400 0.96 4168 198 0.1678 0.2141
REMARK 3 23 1.4400 - 1.4200 0.93 4029 184 0.1833 0.2346
REMARK 3 24 1.4200 - 1.4000 0.88 3810 202 0.2038 0.2319
REMARK 3 25 1.4000 - 1.3800 0.83 3588 166 0.2063 0.2652
REMARK 3 26 1.3800 - 1.3600 0.76 3310 133 0.2163 0.2663
REMARK 3 27 1.3600 - 1.3500 0.72 3118 161 0.2268 0.2664
REMARK 3 28 1.3500 - 1.3300 0.66 2833 168 0.2372 0.2693
REMARK 3 29 1.3300 - 1.3100 0.60 2558 148 0.2538 0.2697
REMARK 3 30 1.3100 - 1.3000 0.54 2360 124 0.2618 0.3123
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) : 0.116
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.325
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.55
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 : 0.006 4204
REMARK 3 ANGLE : 0.936 5785
REMARK 3 CHIRALITY : 0.078 649
REMARK 3 PLANARITY : 0.007 772
REMARK 3 DIHEDRAL : 26.163 1565
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 : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 2 through 9 or
REMARK 3 resid 11 through 12 or resid 15 through
REMARK 3 18 or resid 20 through 24 or resid 26
REMARK 3 through 32 or (resid 33 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 34 through 35 or resid 37
REMARK 3 through 66 or resid 68 or resid 70
REMARK 3 through 100 or resid 102 through 113 or
REMARK 3 resid 115 through 124 or resid 126
REMARK 3 through 130 or resid 132 through 138 or
REMARK 3 resid 140 through 145 or resid 147
REMARK 3 through 158 or resid 160 or resid 162
REMARK 3 through 194 or resid 196 through 201 or
REMARK 3 resid 203 through 213 or resid 215
REMARK 3 through 246 or resid 248 through 249 or
REMARK 3 resid 251 or resid 254 through 259 or
REMARK 3 resid 300))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 2 through 9 or
REMARK 3 resid 11 through 12 or resid 15 through
REMARK 3 18 or resid 20 through 24 or resid 26
REMARK 3 through 35 or resid 37 through 66 or
REMARK 3 resid 68 or resid 70 through 100 or resid
REMARK 3 102 through 113 or resid 115 through 124
REMARK 3 or resid 126 through 130 or resid 132
REMARK 3 through 138 or resid 140 through 145 or
REMARK 3 resid 147 through 158 or resid 160 or
REMARK 3 resid 162 through 194 or resid 196
REMARK 3 through 201 or resid 203 through 213 or
REMARK 3 resid 215 through 246 or resid 248
REMARK 3 through 249 or resid 251 or resid 254
REMARK 3 through 258 or (resid 259 and (name N or
REMARK 3 name CA or name C or name O or name CB or
REMARK 3 name CG or name CD1 or name CD2 or name
REMARK 3 CE1 or name CE2 or name CZ )) or resid
REMARK 3 300))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7NEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-21.
REMARK 100 THE DEPOSITION ID IS D_1292113698.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976260
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20200417
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127681
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 56.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 12.10
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.40400
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: PHASER 2.8.3
REMARK 200 STARTING MODEL: HOMOLOGY MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE 20 % (W/V) PEG
REMARK 280 4,000 20 % (V/V) 2-PROPANOL, PH 5.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 292K
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 28.17500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.55000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.84000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.55000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.17500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.84000
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 MET A 1
REMARK 465 LEU A 260
REMARK 465 GLU A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 MET B 1
REMARK 465 LEU B 260
REMARK 465 GLU B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
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 LEU B 33 CG CD1 CD2
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 415 O HOH A 511 1.96
REMARK 500 O HOH B 656 O HOH B 805 2.01
REMARK 500 OD2 ASP A 10 O HOH A 401 2.03
REMARK 500 O HOH A 803 O HOH A 813 2.10
REMARK 500 O HOH B 598 O HOH B 778 2.12
REMARK 500 O HOH A 780 O HOH A 801 2.14
REMARK 500 O HOH B 510 O HOH B 757 2.16
REMARK 500 O HOH B 791 O HOH B 828 2.17
REMARK 500 O HOH A 789 O HOH A 793 2.18
REMARK 500 O HOH A 707 O HOH A 717 2.18
REMARK 500 O ALA A 35 O HOH A 402 2.19
REMARK 500 O HOH A 812 O HOH A 816 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 421 O HOH B 425 2555 2.11
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 SER A 131 -125.40 60.03
REMARK 500 SER A 131 -126.77 62.16
REMARK 500 HIS A 185 -94.95 -118.55
REMARK 500 PRO A 243 -150.27 -81.01
REMARK 500 SER B 131 -127.89 63.80
REMARK 500 SER B 131 -127.04 62.52
REMARK 500 ASN B 144 92.36 -161.65
REMARK 500 HIS B 185 -96.27 -118.58
REMARK 500 PRO B 243 -156.07 -79.31
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 815 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 816 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 832 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH B 833 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B 834 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH B 835 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH B 836 DISTANCE = 7.11 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 NA A 300 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 148 OE2
REMARK 620 2 PHE A 230 O 105.0
REMARK 620 3 ASP A 233 OD1 165.2 87.1
REMARK 620 4 HOH A 575 O 73.3 84.5 117.2
REMARK 620 5 HOH A 589 O 81.8 84.6 90.9 149.1
REMARK 620 6 HOH A 658 O 85.4 169.6 82.5 99.8 96.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 300 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 148 OE2
REMARK 620 2 PHE B 230 O 104.1
REMARK 620 3 ASP B 233 OD1 162.5 88.4
REMARK 620 4 HOH B 589 O 70.7 83.3 123.8
REMARK 620 5 HOH B 622 O 80.9 86.6 87.9 146.3
REMARK 620 6 HOH B 701 O 81.4 174.5 86.4 97.9 95.2
REMARK 620 N 1 2 3 4 5
DBREF 7NEI A 1 267 PDB 7NEI 7NEI 1 267
DBREF 7NEI B 1 267 PDB 7NEI 7NEI 1 267
SEQRES 1 A 267 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 267 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 A 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 267 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 A 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 A 267 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 A 267 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 267 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 267 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 A 267 LEU VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 267 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 A 267 HIS LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 A 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 A 267 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 267 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 B 267 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 B 267 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 B 267 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 B 267 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 B 267 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 B 267 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 B 267 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 B 267 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 B 267 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 B 267 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 B 267 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 B 267 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 B 267 LEU VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL
SEQRES 15 B 267 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 B 267 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 B 267 HIS LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 B 267 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP
SEQRES 19 B 267 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 B 267 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE LEU
SEQRES 21 B 267 GLU HIS HIS HIS HIS HIS HIS
HET NA A 300 1
HET NA B 300 1
HETNAM NA SODIUM ION
FORMUL 3 NA 2(NA 1+)
FORMUL 5 HOH *852(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 GLY A 66 ALA A 71 5 6
HELIX 3 AA3 TRP A 72 SER A 79 1 8
HELIX 4 AA4 GLN A 95 ARG A 111 1 17
HELIX 5 AA5 VAL A 116 ASN A 118 5 3
HELIX 6 AA6 SER A 131 ASN A 143 1 13
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 SER A 208 THR A 214 5 7
HELIX 9 AA9 ASP A 216 ASP A 232 1 17
HELIX 10 AB1 ASP A 234 LEU A 241 5 8
HELIX 11 AB2 THR B 12 ALA B 18 1 7
HELIX 12 AB3 GLY B 66 ALA B 71 5 6
HELIX 13 AB4 TRP B 72 SER B 79 1 8
HELIX 14 AB5 GLN B 95 ARG B 111 1 17
HELIX 15 AB6 VAL B 116 ASN B 118 5 3
HELIX 16 AB7 SER B 131 ASN B 143 1 13
HELIX 17 AB8 HIS B 185 LEU B 193 1 9
HELIX 18 AB9 SER B 208 THR B 214 5 7
HELIX 19 AC1 ASP B 216 ASP B 232 1 17
HELIX 20 AC2 ASP B 234 LEU B 241 5 8
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O ILE A 43 N THR A 28
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O ILE A 85
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ASP A 121 N PHE A 54
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O ALA A 200 N VAL A 171
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O ARG A 254 N TYR A 201
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O GLY B 41 N VAL B 30
SHEET 3 AA3 6 VAL B 83 ILE B 87 -1 O VAL B 84 N TYR B 44
SHEET 4 AA3 6 PHE B 54 SER B 60 1 N VAL B 57 O ILE B 85
SHEET 5 AA3 6 ILE B 120 HIS B 130 1 O MET B 128 N ALA B 58
SHEET 6 AA3 6 ALA B 149 LEU B 153 1 O LEU B 153 N GLY B 129
SHEET 1 AA4 3 THR B 169 ALA B 174 0
SHEET 2 AA4 3 LYS B 199 LEU B 204 1 O ALA B 200 N VAL B 171
SHEET 3 AA4 3 ILE B 250 SER B 255 -1 O ARG B 254 N TYR B 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.02
SSBOND 2 CYS B 242 CYS B 257 1555 1555 2.02
LINK OE2 GLU A 148 NA NA A 300 1555 1555 2.41
LINK O PHE A 230 NA NA A 300 1555 1555 2.28
LINK OD1 ASP A 233 NA NA A 300 1555 1555 2.46
LINK NA NA A 300 O HOH A 575 1555 1555 2.51
LINK NA NA A 300 O HOH A 589 1555 1555 2.51
LINK NA NA A 300 O HOH A 658 1555 1555 2.40
LINK OE2 GLU B 148 NA NA B 300 1555 1555 2.57
LINK O PHE B 230 NA NA B 300 1555 1555 2.29
LINK OD1 ASP B 233 NA NA B 300 1555 1555 2.43
LINK NA NA B 300 O HOH B 589 1555 1555 2.54
LINK NA NA B 300 O HOH B 622 1555 1555 2.51
LINK NA NA B 300 O HOH B 701 1555 1555 2.37
CISPEP 1 CYS A 242 PRO A 243 0 -8.72
CISPEP 2 CYS A 257 PRO A 258 0 -3.67
CISPEP 3 CYS B 242 PRO B 243 0 -8.98
CISPEP 4 CYS B 257 PRO B 258 0 -3.52
CRYST1 56.350 97.680 101.100 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 0.017746 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009891 0.00000
MTRIX1 1 -0.999992 -0.002693 -0.002949 56.24773 1
MTRIX2 1 -0.002935 0.996359 0.085204 4.38351 1
MTRIX3 1 0.002709 0.085212 -0.996359 -53.93749 1
TER 4028 PHE A 259
TER 8074 PHE B 259
MASTER 415 0 2 20 18 0 0 9 4773 2 20 42
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