HEADER TRANSLATION 28-FEB-14 4CRM
TITLE CRYO-EM OF A PRE-RECYCLING COMPLEX WITH ERF1 AND ABCE1
CAVEAT 4CRM LYS X 331 HAS WRONG CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATION INITIATION FACTOR RLI1;
COMPND 3 CHAIN: P;
COMPND 4 SYNONYM: ATP-BINDING CASSETTE SUB-FAMILY E MEMBER RLI1, RNASE L
COMPND 5 INHIBITOR, ABCE1 IN RIBOSOME BOUND ERF1-ABCE1-ADPNP COMPLEX;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1;
COMPND 9 CHAIN: X;
COMPND 10 SYNONYM: EUKARYOTIC RELEASE FACTOR 1, ERF1, OMNIPOTENT SUPPRESSOR
COMPND 11 PROTEIN 1, ERF1 IN RIBOSOME-BOUND ERF1-ABCE1-ADPNP COMPLEX;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PYES2;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 4932;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSLATION, TERMINATION, RECYCLING
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.PREIS,A.HEUER,C.BARRIO-GARCIA,A.HAUSER,D.EYLER,O.BERNINGHAUSEN,
AUTHOR 2 R.GREEN,T.BECKER,R.BECKMANN
REVDAT 4 20-NOV-19 4CRM 1 CAVEAT REMARK LINK
REVDAT 3 30-AUG-17 4CRM 1 REMARK
REVDAT 2 11-MAY-16 4CRM 1 AUTHOR
REVDAT 1 23-JUL-14 4CRM 0
JRNL AUTH A.PREIS,A.HEUER,C.BARRIO-GARCIA,A.HAUSER,D.E.EYLER,
JRNL AUTH 2 O.BERNINGHAUSEN,R.GREEN,T.BECKER,R.BECKMANN
JRNL TITL CRYOELECTRON MICROSCOPIC STRUCTURES OF EUKARYOTIC
JRNL TITL 2 TRANSLATION TERMINATION COMPLEXES CONTAINING ERF1-ERF3 OR
JRNL TITL 3 ERF1-ABCE1.
JRNL REF CELL REP. V. 8 59 2014
JRNL REFN ESSN 2211-1247
JRNL PMID 25001285
JRNL DOI 10.1016/J.CELREP.2014.04.058
REMARK 2
REMARK 2 RESOLUTION. 8.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : COOT, MDFF, UCSF CHIMERA, STARFISH,
REMARK 3 SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1DT9
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--RIGID BODY
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 8.750
REMARK 3 NUMBER OF PARTICLES : 39309
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD
REMARK 3 -2598.
REMARK 4
REMARK 4 4CRM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290059858.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : CMV-STALLED WHEAT GERM 80S-RNC
REMARK 245 BOUND TO ERF1 AND ABCE1-ADPNP
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFICATION 1 -CRYOGEN-
REMARK 245 ETHANE, HUMIDITY- 100,
REMARK 245 INSTRUMENT- FEI VITROBOT MARK
REMARK 245 IV, METHOD- BLOT FOR 3 SECONDS
REMARK 245 BEFORE PLUNGING
REMARK 245 SAMPLE BUFFER : 20 MM HEPES PH 7.5, 200 MM KCL,
REMARK 245 1.5 MGCL2, 2 MM DTT, 0.01 MG/ML
REMARK 245 CYCLOHEXIMIDE, 0.05 % NIKKOL,
REMARK 245 0.03 % DBC, 0.5 MM ADPNP).
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 20-FEB-13
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI MORGAGNI
REMARK 245 DETECTOR TYPE : TVIPS TEMCAM-F416 (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : 147136
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, X
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 CD1 ILE P 72 S1 SF4 P 1610 0.96
REMARK 500 SG CYS P 61 FE3 SF4 P 1610 0.96
REMARK 500 OG SER P 117 MG MG P 1613 1.19
REMARK 500 CB LEU X 323 CD1 ILE X 370 1.33
REMARK 500 CG2 ILE X 302 CE LYS X 340 1.53
REMARK 500 CB LEU X 173 NH1 ARG X 191 1.57
REMARK 500 OH TYR X 287 CD1 ILE X 318 1.71
REMARK 500 SG CYS P 21 FE2 SF4 P 1611 1.74
REMARK 500 CG2 ILE X 302 NZ LYS X 340 1.75
REMARK 500 C ILE X 302 NZ LYS X 340 1.75
REMARK 500 CG LEU X 323 CG1 ILE X 370 1.79
REMARK 500 CG2 ILE X 302 CD LYS X 340 1.83
REMARK 500 CB LEU X 323 CG1 ILE X 370 1.84
REMARK 500 CD1 LEU X 323 CG1 ILE X 370 1.94
REMARK 500 N GLY P 115 O1B ATP P 1609 1.96
REMARK 500 OD1 ASP X 310 CE1 PHE X 380 1.98
REMARK 500 O ILE X 302 NZ LYS X 340 2.06
REMARK 500 CG LEU X 173 NH1 ARG X 191 2.13
REMARK 500 CD1 ILE X 302 CB THR X 325 2.14
REMARK 500 N LYS P 116 O1B ATP P 1609 2.14
REMARK 500 N GLY P 388 O3B ADP P 1612 2.17
REMARK 500 CB CYS P 61 FE3 SF4 P 1610 2.18
REMARK 500 CG LEU X 323 CD1 ILE X 370 2.18
REMARK 500 O GLY X 301 OG1 THR X 305 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER P 309 CA SER P 309 CB -0.155
REMARK 500 GLN P 589 CA GLN P 589 CB 0.177
REMARK 500 GLN P 589 CB GLN P 589 CG 0.209
REMARK 500 GLN P 589 CA GLN P 589 C 0.245
REMARK 500 ILE P 608 C ILE P 608 O -0.229
REMARK 500 ILE P 608 C ILE P 608 OXT -0.229
REMARK 500 GLY X 150 N GLY X 150 CA 0.117
REMARK 500 GLY X 150 CA GLY X 150 C 0.115
REMARK 500 GLY X 181 CA GLY X 181 C -0.105
REMARK 500 ARG X 186 CD ARG X 186 NE 0.177
REMARK 500 ARG X 186 NE ARG X 186 CZ 0.117
REMARK 500 ILE X 302 C ASP X 303 N 0.147
REMARK 500 SER X 421 C SER X 421 O -0.229
REMARK 500 SER X 421 C SER X 421 OXT -0.229
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 ARG P 573 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASN P 584 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 LYS P 585 CB - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 LEU P 586 CB - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU P 586 CB - CG - CD2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP P 587 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 SER P 588 N - CA - CB ANGL. DEV. = 19.2 DEGREES
REMARK 500 SER P 588 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLN P 589 CB - CA - C ANGL. DEV. = 21.2 DEGREES
REMARK 500 GLN P 589 N - CA - CB ANGL. DEV. = -20.4 DEGREES
REMARK 500 GLN P 589 CA - CB - CG ANGL. DEV. = 28.3 DEGREES
REMARK 500 GLN P 589 CB - CG - CD ANGL. DEV. = 29.5 DEGREES
REMARK 500 GLN P 589 CA - C - N ANGL. DEV. = -21.2 DEGREES
REMARK 500 ASP X 149 CA - C - N ANGL. DEV. = 29.6 DEGREES
REMARK 500 ASP X 149 O - C - N ANGL. DEV. = -30.0 DEGREES
REMARK 500 LYS X 175 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG X 179 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 ARG X 179 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 SER X 183 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG X 186 CA - CB - CG ANGL. DEV. = 23.2 DEGREES
REMARK 500 ARG X 186 CG - CD - NE ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG X 186 NH1 - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG X 186 NE - CZ - NH2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG X 195 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 LYS X 281 CA - CB - CG ANGL. DEV. = 24.9 DEGREES
REMARK 500 GLN X 293 N - CA - CB ANGL. DEV. = 15.4 DEGREES
REMARK 500 PHE X 298 CB - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 PHE X 298 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 PHE X 298 CB - CG - CD1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 LEU X 317 CB - CG - CD2 ANGL. DEV. = 15.6 DEGREES
REMARK 500 PHE X 320 N - CA - CB ANGL. DEV. = 12.3 DEGREES
REMARK 500 LYS X 331 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 LYS X 331 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 ASP X 335 O - C - N ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP X 354 C - N - CA ANGL. DEV. = 18.5 DEGREES
REMARK 500 MET X 361 CG - SD - CE ANGL. DEV. = -11.6 DEGREES
REMARK 500 PRO X 368 CA - N - CD ANGL. DEV. = -12.3 DEGREES
REMARK 500 LEU X 369 CB - CA - C ANGL. DEV. = -12.1 DEGREES
REMARK 500 TRP X 372 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 TRP X 372 CB - CG - CD1 ANGL. DEV. = -14.7 DEGREES
REMARK 500 VAL X 412 CG1 - CB - CG2 ANGL. DEV. = 10.4 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 P 22 -167.35 61.97
REMARK 500 SER P 28 -55.74 79.26
REMARK 500 PHE P 67 -70.31 -81.98
REMARK 500 ASP P 68 36.49 140.78
REMARK 500 THR P 77 45.56 73.50
REMARK 500 SER P 88 -171.37 174.48
REMARK 500 ARG P 96 169.51 55.56
REMARK 500 LEU P 131 32.38 71.37
REMARK 500 ARG P 133 -147.95 -155.45
REMARK 500 ASP P 135 119.23 -31.87
REMARK 500 ASP P 136 -159.17 -88.38
REMARK 500 PRO P 138 88.80 -27.82
REMARK 500 LYS P 186 -162.83 -77.28
REMARK 500 MET P 195 92.56 -68.41
REMARK 500 LYS P 197 -128.63 -72.66
REMARK 500 TYR P 251 -20.37 73.31
REMARK 500 SER P 299 -13.11 72.01
REMARK 500 ALA P 339 -12.96 94.89
REMARK 500 ALA P 350 -139.57 66.74
REMARK 500 ALA P 353 -157.33 -145.20
REMARK 500 LYS P 412 63.91 -105.11
REMARK 500 PRO P 424 -70.42 -44.53
REMARK 500 LYS P 425 56.98 32.96
REMARK 500 ILE P 438 124.93 -172.70
REMARK 500 VAL P 451 -62.77 -95.92
REMARK 500 ARG P 456 74.66 72.02
REMARK 500 GLU P 493 75.68 42.83
REMARK 500 LYS P 547 -79.78 -137.84
REMARK 500 ARG P 573 -147.39 -98.09
REMARK 500 THR X 162 155.54 -34.04
REMARK 500 ARG X 163 126.58 178.69
REMARK 500 THR X 164 144.90 -172.54
REMARK 500 VAL X 171 -66.48 -143.90
REMARK 500 ASP X 172 178.07 127.33
REMARK 500 LEU X 173 117.26 125.49
REMARK 500 LYS X 175 95.40 134.48
REMARK 500 HIS X 177 -8.95 -164.18
REMARK 500 ARG X 179 -60.77 -16.23
REMARK 500 GLN X 182 0.65 -56.64
REMARK 500 ALA X 184 2.88 -53.60
REMARK 500 LEU X 185 -24.05 -140.35
REMARK 500 ASN X 213 50.96 92.72
REMARK 500 ASP X 214 155.85 66.47
REMARK 500 LYS X 215 -108.53 52.77
REMARK 500 ALA X 227 -82.03 -29.49
REMARK 500 LEU X 233 -61.78 -95.88
REMARK 500 ARG X 242 -20.42 90.08
REMARK 500 GLU X 280 -99.67 -55.99
REMARK 500 LYS X 281 -79.57 -21.93
REMARK 500 LYS X 282 -96.63 -39.19
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP X 140 ASP X 141 -148.54
REMARK 500 ASP X 141 LYS X 142 -145.18
REMARK 500 SER X 392 GLU X 393 147.63
REMARK 500 PHE X 401 GLY X 402 -146.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG P 574 0.13 SIDE CHAIN
REMARK 500 ASP X 141 0.08 SIDE CHAIN
REMARK 500 ASP X 149 0.09 SIDE CHAIN
REMARK 500 ARG X 179 0.20 SIDE CHAIN
REMARK 500 ARG X 191 0.21 SIDE CHAIN
REMARK 500 TYR X 198 0.06 SIDE CHAIN
REMARK 500 ASP X 214 0.09 SIDE CHAIN
REMARK 500 ASN X 217 0.08 SIDE CHAIN
REMARK 500 ASP X 240 0.07 SIDE CHAIN
REMARK 500 PHE X 298 0.38 SIDE CHAIN
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 GLN P 589 -17.00
REMARK 500 PRO X 174 10.80
REMARK 500 ARG X 191 -14.21
REMARK 500 GLU X 192 -13.94
REMARK 500 ASN X 262 -12.63
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 SF4 P1611 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 16 SG
REMARK 620 2 SF4 P1611 S1 149.7
REMARK 620 3 SF4 P1611 S2 74.1 108.5
REMARK 620 4 SF4 P1611 S3 102.2 106.1 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 P1610 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 55 SG
REMARK 620 2 SF4 P1610 S1 114.3
REMARK 620 3 SF4 P1610 S3 62.6 95.8
REMARK 620 4 SF4 P1610 S4 143.2 101.8 108.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG P1613 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP P1609 O1G
REMARK 620 2 ATP P1609 O2B 78.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP P 1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 P 1610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 P 1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP P 1612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 1613
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CRN RELATED DB: PDB
REMARK 900 CRYO-EM OF A PRETERMINATION COMPLEX WITH ERF1 AND ERF3
REMARK 900 RELATED ID: EMD-2598 RELATED DB: EMDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 139 AMINO ACIDS ARE MISSING. THE C-TERMINAL
REMARK 999 AMINO ACIDS 422-440 ARE MISSING
DBREF 4CRM P 1 608 UNP Q03195 RLI1_YEAST 1 608
DBREF 4CRM X 140 421 UNP P12385 ERF1_YEAST 140 421
SEQRES 1 P 608 MET SER ASP LYS ASN SER ARG ILE ALA ILE VAL SER ALA
SEQRES 2 P 608 ASP LYS CYS LYS PRO LYS LYS CYS ARG GLN GLU CYS LYS
SEQRES 3 P 608 ARG SER CYS PRO VAL VAL LYS THR GLY LYS LEU CYS ILE
SEQRES 4 P 608 GLU VAL THR PRO THR SER LYS ILE ALA PHE ILE SER GLU
SEQRES 5 P 608 ILE LEU CYS ILE GLY CYS GLY ILE CYS VAL LYS LYS CYS
SEQRES 6 P 608 PRO PHE ASP ALA ILE GLN ILE ILE ASN LEU PRO THR ASN
SEQRES 7 P 608 LEU GLU ALA HIS VAL THR HIS ARG TYR SER ALA ASN SER
SEQRES 8 P 608 PHE LYS LEU HIS ARG LEU PRO THR PRO ARG PRO GLY GLN
SEQRES 9 P 608 VAL LEU GLY LEU VAL GLY THR ASN GLY ILE GLY LYS SER
SEQRES 10 P 608 THR ALA LEU LYS ILE LEU ALA GLY LYS GLN LYS PRO ASN
SEQRES 11 P 608 LEU GLY ARG PHE ASP ASP PRO PRO GLU TRP GLN GLU ILE
SEQRES 12 P 608 ILE LYS TYR PHE ARG GLY SER GLU LEU GLN ASN TYR PHE
SEQRES 13 P 608 THR LYS MET LEU GLU ASP ASP ILE LYS ALA ILE ILE LYS
SEQRES 14 P 608 PRO GLN TYR VAL ASP ASN ILE PRO ARG ALA ILE LYS GLY
SEQRES 15 P 608 PRO VAL GLN LYS VAL GLY GLU LEU LEU LYS LEU ARG MET
SEQRES 16 P 608 GLU LYS SER PRO GLU ASP VAL LYS ARG TYR ILE LYS ILE
SEQRES 17 P 608 LEU GLN LEU GLU ASN VAL LEU LYS ARG ASP ILE GLU LYS
SEQRES 18 P 608 LEU SER GLY GLY GLU LEU GLN ARG PHE ALA ILE GLY MET
SEQRES 19 P 608 SER CYS VAL GLN GLU ALA ASP VAL TYR MET PHE ASP GLU
SEQRES 20 P 608 PRO SER SER TYR LEU ASP VAL LYS GLN ARG LEU ASN ALA
SEQRES 21 P 608 ALA GLN ILE ILE ARG SER LEU LEU ALA PRO THR LYS TYR
SEQRES 22 P 608 VAL ILE CYS VAL GLU HIS ASP LEU SER VAL LEU ASP TYR
SEQRES 23 P 608 LEU SER ASP PHE VAL CYS ILE ILE TYR GLY VAL PRO SER
SEQRES 24 P 608 VAL TYR GLY VAL VAL THR LEU PRO ALA SER VAL ARG GLU
SEQRES 25 P 608 GLY ILE ASN ILE PHE LEU ASP GLY HIS ILE PRO ALA GLU
SEQRES 26 P 608 ASN LEU ARG PHE ARG THR GLU ALA LEU GLN PHE ARG ILE
SEQRES 27 P 608 ALA ASP ALA THR GLU ASP LEU GLN ASN ASP SER ALA SER
SEQRES 28 P 608 ARG ALA PHE SER TYR PRO SER LEU LYS LYS THR GLN GLY
SEQRES 29 P 608 ASP PHE VAL LEU ASN VAL GLU GLU GLY GLU PHE SER ASP
SEQRES 30 P 608 SER GLU ILE LEU VAL MET MET GLY GLU ASN GLY THR GLY
SEQRES 31 P 608 LYS THR THR LEU ILE LYS LEU LEU ALA GLY ALA LEU LYS
SEQRES 32 P 608 PRO ASP GLU GLY GLN ASP ILE PRO LYS LEU ASN VAL SER
SEQRES 33 P 608 MET LYS PRO GLN LYS ILE ALA PRO LYS PHE PRO GLY THR
SEQRES 34 P 608 VAL ARG GLN LEU PHE PHE LYS LYS ILE ARG GLY GLN PHE
SEQRES 35 P 608 LEU ASN PRO GLN PHE GLN THR ASP VAL VAL LYS PRO LEU
SEQRES 36 P 608 ARG ILE ASP ASP ILE ILE ASP GLN GLU VAL GLN HIS LEU
SEQRES 37 P 608 SER GLY GLY GLU LEU GLN ARG VAL ALA ILE VAL LEU ALA
SEQRES 38 P 608 LEU GLY ILE PRO ALA ASP ILE TYR LEU ILE ASP GLU PRO
SEQRES 39 P 608 SER ALA TYR LEU ASP SER GLU GLN ARG ILE ILE CYS SER
SEQRES 40 P 608 LYS VAL ILE ARG ARG PHE ILE LEU HIS ASN LYS LYS THR
SEQRES 41 P 608 ALA PHE ILE VAL GLU HIS ASP PHE ILE MET ALA THR TYR
SEQRES 42 P 608 LEU ALA ASP LYS VAL ILE VAL PHE GLU GLY ILE PRO SER
SEQRES 43 P 608 LYS ASN ALA HIS ALA ARG ALA PRO GLU SER LEU LEU THR
SEQRES 44 P 608 GLY CYS ASN ARG PHE LEU LYS ASN LEU ASN VAL THR PHE
SEQRES 45 P 608 ARG ARG ASP PRO ASN SER PHE ARG PRO ARG ILE ASN LYS
SEQRES 46 P 608 LEU ASP SER GLN MET ASP LYS GLU GLN LYS SER SER GLY
SEQRES 47 P 608 ASN TYR PHE PHE LEU ASP ASN THR GLY ILE
SEQRES 1 X 282 ASP ASP LYS PHE GLY PHE ILE VAL MET ASP GLY GLN GLY
SEQRES 2 X 282 THR LEU PHE GLY SER VAL SER GLY ASN THR ARG THR VAL
SEQRES 3 X 282 LEU HIS LYS PHE THR VAL ASP LEU PRO LYS LYS HIS GLY
SEQRES 4 X 282 ARG GLY GLY GLN SER ALA LEU ARG PHE ALA ARG LEU ARG
SEQRES 5 X 282 GLU GLU LYS ARG HIS ASN TYR VAL ARG LYS VAL ALA GLU
SEQRES 6 X 282 VAL ALA VAL GLN ASN PHE ILE THR ASN ASP LYS VAL ASN
SEQRES 7 X 282 VAL LYS GLY LEU ILE LEU ALA GLY SER ALA ASP PHE LYS
SEQRES 8 X 282 THR ASP LEU ALA LYS SER GLU LEU PHE ASP PRO ARG LEU
SEQRES 9 X 282 ALA CYS LYS VAL ILE SER ILE VAL ASP VAL SER TYR GLY
SEQRES 10 X 282 GLY GLU ASN GLY PHE ASN GLN ALA ILE GLU LEU SER ALA
SEQRES 11 X 282 GLU ALA LEU ALA ASN VAL LYS TYR VAL GLN GLU LYS LYS
SEQRES 12 X 282 LEU LEU GLU ALA TYR PHE ASP GLU ILE SER GLN ASP THR
SEQRES 13 X 282 GLY LYS PHE CYS TYR GLY ILE ASP ASP THR LEU LYS ALA
SEQRES 14 X 282 LEU ASP LEU GLY ALA VAL GLU LYS LEU ILE VAL PHE GLU
SEQRES 15 X 282 ASN LEU GLU THR ILE ARG TYR THR PHE LYS ASP ALA GLU
SEQRES 16 X 282 ASP ASN GLU VAL ILE LYS PHE ALA GLU PRO GLU ALA LYS
SEQRES 17 X 282 ASP LYS SER PHE ALA ILE ASP LYS ALA THR GLY GLN GLU
SEQRES 18 X 282 MET ASP VAL VAL SER GLU GLU PRO LEU ILE GLU TRP LEU
SEQRES 19 X 282 ALA ALA ASN TYR LYS ASN PHE GLY ALA THR LEU GLU PHE
SEQRES 20 X 282 ILE THR ASP LYS SER SER GLU GLY ALA GLN PHE VAL THR
SEQRES 21 X 282 GLY PHE GLY GLY ILE GLY ALA MET LEU ARG TYR LYS VAL
SEQRES 22 X 282 ASN PHE GLU GLN LEU VAL ASP GLU SER
HET ATP P1609 31
HET SF4 P1610 8
HET SF4 P1611 8
HET ADP P1612 27
HET MG P1613 1
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 SF4 2(FE4 S4)
FORMUL 6 ADP C10 H15 N5 O10 P2
FORMUL 7 MG MG 2+
FORMUL 8 HOH *(H2 O)
HELIX 1 1 CYS P 29 GLY P 35 1 7
HELIX 2 2 GLY P 59 CYS P 65 1 7
HELIX 3 3 GLY P 115 GLY P 125 1 11
HELIX 4 4 GLU P 139 PHE P 147 1 9
HELIX 5 5 GLU P 151 ASP P 162 1 12
HELIX 6 6 ASN P 175 ILE P 180 1 6
HELIX 7 7 LYS P 186 MET P 195 1 10
HELIX 8 8 SER P 198 GLN P 210 1 13
HELIX 9 9 GLU P 212 LYS P 216 5 5
HELIX 10 10 SER P 223 GLN P 238 1 16
HELIX 11 11 ASP P 253 SER P 266 1 14
HELIX 12 12 LEU P 267 ALA P 269 5 3
HELIX 13 13 ASP P 280 SER P 288 1 9
HELIX 14 14 VAL P 310 GLY P 320 1 11
HELIX 15 15 GLY P 390 GLY P 400 1 11
HELIX 16 16 THR P 429 ILE P 438 1 10
HELIX 17 17 ARG P 439 LEU P 443 5 5
HELIX 18 18 ASN P 444 VAL P 451 1 8
HELIX 19 19 VAL P 451 ARG P 456 1 6
HELIX 20 20 SER P 469 LEU P 482 1 14
HELIX 21 21 ASP P 499 LYS P 518 1 20
HELIX 22 22 ASP P 527 ALA P 535 1 9
HELIX 23 23 LEU P 557 ASN P 569 1 13
HELIX 24 24 SER P 588 GLY P 598 1 11
HELIX 25 25 LEU X 185 ILE X 211 1 27
HELIX 26 26 ALA X 227 PHE X 229 5 3
HELIX 27 27 LYS X 230 LYS X 235 1 6
HELIX 28 28 LEU X 243 CYS X 245 5 3
HELIX 29 29 GLY X 256 LEU X 267 1 12
HELIX 30 30 SER X 268 GLU X 280 1 13
HELIX 31 31 GLU X 280 ILE X 291 1 12
HELIX 32 32 TYR X 300 LEU X 311 1 12
HELIX 33 33 ALA X 346 PHE X 351 1 6
HELIX 34 34 LEU X 369 ALA X 375 1 7
HELIX 35 35 ASN X 376 GLY X 381 1 6
HELIX 36 36 GLU X 393 GLY X 400 1 8
SHEET 1 PA 2 SER P 6 VAL P 11 0
SHEET 2 PA 2 ILE P 70 LEU P 75 -1 O GLN P 71 N ILE P 10
SHEET 1 PB 2 ILE P 39 THR P 42 0
SHEET 2 PB 2 ILE P 47 ILE P 50 -1 O ILE P 47 N THR P 42
SHEET 1 PC 2 VAL P 83 ARG P 86 0
SHEET 2 PC 2 LYS P 93 HIS P 95 -1 O LEU P 94 N THR P 84
SHEET 1 PD 6 ILE P 167 LYS P 169 0
SHEET 2 PD 6 VAL P 242 ASP P 246 1 O VAL P 242 N ILE P 167
SHEET 3 PD 6 TYR P 273 VAL P 277 1 O TYR P 273 N TYR P 243
SHEET 4 PD 6 VAL P 105 VAL P 109 1 O LEU P 106 N CYS P 276
SHEET 5 PD 6 PHE P 290 TYR P 295 1 O PHE P 290 N GLY P 107
SHEET 6 PD 6 VAL P 303 VAL P 304 -1 O VAL P 303 N TYR P 295
SHEET 1 PE 6 ILE P 167 LYS P 169 0
SHEET 2 PE 6 VAL P 242 ASP P 246 1 O VAL P 242 N ILE P 167
SHEET 3 PE 6 TYR P 273 VAL P 277 1 O TYR P 273 N TYR P 243
SHEET 4 PE 6 VAL P 105 VAL P 109 1 O LEU P 106 N CYS P 276
SHEET 5 PE 6 PHE P 290 TYR P 295 1 O PHE P 290 N GLY P 107
SHEET 6 PE 6 ALA P 308 SER P 309 -1 O ALA P 308 N VAL P 291
SHEET 1 PF 2 VAL P 303 VAL P 304 0
SHEET 2 PF 2 PHE P 290 TYR P 295 -1 O TYR P 295 N VAL P 303
SHEET 1 PG 2 HIS P 321 ILE P 322 0
SHEET 2 PG 2 LEU P 327 ARG P 328 -1 O LEU P 327 N ILE P 322
SHEET 1 PH 2 SER P 355 TYR P 356 0
SHEET 2 PH 2 GLY P 373 GLU P 374 -1 O GLY P 373 N TYR P 356
SHEET 1 PI 4 LEU P 359 THR P 362 0
SHEET 2 PI 4 VAL P 367 VAL P 370 -1 O LEU P 368 N LYS P 361
SHEET 3 PI 4 ASN P 548 HIS P 550 1 O ALA P 549 N ASN P 369
SHEET 4 PI 4 GLU P 542 ILE P 544 -1 O GLU P 542 N HIS P 550
SHEET 1 PJ 6 VAL P 415 LYS P 418 0
SHEET 2 PJ 6 ILE P 488 ASP P 492 1 O ILE P 488 N SER P 416
SHEET 3 PJ 6 THR P 520 VAL P 524 1 O THR P 520 N TYR P 489
SHEET 4 PJ 6 ILE P 380 MET P 384 1 O LEU P 381 N ILE P 523
SHEET 5 PJ 6 LYS P 537 VAL P 540 1 O LYS P 537 N VAL P 382
SHEET 6 PJ 6 GLU P 555 SER P 556 -1 O GLU P 555 N VAL P 538
SHEET 1 XA 5 THR X 162 PHE X 169 0
SHEET 2 XA 5 THR X 153 SER X 159 -1 O THR X 153 N PHE X 169
SHEET 3 XA 5 PHE X 143 MET X 148 -1 O PHE X 143 N VAL X 158
SHEET 4 XA 5 LEU X 221 ALA X 224 1 O ILE X 222 N ILE X 146
SHEET 5 XA 5 VAL X 247 VAL X 251 1 N ILE X 248 O LEU X 221
SHEET 1 XB 4 PHE X 298 CYS X 299 0
SHEET 2 XB 4 ALA X 406 LEU X 408 -1 O ALA X 406 N CYS X 299
SHEET 3 XB 4 VAL X 314 ILE X 318 -1 N GLU X 315 O MET X 407
SHEET 4 XB 4 LEU X 384 GLU X 385 1 N GLU X 385 O LEU X 317
SHEET 1 XC 3 ASN X 336 PHE X 341 0
SHEET 2 XC 3 ILE X 326 LYS X 331 -1 O ILE X 326 N PHE X 341
SHEET 3 XC 3 VAL X 363 PRO X 368 -1 N VAL X 364 O THR X 329
LINK SG CYS P 16 FE4 SF4 P1611 1555 1555 2.42
LINK SG CYS P 55 FE2 SF4 P1610 1555 1555 2.62
LINK O1G ATP P1609 MG MG P1613 1555 1555 2.67
LINK O2B ATP P1609 MG MG P1613 1555 1555 2.20
SITE 1 AC1 12 HOH P1903 TYR P 87 PHE P 92 ASN P 112
SITE 2 AC1 12 GLY P 113 ILE P 114 GLY P 115 LYS P 116
SITE 3 AC1 12 SER P 117 THR P 118 SER P 299 MG P1613
SITE 1 AC2 8 CYS P 29 CYS P 38 ILE P 50 CYS P 55
SITE 2 AC2 8 CYS P 58 GLY P 59 CYS P 61 ILE P 72
SITE 1 AC3 11 CYS P 16 LYS P 17 PRO P 18 CYS P 21
SITE 2 AC3 11 ARG P 22 GLU P 24 CYS P 25 CYS P 65
SITE 3 AC3 11 PRO P 66 PHE P 67 ALA P 69
SITE 1 AC4 12 ARG P 217 GLN P 363 PHE P 366 GLU P 386
SITE 2 AC4 12 ASN P 387 GLY P 388 THR P 389 GLY P 390
SITE 3 AC4 12 LYS P 391 THR P 392 THR P 393 SER P 546
SITE 1 AC5 3 SER P 117 GLN P 171 ATP P1609
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
