Header list of 1f6u.pdb file
Complete list - b 16 2 Bytes
HEADER STRUCTURAL PROTEIN/RNA 23-JUN-00 1F6U
TITLE NMR STRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO STEM-LOOP SL2
TITLE 2 OF THE PSI-RNA PACKAGING SIGNAL. IMPLICATIONS FOR GENOME RECOGNITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 STEM-LOOP SL2 FROM PSI-RNA PACKAGING;
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HIV-1 NUCLEOCAPSID PROTEIN;
COMPND 7 CHAIN: A;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 5 ORGANISM_TAXID: 11676;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNL4-3
KEYWDS HIV-1, RNA, PROTEIN-RNA COMPLEX, PACKAGING SIGNAL, STRUCTURAL
KEYWDS 2 PROTEIN-RNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.K.AMARASINGHE,R.N.DE GUZMAN,R.B.TURNER,K.J.CHANCELLOR,M.F.SUMMERS
REVDAT 3 16-FEB-22 1F6U 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1F6U 1 VERSN
REVDAT 1 09-OCT-00 1F6U 0
JRNL AUTH G.K.AMARASINGHE,R.N.DE GUZMAN,R.B.TURNER,K.J.CHANCELLOR,
JRNL AUTH 2 Z.R.WU,M.F.SUMMERS
JRNL TITL NMR STRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO
JRNL TITL 2 STEM-LOOP SL2 OF THE PSI-RNA PACKAGING SIGNAL. IMPLICATIONS
JRNL TITL 3 FOR GENOME RECOGNITION.
JRNL REF J.MOL.BIOL. V. 301 491 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10926523
JRNL DOI 10.1006/JMBI.2000.3979
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5
REMARK 3 AUTHORS : BURKER (XWINNMR), GUNTERT, MUMENTHALER AND
REMARK 3 WUTHRICH (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F6U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011315.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 278
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 25MM NACL; 25MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6-1.2 MM COMPLEX OF
REMARK 210 NUCLEOCAPSID PROTEIN AND SL2 RNA;
REMARK 210 NATURAL ABUNDANCE, 15N OR 13C/
REMARK 210 15N ISOTOPIC LABELED; 0.6-1.2 MM
REMARK 210 COMPLEX OF NUCLEOCAPSID PROTEIN
REMARK 210 AND SL2 RNA; NATURAL 15N
REMARK 210 ISOTOPIC LABELED; 0.6-1.2 MM
REMARK 210 COMPLEX OF NUCLEOCAPSID PROTEIN
REMARK 210 AND SL2 RNA; NATURAL A13C/15N
REMARK 210 ISOTOPIC LABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_ROESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; HNCA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.0, NMRVIEW 3.0, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: B, 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
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
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 1 G B 202 O4' G B 202 C4' -0.211
REMARK 500 1 C B 203 O4' C B 203 C4' -0.108
REMARK 500 1 G B 204 O4' G B 204 C4' -0.130
REMARK 500 1 C B 206 O4' C B 206 C4' -0.211
REMARK 500 1 G B 208 O4' G B 208 C4' -0.357
REMARK 500 1 U B 210 O4' U B 210 C4' -0.158
REMARK 500 1 G B 211 O4' G B 211 C4' -0.378
REMARK 500 1 G B 213 O4' G B 213 C4' -0.287
REMARK 500 1 U B 214 O4' U B 214 C4' -0.322
REMARK 500 1 C B 216 O4' C B 216 C4' -0.355
REMARK 500 1 G B 217 O4' G B 217 C4' -0.306
REMARK 500 1 C B 218 O4' C B 218 C4' -0.170
REMARK 500 2 G B 202 O4' G B 202 C4' -0.086
REMARK 500 2 G B 204 O4' G B 204 C4' -0.364
REMARK 500 2 A B 205 O4' A B 205 C4' -0.093
REMARK 500 2 G B 208 O4' G B 208 C4' -0.372
REMARK 500 2 U B 210 O4' U B 210 C4' -0.163
REMARK 500 2 G B 211 O4' G B 211 C4' -0.361
REMARK 500 2 G B 213 O4' G B 213 C4' -0.206
REMARK 500 2 U B 214 O4' U B 214 C4' -0.378
REMARK 500 2 C B 216 O4' C B 216 C4' -0.297
REMARK 500 2 G B 217 O4' G B 217 C4' -0.287
REMARK 500 3 G B 202 O4' G B 202 C4' -0.098
REMARK 500 3 C B 203 O4' C B 203 C4' -0.188
REMARK 500 3 G B 204 O4' G B 204 C4' -0.370
REMARK 500 3 A B 205 O4' A B 205 C4' -0.241
REMARK 500 3 C B 206 O4' C B 206 C4' -0.245
REMARK 500 3 G B 208 O4' G B 208 C4' -0.292
REMARK 500 3 G B 211 O4' G B 211 C4' -0.340
REMARK 500 3 G B 213 O4' G B 213 C4' -0.272
REMARK 500 3 U B 214 O4' U B 214 C4' -0.347
REMARK 500 3 C B 216 O4' C B 216 C4' -0.317
REMARK 500 3 G B 217 O4' G B 217 C4' -0.286
REMARK 500 4 C B 203 O4' C B 203 C4' -0.277
REMARK 500 4 G B 204 O4' G B 204 C4' -0.282
REMARK 500 4 A B 205 O4' A B 205 C4' -0.186
REMARK 500 4 C B 206 O4' C B 206 C4' -0.234
REMARK 500 4 U B 207 O4' U B 207 C4' -0.284
REMARK 500 4 G B 208 O4' G B 208 C4' -0.372
REMARK 500 4 G B 211 O4' G B 211 C4' -0.375
REMARK 500 4 G B 213 O4' G B 213 C4' -0.346
REMARK 500 4 U B 214 O4' U B 214 C4' -0.352
REMARK 500 4 C B 216 O4' C B 216 C4' -0.368
REMARK 500 4 G B 217 O4' G B 217 C4' -0.296
REMARK 500 4 C B 218 O4' C B 218 C4' -0.223
REMARK 500 5 G B 202 O4' G B 202 C4' -0.343
REMARK 500 5 C B 203 O4' C B 203 C4' -0.121
REMARK 500 5 G B 204 O4' G B 204 C4' -0.278
REMARK 500 5 A B 205 O4' A B 205 C4' -0.228
REMARK 500 5 C B 206 O4' C B 206 C4' -0.180
REMARK 500
REMARK 500 THIS ENTRY HAS 235 BOND DEVIATIONS.
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 1 G B 202 C5' - C4' - O4' ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 G B 202 C1' - O4' - C4' ANGL. DEV. = 6.3 DEGREES
REMARK 500 1 G B 202 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 202 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 202 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 C B 203 O4' - C4' - C3' ANGL. DEV. = -8.9 DEGREES
REMARK 500 1 G B 204 C5' - C4' - O4' ANGL. DEV. = 15.5 DEGREES
REMARK 500 1 G B 204 C1' - O4' - C4' ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 G B 204 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 204 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 204 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 A B 205 O4' - C4' - C3' ANGL. DEV. = -11.6 DEGREES
REMARK 500 1 A B 205 C5' - C4' - O4' ANGL. DEV. = 24.9 DEGREES
REMARK 500 1 C B 206 C5' - C4' - O4' ANGL. DEV. = 16.1 DEGREES
REMARK 500 1 C B 206 C1' - O4' - C4' ANGL. DEV. = 9.8 DEGREES
REMARK 500 1 U B 207 O4' - C4' - C3' ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 U B 207 C5' - C4' - O4' ANGL. DEV. = 18.9 DEGREES
REMARK 500 1 U B 207 C1' - O4' - C4' ANGL. DEV. = 8.0 DEGREES
REMARK 500 1 G B 208 C5' - C4' - O4' ANGL. DEV. = 9.9 DEGREES
REMARK 500 1 G B 208 C1' - O4' - C4' ANGL. DEV. = 13.3 DEGREES
REMARK 500 1 G B 208 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 208 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 208 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 G B 209 O4' - C4' - C3' ANGL. DEV. = -9.8 DEGREES
REMARK 500 1 G B 209 C5' - C4' - O4' ANGL. DEV. = 39.5 DEGREES
REMARK 500 1 G B 209 C1' - O4' - C4' ANGL. DEV. = 6.7 DEGREES
REMARK 500 1 G B 209 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 209 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 209 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 U B 210 C5' - C4' - O4' ANGL. DEV. = 18.1 DEGREES
REMARK 500 1 U B 210 C1' - O4' - C4' ANGL. DEV. = 9.6 DEGREES
REMARK 500 1 G B 211 C1' - O4' - C4' ANGL. DEV. = 13.3 DEGREES
REMARK 500 1 G B 211 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 211 N1 - C2 - N3 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 G B 211 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 A B 212 O4' - C4' - C3' ANGL. DEV. = -11.1 DEGREES
REMARK 500 1 A B 212 C5' - C4' - O4' ANGL. DEV. = 29.8 DEGREES
REMARK 500 1 A B 212 C1' - O4' - C4' ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 G B 213 C5' - C4' - O4' ANGL. DEV. = 18.6 DEGREES
REMARK 500 1 G B 213 C1' - O4' - C4' ANGL. DEV. = 10.1 DEGREES
REMARK 500 1 G B 213 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 G B 213 N1 - C2 - N3 ANGL. DEV. = 5.1 DEGREES
REMARK 500 1 G B 213 C5 - C6 - N1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 1 U B 214 C5' - C4' - O4' ANGL. DEV. = 25.3 DEGREES
REMARK 500 1 U B 214 C1' - O4' - C4' ANGL. DEV. = 12.4 DEGREES
REMARK 500 1 C B 216 C5' - C4' - O4' ANGL. DEV. = 26.5 DEGREES
REMARK 500 1 C B 216 C1' - O4' - C4' ANGL. DEV. = 11.5 DEGREES
REMARK 500 1 G B 217 C5' - C4' - O4' ANGL. DEV. = 21.2 DEGREES
REMARK 500 1 G B 217 C1' - O4' - C4' ANGL. DEV. = 12.3 DEGREES
REMARK 500 1 G B 217 C6 - N1 - C2 ANGL. DEV. = -6.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 1098 ANGLE DEVIATIONS.
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 1 THR A 12 123.85 82.59
REMARK 500 1 LYS A 20 171.30 -46.48
REMARK 500 1 ASN A 27 57.77 -151.41
REMARK 500 1 LYS A 34 117.77 -167.49
REMARK 500 1 GLU A 51 56.56 -109.84
REMARK 500 1 GLN A 53 49.13 38.33
REMARK 500 2 THR A 12 123.15 79.40
REMARK 500 2 LYS A 20 141.65 -38.29
REMARK 500 2 LYS A 26 -30.81 -39.45
REMARK 500 2 ASN A 27 57.41 -148.80
REMARK 500 2 ALA A 30 100.34 -39.67
REMARK 500 2 PRO A 31 49.70 -74.94
REMARK 500 2 ARG A 32 122.45 73.37
REMARK 500 2 LYS A 33 -58.63 170.60
REMARK 500 2 LYS A 34 126.92 62.36
REMARK 500 2 ARG A 52 161.02 60.18
REMARK 500 3 THR A 12 149.97 74.55
REMARK 500 3 PHE A 16 6.58 -69.61
REMARK 500 3 ASN A 17 -82.39 -116.41
REMARK 500 3 ASN A 27 56.85 -150.31
REMARK 500 3 PRO A 31 49.22 -75.02
REMARK 500 3 ARG A 32 144.17 -174.92
REMARK 500 3 THR A 50 21.62 -145.28
REMARK 500 3 ARG A 52 103.47 -42.79
REMARK 500 3 GLN A 53 59.99 -177.79
REMARK 500 3 ALA A 54 -61.05 -101.49
REMARK 500 4 THR A 12 123.18 83.82
REMARK 500 4 ASN A 27 57.58 -151.03
REMARK 500 4 LYS A 34 113.88 70.04
REMARK 500 4 GLU A 51 69.28 37.79
REMARK 500 4 GLN A 53 141.14 61.76
REMARK 500 5 THR A 12 141.15 84.59
REMARK 500 5 LYS A 20 175.93 -48.35
REMARK 500 5 ASN A 27 56.29 -148.31
REMARK 500 5 PRO A 31 49.48 -74.95
REMARK 500 5 LYS A 33 -70.46 -87.01
REMARK 500 6 GLN A 2 161.93 72.83
REMARK 500 6 THR A 12 140.75 161.60
REMARK 500 6 ASN A 17 -81.84 -118.87
REMARK 500 6 LYS A 20 177.71 -49.16
REMARK 500 6 ASN A 27 56.61 -150.52
REMARK 500 6 LYS A 33 48.93 -140.48
REMARK 500 6 LYS A 34 115.96 70.46
REMARK 500 7 THR A 12 145.26 84.81
REMARK 500 7 ASN A 17 -64.83 -107.64
REMARK 500 7 LYS A 20 173.59 -47.00
REMARK 500 7 ASN A 27 57.68 -150.38
REMARK 500 7 ALA A 30 151.91 -47.60
REMARK 500 7 PRO A 31 48.13 -74.98
REMARK 500 7 ARG A 32 -179.07 165.44
REMARK 500
REMARK 500 THIS ENTRY HAS 165 RAMACHANDRAN OUTLIERS.
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 128 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 18 SG 92.1
REMARK 620 3 HIS A 23 NE2 116.0 117.7
REMARK 620 4 CYS A 28 SG 127.6 115.3 90.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 149 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 85.5
REMARK 620 3 HIS A 44 NE2 99.6 108.7
REMARK 620 4 CYS A 49 SG 106.2 115.9 129.5
REMARK 620 N 1 2 3
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 128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 149
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A1T RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN COMPLEXED WITH STEM-LOOP SL3 FROM HIV-1
REMARK 900 RELATED ID: 1ESY RELATED DB: PDB
REMARK 900 THE UNBOUND STEM-LOOP SL2 FROM HIV-1
DBREF 1F6U A 1 55 UNP P35962 GAG_HV1Y2 378 432
DBREF 1F6U B 201 219 PDB 1F6U 1F6U 201 219
SEQADV 1F6U LYS A 3 UNP P35962 ARG 380 CONFLICT
SEQRES 1 B 19 CG1 G C G A C U G G U G A G
SEQRES 2 B 19 U A C G C C
SEQRES 1 A 56 MET GLN LYS GLY ASN PHE ARG ASN GLN ARG LYS THR VAL
SEQRES 2 A 56 LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS ILE ALA LYS
SEQRES 3 A 56 ASN CYS ARG ALA PRO ARG LYS LYS GLY CYS TRP LYS CYS
SEQRES 4 A 56 GLY LYS GLU GLY HIS GLN MET LYS ASP CYS THR GLU ARG
SEQRES 5 A 56 GLN ALA ASN NH2
MODRES 1F6U CG1 B 201 G
HET CG1 B 201 36
HET NH2 A 56 1
HET ZN A 128 1
HET ZN A 149 1
HETNAM CG1 5'-O-[(R)-HYDROXY(METHOXY)PHOSPHORYL]GUANOSINE
HETNAM NH2 AMINO GROUP
HETNAM ZN ZINC ION
FORMUL 1 CG1 C11 H16 N5 O8 P
FORMUL 2 NH2 H2 N
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 GLN A 2 THR A 12 5 11
HELIX 2 2 ILE A 24 CYS A 28 5 5
HELIX 3 3 GLN A 45 CYS A 49 5 5
SHEET 1 A 2 GLY A 35 CYS A 36 0
SHEET 2 A 2 LYS A 41 GLU A 42 -1 O LYS A 41 N CYS A 36
LINK O3' CG1 B 201 P G B 202 1555 1555 1.60
LINK C ASN A 55 N NH2 A 56 1555 1555 1.33
LINK SG CYS A 15 ZN ZN A 128 1555 1555 2.40
LINK SG CYS A 18 ZN ZN A 128 1555 1555 2.37
LINK NE2 HIS A 23 ZN ZN A 128 1555 1555 2.12
LINK SG CYS A 28 ZN ZN A 128 1555 1555 2.30
LINK SG CYS A 36 ZN ZN A 149 1555 1555 2.35
LINK SG CYS A 39 ZN ZN A 149 1555 1555 2.36
LINK NE2 HIS A 44 ZN ZN A 149 1555 1555 2.05
LINK SG CYS A 49 ZN ZN A 149 1555 1555 2.31
SITE 1 AC1 4 CYS A 15 CYS A 18 HIS A 23 CYS A 28
SITE 1 AC2 4 CYS A 36 CYS A 39 HIS A 44 CYS A 49
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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
MODEL 1
Complete list - b 16 2 Bytes